Affinage

PARD3

Partitioning defective 3 homolog · UniProt Q8TEW0

Length
1356 aa
Mass
151.4 kDa
Annotated
2026-06-10
100 papers in source corpus 55 papers cited in narrative 55 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 9/9 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

PARD3 (PAR-3/ASIP/Bazooka) is an evolutionarily conserved multi-PDZ scaffold protein that serves as the master organizer of cell polarity, partitioning membrane domains during asymmetric cell division, epithelial apicobasal polarization, and neuronal axon specification (PMID:8521491, PMID:9889099). It nucleates the core polarity machinery by directly binding atypical PKC (PKCλ/ζ) and PAR-6 through its PDZ domains, assembling the trimeric PAR-3/PAR-6/aPKC complex that depends mutually on each subunit for cortical localization (PMID:9763423, PMID:9834192, PMID:10934475). PAR-3 is targeted to apical junctional membranes by two cooperating mechanisms: oligomerization through its conserved N-terminal CR1 domain (PMID:12756256, PMID:12906794), and direct phosphoinositide lipid binding by its PDZ2 domain and conserved C-terminal region (PMID:18082612, PMID:20303268). There it is tethered to tight and adherens junctions through direct association with the transmembrane adhesion proteins JAM and nectin via its first PDZ domain (PMID:11447115, PMID:11489913, PMID:12515806). PAR-3 spatially restricts the Rac-GEFs Tiam1/STEF through direct binding, thereby controlling Rac activity and actin dynamics during tight junction assembly, dendritic spine morphogenesis, and cell migration (PMID:15723052, PMID:15723051, PMID:16474385), and it concatenates phosphoinositide signaling by binding the lipid phosphatase PTEN through its third PDZ domain (PMID:18082612, PMID:18550519). The complex is dynamically regulated by an antagonistic phosphorylation network: aPKC phosphorylates PAR-3 at Ser-827/833 to destabilize the interaction and tune localization (PMID:12390250, PMID:19401335), PAR-1/MARK phosphorylates conserved serines to generate 14-3-3 sites that exclude PAR-3 from lateral membranes (PMID:14675534), Rho-kinase phosphorylates Thr-833 to disrupt aPKC/PAR-6 binding and inhibit lipid association during migration and planar polarity (PMID:18267089, PMID:20833361), and these are counterbalanced by PP1α and PP2A dephosphorylation (PMID:18641122, PMID:19531360). PAR-3 abundance is further controlled by Siah E3 ligase-mediated proteasomal degradation (PMID:21109632). Through cytoplasmic promotion of PP1A–LATS1 interaction it inactivates LATS1 and activates TAZ, linking PAR-3 to Hippo/YAP-TAZ signaling and the control of neural progenitor division mode in vivo (PMID:26116754, PMID:29899142). PAR-3 also directs neuronal polarity through KIF3 motor-mediated transport to the axon tip (PMID:15048131) and Schwann cell myelination via a Par-3/p75NTR complex (PMID:17082460).

Mechanistic history

Synthesis pass · year-by-year structured walk · 17 steps
  1. 1995 High

    Established PAR-3 as an asymmetrically localized determinant of embryonic polarity, defining the founding member of the PAR polarity system and its epistatic relationships with other par genes.

    Evidence Immunolocalization and genetic epistasis with par mutants in C. elegans zygotes

    PMID:7713417 PMID:8521491

    Open questions at the time
    • No molecular function or binding partners identified
    • Mechanism of asymmetric localization unknown
  2. 1998 High

    Identified the conserved PAR-3/aPKC interaction across species, revealing PAR-3 as a PDZ scaffold that physically couples a kinase to the polarity machinery and tethers it to tight junctions.

    Evidence Co-IP and immunoelectron microscopy in mammalian epithelia; in vitro binding and RNAi in C. elegans; loss-of-function genetics in Drosophila

    PMID:9716526 PMID:9763423 PMID:9889099

    Open questions at the time
    • Stoichiometry of the complex not resolved
    • Functional consequence of phosphorylation not defined
  3. 1999 High

    Defined the trimeric PAR-3/PAR-6/aPKC complex and linked it to spindle orientation determinants, showing PAR-3 organizes downstream fate factors during asymmetric division.

    Evidence In vitro binding, co-IP, and genetic null analysis in C. elegans and Drosophila neuroblasts (Inscuteable/Staufen)

    PMID:10591216 PMID:10591217 PMID:9834192

    Open questions at the time
    • How PAR-3 selects apical versus basal targets unknown
  4. 2000 High

    Showed PAR-3 acts as both substrate and inhibitor of aPKC and that PAR-6 bridges Cdc42/Rac1 to the complex, establishing PAR-3 as a signaling scaffold rather than a passive adaptor.

    Evidence Co-IP, PDZ domain mapping, and in vitro kinase assays of mammalian mPAR-3/mPAR-6

    PMID:10934475

    Open questions at the time
    • aPKC phosphorylation sites on PAR-3 not yet mapped
    • Mechanism of GTPase regulation unresolved
  5. 2001 High

    Determined how the complex is anchored at junctions, showing PAR-3 directly binds JAM C-termini while ZO-1 links JAM to claudin strands, providing a structural route for tight junction recruitment.

    Evidence In vitro binding, reciprocal co-IP, and overexpression with localization readout in fibroblasts/CHO cells

    PMID:11447115 PMID:11489913

    Open questions at the time
    • Whether JAM binding is sufficient for in vivo recruitment unclear
  6. 2002 High

    Identified Ser-827 as the aPKC phosphorylation site whose modification destabilizes the PAR-3–aPKC interaction, introducing dynamic regulation of complex assembly during junction formation.

    Evidence In vitro kinase assay, phospho-specific antibody, and S827A mutant rescue in MDCK cells

    PMID:12045219 PMID:12390250

    Open questions at the time
    • Counteracting phosphatase not identified
    • Other phosphosites unknown
  7. 2003 High

    Resolved PAR-3 cortical targeting via CR1-mediated oligomerization and identified PAR-1 phosphorylation generating 14-3-3 sites that exclude PAR-3 from lateral membranes, establishing the kinase-driven spatial code for membrane domain restriction.

    Evidence Oligomerization assays, domain deletion in MDCK, in vitro kinase assay and genetic epistasis in Drosophila; nectin/JAM binding by PDZ1

    PMID:12510193 PMID:12515806 PMID:12756256 PMID:12906794 PMID:12953056 PMID:14675534

    Open questions at the time
    • How oligomerization and phosphorylation are coordinated temporally unclear
    • Lipid-binding contribution not yet defined
  8. 2004 High

    Linked PAR-3 to directional transport by showing KIF3A motor binding delivers PAR-3/aPKC to the neurite tip, extending the polarity scaffold to neuronal axon specification.

    Evidence Co-IP and dominant-negative fragment expression in hippocampal neurons

    PMID:15048131

    Open questions at the time
    • Cargo selectivity of transport not defined
  9. 2005 High

    Established PAR-3 as a spatial regulator of Rac through direct binding and restriction of the Rac-GEFs Tiam1/STEF, connecting the polarity complex to actin dynamics and tight junction assembly.

    Evidence Direct binding, siRNA knockdown, dominant-negative Rac rescue, and Rac activity assays in epithelia and neurons; PTEN binding and genetics in Drosophila

    PMID:15723051 PMID:15723052 PMID:15743877

    Open questions at the time
    • Whether PAR-3 activates or sequesters Tiam1 context-dependent and unresolved
  10. 2006 High

    Expanded PAR-3 targets to LIMK2/cofilin actin regulation, p75NTR-dependent Schwann cell myelination, and dendritic spine morphogenesis, demonstrating tissue-specific deployment of the scaffold.

    Evidence In vitro kinase inhibition, direct binding, siRNA rescue in epithelia and neurons, and myelination assays in Schwann cells

    PMID:16474385 PMID:16505165 PMID:16717194 PMID:17082460

    Open questions at the time
    • How PAR-3 selects different effectors across tissues not established
  11. 2007 High

    Defined the lipid-integration function of PAR-3, showing PDZ2 binds phosphoinositides while PDZ3 binds PTEN, and linked PAR-3/aPKC to Numb phosphorylation and integrin endocytosis during migration.

    Evidence Biochemical lipid-binding, structural characterization, cell polarization assays, and endocytosis/migration assays

    PMID:17606991 PMID:17609107 PMID:18082612

    Open questions at the time
    • How lipid and protein binding are spatially combined at junctions not fully resolved
  12. 2008 High

    Mapped the antagonistic phosphorylation network controlling PAR-3, identifying Rho-kinase phosphorylation at Thr-833 that disrupts the complex and PP1α dephosphorylation that maintains it, plus the structural basis of PTEN recruitment.

    Evidence In vitro kinase assays, mutagenesis, quantitative mass spectrometry of phosphosites, phosphatase assays, and PDZ3-PTEN crystal structure

    PMID:18267089 PMID:18550519 PMID:18641122

    Open questions at the time
    • Integration of multiple kinase/phosphatase inputs into a single localization decision not modeled
  13. 2009 High

    Demonstrated that the PAR-3–aPKC interaction is essential for apical domain development but dispensable for tight junction maturation, separating distinct scaffold functions.

    Evidence siRNA knockdown with separation-of-function mutant rescue in 2D/3D MDCK culture; exocyst/RalA association in neurons

    PMID:19383721 PMID:19401335

    Open questions at the time
    • Mechanism of apical cargo delivery downstream of the complex unclear
    • Exocyst link rests on single-method co-IP
  14. 2010 High

    Consolidated the regulatory logic of PAR-3 localization through PP2A counter-balancing of PAR-1, Rho-kinase inhibition of lipid binding, Crumbs/Stardust competition, Siah-mediated degradation, and Sirt2 deacetylation controlling aPKC activity.

    Evidence Phospho-mutant and genetic epistasis in Drosophila, in vitro lipid-binding, ubiquitination assays, transgenic mouse deacetylation in Schwann cells, and live imaging in C. elegans

    PMID:19531360 PMID:20303268 PMID:20431121 PMID:20434988 PMID:20619750 PMID:20819933 PMID:20833361 PMID:21109632 PMID:21949390

    Open questions at the time
    • Relative contributions of degradation versus phosphorylation to localization not quantified
  15. 2012 High

    Provided the structural basis for aPKC substrate recognition of PAR-3, defining the kinase groove and consensus sequence that governs phosphorylation-dependent complex regulation.

    Evidence X-ray crystallography of PKCι–PAR-3 peptide complex at 2.4 Å with mutagenesis and in vitro kinase assays

    PMID:22579248

    Open questions at the time
    • Structure of full-length PAR-3 scaffold not determined
  16. 2015 Medium

    Connected PAR-3 to Hippo signaling, showing cytoplasmic PARD3 promotes PP1A–LATS1 association to inactivate LATS1 and activate TAZ, defining a junction-independent signaling role.

    Evidence Co-IP of the ternary complex, phosphorylation status measurement, and domain separation experiments; centrosome orientation and Girdin transcriptional roles

    PMID:25793442 PMID:25977476 PMID:26116754

    Open questions at the time
    • Single-lab co-IP without reciprocal in vivo validation
    • How cytoplasmic versus junctional pools are partitioned unclear
  17. 2018 High

    Validated the PARD3–Hippo axis in vivo, showing PARD3 acts upstream of YAP/TAZ to control radial glial division mode and cortical development, and extended polarity control to flow-dependent endothelial planar polarity via GSK3β.

    Evidence In vivo conditional knockout with YAP/TAZ epistasis and live imaging in mouse cortex; co-IP and flow assays in endothelial cells

    PMID:29899142 PMID:30018153

    Open questions at the time
    • Direct biochemical link between junctional PARD3 and YAP/TAZ regulation not fully reconstituted
    • Endothelial findings rest on single-lab functional assays

Open questions

Synthesis pass · forward-looking unresolved questions
  • How the multiple kinase, phosphatase, lipid, adhesion, and degradation inputs are integrated in real time to produce a single sharp polarity boundary, and how PAR-3 partitions between junctional and cytoplasmic signaling pools, remain unresolved.
  • No quantitative model integrating competing inputs
  • Full-length PAR-3 structure unknown
  • Mechanism partitioning junctional polarity from cytoplasmic Hippo signaling undefined

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0060090 molecular adaptor activity 4 GO:0098772 molecular function regulator activity 4 GO:0008289 lipid binding 3 GO:0098631 cell adhesion mediator activity 3
Localization
GO:0005886 plasma membrane 4 GO:0005829 cytosol 2 GO:0005856 cytoskeleton 2
Pathway
R-HSA-1266738 Developmental Biology 4 R-HSA-1500931 Cell-Cell communication 4 R-HSA-1640170 Cell Cycle 4 R-HSA-162582 Signal Transduction 3
Partners
F11RKIF3ALIMK2PARD6PRKCIPTENPVRL1TIAM1
Complex memberships
PAR-3/PAR-6/aPKC polarity complex

Evidence

Reading pass · 55 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1995 PAR-3 protein is asymmetrically distributed at the periphery of the zygote and asymmetrically dividing blastomeres in C. elegans. PAR-3 is required for proper localization of PAR-1, and par-2 activity is required for proper localization of PAR-3, establishing a mutual epistatic relationship between PAR-2, PAR-3, and PAR-1 in controlling embryonic polarity and cleavage spindle orientation. Immunolocalization, genetic epistasis analysis using par mutants Cell High 8521491
1995 par-3 and par-2 act in concert during the first cell cycle to affect asymmetric modification of the cytoskeleton; par-3 is epistatic to par-2 in controlling spindle orientation in C. elegans embryos. Genetic epistasis analysis, temperature-shift experiments with double mutants Genetics High 7713417
1996 par-6 acts upstream of par-3 by localizing or maintaining the PAR-3 protein at the cell periphery in C. elegans embryos; loss-of-function par-6 mutations act as dominant bypass suppressors of par-2 loss-of-function mutations. Genetic epistasis, immunolocalization of PAR-3 in par-6 mutant embryos Development High 8898226
1998 ASIP (mammalian PAR-3 homolog) directly binds to atypical PKC isoforms (PKCλ/PKCζ) via PDZ domains and colocalizes with PKCλ to the tight junction complex in epithelial cells, suggesting a conserved role for the PAR-3/aPKC complex in cell polarity. Co-immunoprecipitation, immunoelectron microscopy, sequence analysis The Journal of cell biology High 9763423
1998 In C. elegans, aPKC (PKC-3) directly interacts with PAR-3, co-localizes with PAR-3 to the anterior periphery of asymmetrically dividing cells, and shows mutual dependence on PAR-3 (and par-6) for correct localization. PKC-3 depletion by RNAi causes Par-like polarity phenotypes. In vitro binding assay, RNA interference, immunolocalization Development High 9716526
1998 Drosophila Bazooka (PAR-3 ortholog) is required for establishment of apico-basal polarity in epithelia and neuroblasts; Baz protein is restricted to the apical cortical cytoplasm of epithelial cells and neuroblasts, and bazooka mutants show defective spindle orientation. Loss-of-function genetics, immunolocalization Current biology High 9889099
1999 Bazooka/PAR-3 directly binds Inscuteable in vitro and in vivo, forming a complex that also contains Staufen; Bazooka is required for asymmetric apical localization of Inscuteable in Drosophila neuroblasts, which in turn controls spindle orientation and Numb/Miranda asymmetric localization. In vitro binding assay, in vivo co-immunoprecipitation, genetic loss-of-function (maternal/zygotic null) Nature High 10591216 10591217
1999 PAR-6 is a PDZ-domain protein that colocalizes with PAR-3 in C. elegans embryos; PAR-3 and PKC-3 activity are required for peripheral localization of PAR-6, supporting a trimeric PAR-3/PAR-6/PKC-3 complex. Molecular cloning, immunolocalization, genetic analysis Development High 9834192
2000 Mammalian mPAR-3 and mPAR-6 associate through their PDZ domains. mPAR-6 binds Cdc42/Rac1 GTPases. Both mPAR-3 and mPAR-6 bind independently to atypical PKC isoforms. In vitro, mPAR-3 acts as both a substrate and an inhibitor of aPKC, suggesting a scaffolding function coordinating signaling proteins for cell polarity. Co-immunoprecipitation, in vitro kinase assay, PDZ domain binding assays Nature cell biology High 10934475
2000 Drosophila aPKC (DaPKC) directly binds to Bazooka/PAR-3, and both proteins are mutually dependent for correct apical localization. Loss-of-function of DaPKC causes loss of apico-basal polarity, multilayering of epithelia, mislocalization of Inscuteable, and abnormal spindle orientation in neuroblasts. Direct binding assay, genetic loss-of-function, immunolocalization The Journal of cell biology High 10995441
2001 ASIP/PAR-3 directly associates with junctional adhesion molecule (JAM) in vitro and in vivo through its PDZ domains. Overexpression of truncated JAM lacking the extracellular domain disrupts ASIP/PAR-3 localization at intercellular junctions, suggesting JAM tethers the PAR-3/aPKC complex to tight junctions. In vitro binding assay, co-immunoprecipitation, overexpression studies in fibroblasts and CHO cells The EMBO journal High 11447115
2001 ZO-1 directly binds JAM at its PDZ3 domain, while PAR-3 directly binds the C-terminus of JAM (but not claudins). A model is proposed where JAM aggregates tethered to claudin-based strands through ZO-1 recruit PAR-3 to tight junctions. In vitro binding assays, immunofluorescence, immunoreplica electron microscopy The Journal of cell biology High 11489913
2002 aPKC preferentially phosphorylates PAR-3 at serine-827 in vitro and in vivo; this phosphorylation reduces the stability of the PAR-3–aPKC interaction. Overexpression of PAR-3 S827A (non-phosphorylatable) causes defects in cell-cell contact-induced cell polarization of MDCK cells, similar to dominant-negative aPKC. In vitro kinase assay, phospho-specific antibody, MDCK overexpression studies Genes to cells High 12390250
2002 Overexpression of ASIP/PAR-3, but not a deletion mutant lacking the aPKC-binding sequence, promotes cell-cell contact-induced tight junction formation in MDCK cells. PAR-3 Ser827 is phosphorylated at the most apical tip of cell-cell contacts during initial tight junction formation, implicating PAR-3/aPKC interaction in this process. Inducible overexpression, transepithelial resistance measurement, occludin insolubilization assay, immunofluorescence Journal of cell science High 12045219
2003 PAR-3 directly binds nectin-1 and nectin-3 (but not nectin-2) through its first PDZ domain at neuroepithelial adherens junctions; PAR-3 and nectin-1/-3 co-immunoprecipitate from embryonic mouse brain and recombinant proteins bind stoichiometrically. Co-immunoprecipitation from mouse brain, recombinant protein binding assay, PDZ domain mapping The Journal of biological chemistry High 12515806
2003 PAR-1 phosphorylates Bazooka/PAR-3 on two conserved serines (generating 14-3-3 binding sites), which inhibits Bazooka oligomerization and binding to aPKC. This excludes Bazooka from lateral membranes in epithelia; a Bazooka lacking PAR-1 phosphorylation/14-3-3 binding sites forms ectopic lateral complexes, disrupting polarity. In vitro kinase assay, genetic epistasis, site-directed mutagenesis, immunolocalization Cell High 14675534
2003 The conserved N-terminal domain CR1 of PAR-3 mediates self-association/oligomerization in vitro and in vivo. CR1 deletion disrupts localization of aPKC and PAR-6 as well as PAR-3 and delays formation of functional tight junctions. Sequence 937-1024 is also required for recruitment to the apical side of cell-cell contact. In vitro and in vivo oligomerization assays, MDCK overexpression, transepithelial resistance The Journal of biological chemistry High 12756256
2003 Bazooka CR1 domain mediates oligomerization in vitro and in vivo (predicted by structural fold comparison to a bacterial oligomerization domain); deletion of CR1 disrupts BAZ localization in epithelial cells and germline and strongly impairs BAZ function in epithelial polarity. Sequence-structure comparison (FUGUE), biochemical oligomerization assay, Drosophila genetics Current biology High 12906794
2003 JAM-2 and JAM-3 directly associate with PAR-3 through its first PDZ domain; junctional localization of JAM-2 is regulated by serine phosphorylation, and JAM-2 clustering at cell-cell contacts recruits endogenous PAR-3 and ZO-1. In vitro binding assay, co-immunoprecipitation, ectopic expression in CHO cells Journal of cell science High 12953056
2003 Genetic epistasis in Drosophila shows bazooka functions redundantly with crumbs/stardust to support apical polarity at mid-to-late embryogenesis; crb and lgl pathways function competitively to define apical and basolateral surfaces. Drosophila genetic epistasis, double and triple mutant analysis Nature cell biology High 12510193
2004 PAR-3 directly interacts with KIF3A (a plus-end-directed microtubule motor), and aPKC can associate with KIF3A through PAR-3. Expression of dominant-negative PAR-3 and KIF3A fragments that disrupt PAR-3–KIF3A binding inhibited accumulation of PAR-3 and aPKC at the neurite tip and abolished neuronal polarity in cultured hippocampal neurons. Co-immunoprecipitation, dominant-negative fragment expression, immunofluorescence in hippocampal neurons Nature cell biology High 15048131
2005 Par-3 depletion in mammalian epithelial cells profoundly disrupts tight junction assembly; Rac is constitutively activated in cells lacking Par-3. Par-3 directly binds the Rac-GEF Tiam1 through its C-terminal region; knockdown of Tiam1 enhances tight junction formation in Par-3-depleted cells, revealing Par-3 as a spatial regulator of Rac activity via Tiam1. siRNA knockdown, dominant-negative Rac rescue, direct binding assay, tight junction formation assay Nature cell biology High 15723052
2005 PAR-3 directly interacts with STEF/Tiam1 (Rac-specific GEFs) and forms a complex with PAR-3–aPKC–PAR-6–Cdc42-GTP. Disruption of PAR-3–STEF binding inhibits Cdc42-induced lamellipodia. PAR-3 is required for Cdc42-induced Rac activation. In hippocampal neurons, STEF accumulates at the axon tip colocalizing with PAR-3, suggesting a Cdc42–PAR-6–PAR-3–STEF/Tiam1–Rac signaling cascade in neuronal polarity. Co-immunoprecipitation, dominant-negative fragment expression, Rac GTPase activity assay, immunofluorescence Nature cell biology High 15723051
2005 Drosophila Bazooka directly binds the lipid phosphatase PTEN in vitro and in vivo; PTEN colocalizes with Baz in the apical cortex of epithelia and neuroblasts. Pten mutant phenotypes include defects in posterior germ plasm determinant localization and actin-dependent nuclear movements. In vitro binding assay, co-immunoprecipitation, genetic loss-of-function Development High 15743877
2006 Par-3 directly binds p75 neurotrophin receptor (p75NTR) and recruits it to the axon-glial junction in Schwann cells; disruption of Par-3 localization by overexpression or knockdown inhibits myelination, defining a Par-3/p75NTR complex necessary for Schwann cell myelination. Direct binding assay, co-immunoprecipitation, overexpression and knockdown in Schwann cells, myelination assay Science High 17082460
2006 Par-3 depletion elevates phosphorylated cofilin levels; Par-3 directly binds LIMK2 (but not LIMK1) and inhibits LIMK2 kinase activity in vitro. A non-phosphorylatable cofilin mutant partially rescues tight junction assembly in Par-3-depleted cells. This identifies LIMK2 as a novel Par-3 target linking actin dynamics to tight junction assembly. siRNA knockdown, direct binding assay, in vitro kinase assay, rescue experiments The Journal of cell biology High 16505165
2006 PAR-3 is necessary for normal dendritic spine development; depletion causes multiple filopodia/lamellipodia-like protrusions (similar to activated Rac). PAR-3 spatially restricts TIAM1 to dendritic spines by direct binding, thereby modulating Rac-GTP levels during spine morphogenesis. siRNA knockdown, direct binding assay, live imaging, Rac activity assay in hippocampal neurons Nature cell biology High 16474385
2006 MARK2/PAR-1 functions downstream of the PAR-3/PAR-6/aPKC complex in hippocampal neuron polarity; aPKC phosphorylates MARK2 at T595, and an MARK2 mutant not responsive to aPKC is not rescued by the PAR-3/PAR-6/aPKC complex. Genetic epistasis places MARK2 downstream of aPKC in neuronal polarization. siRNA knockdown, ectopic expression, epistasis analysis, phosphorylation assays in hippocampal neurons Proceedings of the National Academy of Sciences High 16717194
2007 PAR-3 directly interacts with KIF3A-containing KIF3 complex; the PAR-3/KIF3 association mediates transport of PAR-3 to the distal tip of the axon. Disruption of this interaction impairs axon formation and neuronal polarity in hippocampal neurons. Co-immunoprecipitation, dominant-negative expression, immunofluorescence Nature cell biology High 15048131
2007 Numb binds to PAR-3 and is phosphorylated by aPKC, causing release from clathrin-coated structures; PAR-3/aPKC-mediated polarized phosphorylation of Numb contributes to directional integrin endocytosis and cell migration toward integrin substrates. RNAi, co-immunoprecipitation, integrin endocytosis assay, cell migration assay Developmental cell High 17609107
2007 The second PDZ domain of Par-3 binds phosphatidylinositol lipid membranes with high affinity; Par-3 PDZ2 membrane binding capacity is critical for epithelial cell polarization. The third PDZ domain of Par-3 directly binds PTEN. Concatenation of PIP-binding PDZ2 and PTEN-binding PDZ3 enables Par-3 to integrate phosphoinositide signaling. Biochemical lipid-binding assays, structural characterization, cell polarization assay Molecular cell High 18082612
2007 Par-3 cooperates with afadin in forming adherens and tight junctions; Par-3 promotes the association of afadin with nectin, while afadin is not required for Par-3–nectin association. Par-3 and afadin cooperatively regulate AJ and TJ formation downstream of nectin-based cell-cell adhesion. Par-3 knockdown in MDCK cells, co-immunoprecipitation, immunofluorescence Journal of cell science Medium 17606991
2008 Rho-kinase/ROCK phosphorylates PAR-3 at Thr833, disrupting its interaction with aPKC and PAR-6 but not with Tiam2/STEF. Phospho-PAR-3 is observed in the leading edge of migrating cells; PAR-3 knockdown impairs cell migration and PAR-3-mediated Rac1 activation, which are recovered with siRNA-resistant PAR-3 but not with a phospho-mimic mutant. In vitro kinase assay, site-directed mutagenesis, siRNA knockdown, rescue experiments, Rac1 activity assay Developmental cell High 18267089
2008 Protein phosphatase PP1 (predominantly PPα isoform) binds Par-3 and retains phosphatase activity; PP1α specifically dephosphorylates Par-3 at Ser-144, Ser-824, and Ser-885 (identified by quantitative mass spectrometry/MRM). PP1α regulates 14-3-3 and aPKCζ binding to Par-3. Catalytically inactive PP1α severely delays tight junction formation in MDCK cells. Co-immunoprecipitation, quantitative mass spectrometry (MRM), phosphatase activity assay, tight junction formation assay Proceedings of the National Academy of Sciences High 18641122
2008 Crystal structures of Par-3 PDZ3 in free and PTEN-peptide-bound forms reveal that Par-3 PDZ3 binds PTEN via two discrete sites: a canonical PDZ-ligand site and a distal charge-charge interaction site. Par-3 PDZ3-PTEN binding is required for enrichment of PTEN at junctional membranes of MDCK cells, and junctional PTEN is specifically required for cell polarization. X-ray crystallography, mutagenesis, MDCK cell polarization assay The Journal of biological chemistry High 18550519
2009 PAR-3 knockdown in MDCK cells retards apical protein delivery; PAR-3 S827/829A mutant (unable to interact with aPKC) fails to rescue PAR-3 knockdown defects in apical membrane development, demonstrating that formation of the PAR-3–aPKC–PAR-6 complex is essential for apical domain development. Tight junction maturation does not require the aPKC–PAR-3 interaction. siRNA knockdown, point mutant rescue, 2D and 3D MDCK culture, immunofluorescence Journal of cell science High 19401335
2009 PP2A binds Baz/PAR-3 via its structural A subunit and dephosphorylates Baz at the conserved serine 1085 (PAR-1 phosphorylation site), antagonizing PAR-1 kinase activity. Loss of PP2A function in Drosophila neuroblasts causes complete reversal of polarity; overexpression of PAR-1 or Baz or 14-3-3 mutation causes the same phenotype, placing PP2A activity in the PAR-1/Baz phosphorylation balance determining NB polarity. Co-immunoprecipitation, phospho-specific antibodies, genetic epistasis in Drosophila Developmental cell High 19531360
2009 RalA-regulated association between the exocyst complex and PAR-3 increases during early stages of neuronal polarization. Depletion of Sec6, Sec8, or Exo84 exocyst subunits leads to unpolarized neurons, and constitutively active RalA unable to bind the exocyst has no effect on neuronal polarization. Co-immunoprecipitation, siRNA knockdown, overexpression in cultured neurons Journal of cell science Medium 19383721
2010 aPKC phosphorylation of Bazooka disrupts the Baz/aPKC interaction and excludes Baz from the apical domain in Drosophila epithelia. Additionally, the Crumbs complex prevents Baz/PAR-6 interaction in epithelia. Without Crumbs or aPKC phosphorylation, mislocalized Baz recruits adherens junction components apically, expanding the lateral domain at the expense of the apical domain. Phospho-mutant analysis, genetic epistasis, immunolocalization in Drosophila epithelia Cell High 20434988
2010 Rho-kinase is required for planar polarized distribution of Bazooka/PAR-3 in Drosophila embryo intercalating cells; activated Rho-kinase is sufficient to exclude Baz from the cortex. Rho-kinase can phosphorylate the Baz C-terminal domain and inhibit its interaction with phosphoinositide membrane lipids, providing a mechanism for regulating Baz cortical association. Genetic loss-of-function, constitutively active expression, in vitro phosphorylation, lipid-binding assays Developmental cell High 20833361
2010 The conserved C-terminal region of Bazooka/PAR-3 (not PDZ domains) binds phosphoinositide lipids directly and mediates cortical localization of Baz by direct plasma membrane interaction in multiple Drosophila cell types. PDZ domains are dispensable for correct Baz localization. Structure-function analysis, lipid-binding assay, Drosophila genetics in multiple cell types Current biology High 20303268
2010 ASPP2 directly binds Par-3, and the junctional localization of ASPP2 and Par-3 is interdependent. ASPP2 controls apical/junctional Par-3 localization without affecting Par-3 expression or Par-3/aPKCλ binding; disruption leads to neuroblastic rosette formation and impaired neural progenitor proliferation in vivo. Co-immunoprecipitation, in vivo mouse CNS analysis, immunofluorescence Developmental cell Medium 20619750
2010 Sirt2 deacetylates Par-3 in Schwann cells; deacetylation of Par-3 by Sirt2 decreases the activity of aPKC, thereby regulating myelin formation. Transgenic mice lacking or overexpressing Sirt2 specifically in Schwann cells show delays in myelin formation. In vivo genetic mouse model, deacetylation assay, aPKC activity assay Proceedings of the National Academy of Sciences High 21949390
2010 Siah E3 ubiquitin ligase promotes proteasomal degradation of Pard3A in cerebellar granule neurons. Pard3A gain of function and Siah loss of function induce precocious radial migration. Pard3A promotes adhesive interactions for germinal zone exit by recruiting epithelial tight junction adhesion molecule C to the neuronal cell surface. In vivo gain-of-function and loss-of-function, ubiquitin ligase assay, time-lapse imaging, cell surface recruitment assay Science High 21109632
2010 PAR-3 mediates the initial clustering of E-cadherin and other adherens junction/polarity proteins into cortical foci that then travel and accumulate apically during C. elegans intestinal epithelial cell polarization. PAR-3 is required to assemble E-cadherin into foci and for foci to accumulate at the apical surface. Targeted protein degradation strategy in C. elegans, live imaging Development High 20431121
2010 Baz directly interacts with Stardust (Sdt) via Sdt's PDZ domain and the aPKC phosphorylation site region of Baz; aPKC phosphorylation of Baz causes dissociation of the Baz-Sdt complex. Non-phosphorylatable Baz overexpression blocks Sdt dissociation and causes crb/sdt-like polarity phenotypes. In vitro binding assay, phospho-mutant analysis, Drosophila genetics The Journal of cell biology High 20819933
2012 Crystal structure of PKCι in complex with a Par-3 substrate peptide at 2.4 Å reveals that the Par-3 peptide binds an elongated groove formed by N- and C-lobes of the kinase domain. Structural analysis together with mutagenesis identifies a hydrophobic pocket unique to aPKC isozymes and a consensus aPKC substrate recognition sequence. The pseudosubstrate sequence of PKCι directly binds and inhibits kinase activity similarly to the Par-3 peptide. X-ray crystallography, mutagenesis, in vitro kinase assay Structure High 22579248
2013 Dynamic microtubules positioned along the dorso-ventral axis inhibit RhoGEF2, reducing Rho-kinase membrane recruitment and increasing a mobile E-cadherin pool complexed with Bazooka/PAR-3 (measured by FRAP). This mobile E-cadherin-Bazooka complex prevents multicellular rosette formation and cell motility across segment borders. FRAP, genetic analysis, immunofluorescence in Drosophila embryos The Journal of cell biology Medium 23751496
2013 Loss of Par3/Bazooka from cell-cell junctions at epithelial edges during Drosophila wound healing results in localized PIP3 accumulation, which promotes actin protrusion formation; depleting PIP3 causes defective epithelial closure. This establishes a direct molecular link between Par3 loss, PI3K signaling, and actin protrusion. Drosophila genetics, wound healing assay, dorsal closure assay, PIP3 biosensor imaging Development Medium 23318638
2014 PI(4,5)P2, produced by the PI4P5K SKTL, is required to maintain apical PAR-3/Bazooka localization at the plasma membrane; reduction of PI(4,5)P2 causes loss of apical Baz, disassembly of adherens junctions, actin reorganization, and apical constriction similar to EMT. Loss of polarized PAR-3 distribution is sufficient to induce these cell shape changes. PI4P5K genetic inactivation, PI(4,5)P2 reporters, immunofluorescence, Drosophila follicular epithelium Current biology Medium 24768049
2015 PARD3 promotes interaction between PP1A and LATS1, inducing LATS1 dephosphorylation and inactivation, leading to dephosphorylation and activation of TAZ. Cytoplasmic (but not tight junction complex-associated) PARD3 is responsible for TAZ regulation, providing a mechanism by which PARD3 modulates Hippo pathway signaling. Co-immunoprecipitation, phosphorylation assays, domain separation experiments EMBO reports Medium 26116754
2015 Bazooka provides a cortical platform for correct centrosome orientation in Drosophila male germline stem cells; Baz-centrosome association is the key event monitored by the centrosome orientation checkpoint (COC) to ensure productive asymmetric cell division. Drosophila genetics, live imaging, centrosome orientation assay eLife Medium 25793442
2015 PAR-3 regulates the protein expression of Girdin (a GEF for Gαi subunits) at the transcriptional level by cooperating with the AP-2 transcription factor. PAR-3 physically interacts with Girdin; Girdin together with Gαi3 controls tight junction formation, apical domain development, and actin organization downstream of PAR-3. siRNA knockdown, co-immunoprecipitation, transcriptional reporter assay, MDCK cell polarity assay Journal of cell science Medium 25977476
2018 PARD3-deficient radial glial progenitors (RGPs) exhibit stage-dependent abnormal switches in division mode; simultaneous removal of YAP and TAZ suppresses cortical enlargement and heterotopia formation in PARD3-null cortex. This places PARD3 upstream of HIPPO pathway effectors in controlling RGP division mode and cortical development. In vivo conditional knockout in mouse cortex, epistasis with YAP/TAZ double knockout, live imaging Genes & development High 29899142
2018 PAR-3 acts as an essential gatekeeper of GSK3β activity in response to laminar blood flow in endothelial cells; flow-induced spatial distribution of PAR-3/aPKCλ and aPKCλ/GSK3β complexes controls local GSK3β activity and regulates endothelial planar polarity. PAR-3/aPKCλ spatial information is required for flow-dependent polarity but not for flow-induced anti-inflammatory response. Co-immunoprecipitation, kinase activity assays, endothelial cell flow experiments, siRNA knockdown EMBO reports Medium 30018153

Source papers

Stage 0 corpus · 100 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2000 A mammalian PAR-3-PAR-6 complex implicated in Cdc42/Rac1 and aPKC signalling and cell polarity. Nature cell biology 636 10934475
1998 An atypical PKC directly associates and colocalizes at the epithelial tight junction with ASIP, a mammalian homologue of Caenorhabditis elegans polarity protein PAR-3. The Journal of cell biology 424 9763423
2000 Drosophila atypical protein kinase C associates with Bazooka and controls polarity of epithelia and neuroblasts. The Journal of cell biology 397 10995441
2005 Par-3 controls tight junction assembly through the Rac exchange factor Tiam1. Nature cell biology 382 15723052
1999 Bazooka provides an apical cue for Inscuteable localization in Drosophila neuroblasts. Nature 381 10591216
1995 Asymmetrically distributed PAR-3 protein contributes to cell polarity and spindle alignment in early C. elegans embryos. Cell 368 8521491
2003 Drosophila PAR-1 and 14-3-3 inhibit Bazooka/PAR-3 to establish complementary cortical domains in polarized cells. Cell 345 14675534
1996 armadillo, bazooka, and stardust are critical for early stages in formation of the zonula adherens and maintenance of the polarized blastoderm epithelium in Drosophila. The Journal of cell biology 330 8698811
1998 Atypical protein kinase C cooperates with PAR-3 to establish embryonic polarity in Caenorhabditis elegans. Development (Cambridge, England) 321 9716526
1999 Bazooka recruits Inscuteable to orient asymmetric cell divisions in Drosophila neuroblasts. Nature 314 10591217
2005 PAR-6-PAR-3 mediates Cdc42-induced Rac activation through the Rac GEFs STEF/Tiam1. Nature cell biology 313 15723051
2001 The cell polarity protein ASIP/PAR-3 directly associates with junctional adhesion molecule (JAM). The EMBO journal 310 11447115
2001 Junctional adhesion molecule (JAM) binds to PAR-3: a possible mechanism for the recruitment of PAR-3 to tight junctions. The Journal of cell biology 304 11489913
2003 Interactions between the crumbs, lethal giant larvae and bazooka pathways in epithelial polarization. Nature cell biology 301 12510193
2007 Numb controls integrin endocytosis for directional cell migration with aPKC and PAR-3. Developmental cell 293 17609107
2003 Mammalian Lgl forms a protein complex with PAR-6 and aPKC independently of PAR-3 to regulate epithelial cell polarity. Current biology : CB 290 12725730
1999 PAR-6 is a conserved PDZ domain-containing protein that colocalizes with PAR-3 in Caenorhabditis elegans embryos. Development (Cambridge, England) 252 9834192
2004 Role of the PAR-3-KIF3 complex in the establishment of neuronal polarity. Nature cell biology 233 15048131
1996 par-6, a gene involved in the establishment of asymmetry in early C. elegans embryos, mediates the asymmetric localization of PAR-3. Development (Cambridge, England) 229 8898226
2010 aPKC phosphorylation of Bazooka defines the apical/lateral border in Drosophila epithelial cells. Cell 226 20434988
2010 Rho-kinase directs Bazooka/Par-3 planar polarity during Drosophila axis elongation. Developmental cell 214 20833361
2003 The junctional adhesion molecule (JAM) family members JAM-2 and JAM-3 associate with the cell polarity protein PAR-3: a possible role for JAMs in endothelial cell polarity. Journal of cell science 204 12953056
1998 Control of spindle orientation in Drosophila by the Par-3-related PDZ-domain protein Bazooka. Current biology : CB 193 9889099
2006 The polarity protein PAR-3 and TIAM1 cooperate in dendritic spine morphogenesis. Nature cell biology 178 16474385
2005 Direct association of Bazooka/PAR-3 with the lipid phosphatase PTEN reveals a link between the PAR/aPKC complex and phosphoinositide signaling. Development (Cambridge, England) 165 15743877
2003 C. elegans PAR-3 and PAR-6 are required for apicobasal asymmetries associated with cell adhesion and gastrulation. Development (Cambridge, England) 162 13129846
2007 PDZ domains of Par-3 as potential phosphoinositide signaling integrators. Molecular cell 154 18082612
2003 Direct binding of cell polarity protein PAR-3 to cell-cell adhesion molecule nectin at neuroepithelial cells of developing mouse. The Journal of biological chemistry 149 12515806
2002 Regulated protein-protein interaction between aPKC and PAR-3 plays an essential role in the polarization of epithelial cells. Genes to cells : devoted to molecular & cellular mechanisms 145 12390250
2011 Sir-two-homolog 2 (Sirt2) modulates peripheral myelination through polarity protein Par-3/atypical protein kinase C (aPKC) signaling. Proceedings of the National Academy of Sciences of the United States of America 143 21949390
2002 Involvement of ASIP/PAR-3 in the promotion of epithelial tight junction formation. Journal of cell science 141 12045219
2009 Interaction between PAR-3 and the aPKC-PAR-6 complex is indispensable for apical domain development of epithelial cells. Journal of cell science 135 19401335
2003 A conserved oligomerization domain in drosophila Bazooka/PAR-3 is important for apical localization and epithelial polarity. Current biology : CB 131 12906794
2008 Rho-kinase phosphorylates PAR-3 and disrupts PAR complex formation. Developmental cell 130 18267089
2007 Associations with tight junction genes PARD3 and MAGI2 in Dutch patients point to a common barrier defect for coeliac disease and ulcerative colitis. Gut 129 17989107
2006 Microtubule affinity-regulating kinase 2 functions downstream of the PAR-3/PAR-6/atypical PKC complex in regulating hippocampal neuronal polarity. Proceedings of the National Academy of Sciences of the United States of America 128 16717194
2006 The polarity protein Par-3 directly interacts with p75NTR to regulate myelination. Science (New York, N.Y.) 124 17082460
2007 Cdc42 acts downstream of Bazooka to regulate neuroblast polarity through Par-6 aPKC. Journal of cell science 122 17726059
1995 Control of cleavage spindle orientation in Caenorhabditis elegans: the role of the genes par-2 and par-3. Genetics 119 7713417
2003 Self-association of PAR-3-mediated by the conserved N-terminal domain contributes to the development of epithelial tight junctions. The Journal of biological chemistry 111 12756256
2004 Requirement for Par-6 and Bazooka in Drosophila border cell migration. Development (Cambridge, England) 109 15456726
2010 Membrane targeting of Bazooka/PAR-3 is mediated by direct binding to phosphoinositide lipids. Current biology : CB 106 20303268
2012 A role for the centrosome and PAR-3 in the hand-off of MTOC function during epithelial polarization. Current biology : CB 103 22425160
2011 Cell polarity-determining proteins Par-3 and PP-1 are involved in epithelial tight junction defects in coeliac disease. Gut 102 21865402
2006 Lgl mediates apical domain disassembly by suppressing the PAR-3-aPKC-PAR-6 complex to orient apical membrane polarity. Journal of cell science 102 16638806
2008 Par-3-mediated junctional localization of the lipid phosphatase PTEN is required for cell polarity establishment. The Journal of biological chemistry 100 18550519
1998 The human proteinase-activated receptor-3 (PAR-3) gene. Identification within a Par gene cluster and characterization in vascular endothelial cells and platelets. The Journal of biological chemistry 100 9614115
2010 PAR-3 mediates the initial clustering and apical localization of junction and polarity proteins during C. elegans intestinal epithelial cell polarization. Development (Cambridge, England) 97 20431121
2010 ASPP2 binds Par-3 and controls the polarity and proliferation of neural progenitors during CNS development. Developmental cell 97 20619750
2009 Independent cadherin-catenin and Bazooka clusters interact to assemble adherens junctions. The Journal of cell biology 97 19468069
2007 Cooperative roles of Par-3 and afadin in the formation of adherens and tight junctions. Journal of cell science 89 17606991
2004 Differential functions of G protein and Baz-aPKC signaling pathways in Drosophila neuroblast asymmetric division. The Journal of cell biology 89 14981094
2001 Bazooka and atypical protein kinase C are required to regulate oocyte differentiation in the Drosophila ovary. Proceedings of the National Academy of Sciences of the United States of America 79 11734648
2010 Siah regulation of Pard3A controls neuronal cell adhesion during germinal zone exit. Science (New York, N.Y.) 78 21109632
2009 Defective expression of polarity protein PAR-3 gene (PARD3) in esophageal squamous cell carcinoma. Oncogene 78 19503097
2010 Formation of a Bazooka-Stardust complex is essential for plasma membrane polarity in epithelia. The Journal of cell biology 77 20819933
2008 Protein phosphatase 1 regulates the phosphorylation state of the polarity scaffold Par-3. Proceedings of the National Academy of Sciences of the United States of America 75 18641122
2001 Bazooka and PAR-6 are required with PAR-1 for the maintenance of oocyte fate in Drosophila. Current biology : CB 75 11516655
2006 Par-3 mediates the inhibition of LIM kinase 2 to regulate cofilin phosphorylation and tight junction assembly. The Journal of cell biology 74 16505165
2003 Distinct roles of Bazooka and Stardust in the specification of Drosophila photoreceptor membrane architecture. Proceedings of the National Academy of Sciences of the United States of America 71 14569003
2009 RalA and the exocyst complex influence neuronal polarity through PAR-3 and aPKC. Journal of cell science 65 19383721
2017 Listeriolysin O: from bazooka to Swiss army knife. Philosophical transactions of the Royal Society of London. Series B, Biological sciences 62 28630160
2010 Bazooka is required for polarisation of the Drosophila anterior-posterior axis. Development (Cambridge, England) 62 20430751
2009 PP2A antagonizes phosphorylation of Bazooka by PAR-1 to control apical-basal polarity in dividing embryonic neuroblasts. Developmental cell 62 19531360
2006 The aPKC-PAR-6-PAR-3 cell polarity complex localizes to the centrosome attracting body, a macroscopic cortical structure responsible for asymmetric divisions in the early ascidian embryo. Journal of cell science 60 16569661
2004 Baz, Par-6 and aPKC are not required for axon or dendrite specification in Drosophila. Nature neuroscience 58 15543144
2018 PARD3 dysfunction in conjunction with dynamic HIPPO signaling drives cortical enlargement with massive heterotopia. Genes & development 57 29899142
2005 PAR-3 defines a central subdomain of the cortical actin cap in mouse eggs. Developmental biology 57 15766746
2004 The zebrafish Pard3 ortholog is required for separation of the eye fields and retinal lamination. Developmental biology 56 15081374
2007 Similar requirements for CDC-42 and the PAR-3/PAR-6/PKC-3 complex in diverse cell types. Developmental biology 55 17383625
2014 PI(4,5)P2 produced by the PI4P5K SKTL controls apical size by tethering PAR-3 in Drosophila epithelial cells. Current biology : CB 54 24768049
2013 Dynamic microtubules produce an asymmetric E-cadherin-Bazooka complex to maintain segment boundaries. The Journal of cell biology 54 23751496
2007 Downregulation of Par-3 expression and disruption of Par complex integrity by TGF-beta during the process of epithelial to mesenchymal transition in rat proximal epithelial cells. Biochimica et biophysica acta 52 18070611
2015 The polarity protein Baz forms a platform for the centrosome orientation during asymmetric stem cell division in the Drosophila male germline. eLife 51 25793442
2015 PARD3 induces TAZ activation and cell growth by promoting LATS1 and PP1 interaction. EMBO reports 50 26116754
2002 The fusome and microtubules enrich Par-1 in the oocyte, where it effects polarization in conjunction with Par-3, BicD, Egl, and dynein. Current biology : CB 49 12225669
2011 PAR-3 oligomerization may provide an actin-independent mechanism to maintain distinct par protein domains in the early Caenorhabditis elegans embryo. Biophysical journal 48 21943422
2012 β2-syntrophin and Par-3 promote an apicobasal Rac activity gradient at cell-cell junctions by differentially regulating Tiam1 activity. Nature cell biology 46 23103911
2010 TGF-{beta}-induced MiR-491-5p expression promotes Par-3 degradation in rat proximal tubular epithelial cells. The Journal of biological chemistry 46 20966078
2003 Bazooka is a permissive factor for the invasive behavior of discs large tumor cells in Drosophila ovarian follicular epithelia. Development (Cambridge, England) 46 12642496
2018 MicroRNA 483-3p targets Pard3 to potentiate TGF-β1-induced cell migration, invasion, and epithelial-mesenchymal transition in anaplastic thyroid cancer cells. Oncogene 45 30171257
2010 The polarity protein Pard3 is required for centrosome positioning during neurulation. Developmental biology 45 20138861
2019 LncRNA SLCO4A1-AS1 promotes colorectal cancer cell proliferation by enhancing autophagy via miR-508-3p/PARD3 axis. Aging 44 31308265
2004 PAR-3 is required for epithelial cell polarity in the distal spermatheca of C. elegans. Development (Cambridge, England) 44 15151982
2015 PARD3 Inactivation in Lung Squamous Cell Carcinomas Impairs STAT3 and Promotes Malignant Invasion. Cancer research 43 25833829
2013 Par3/Bazooka and phosphoinositides regulate actin protrusion formation during Drosophila dorsal closure and wound healing. Development (Cambridge, England) 43 23318638
2012 Assembly of Bazooka polarity landmarks through a multifaceted membrane-association mechanism. Journal of cell science 43 22303000
2003 Evidence for functionally active protease-activated receptor-3 (PAR-3) in human vascular smooth muscle cells. Thrombosis and haemostasis 43 14515192
2012 Substrate recognition mechanism of atypical protein kinase Cs revealed by the structure of PKCι in complex with a substrate peptide from Par-3. Structure (London, England : 1993) 42 22579248
2000 Meiotic maturation induces animal-vegetal asymmetric distribution of aPKC and ASIP/PAR-3 in Xenopus oocytes. Development (Cambridge, England) 41 11060229
2010 Different domains of C. elegans PAR-3 are required at different times in development. Developmental biology 40 20678977
2008 The protease-activated receptor-3 (PAR-3) can signal autonomously to induce interleukin-8 release. Cellular and molecular life sciences : CMLS 39 18264801
2001 Bazooka is required for localization of determinants and controlling proliferation in the sensory organ precursor cell lineage in Drosophila. Proceedings of the National Academy of Sciences of the United States of America 38 11734647
2013 Bazooka inhibits aPKC to limit antagonism of actomyosin networks during amnioserosa apical constriction. Development (Cambridge, England) 36 24173807
2010 Binding to PKC-3, but not to PAR-3 or to a conventional PDZ domain ligand, is required for PAR-6 function in C. elegans. Developmental biology 36 20122916
2009 A critical step for postsynaptic F-actin organization: regulation of Baz/Par-3 localization by aPKC and PTEN. Developmental neurobiology 36 19472188
2018 PAR-3 controls endothelial planar polarity and vascular inflammation under laminar flow. EMBO reports 34 30018153
2014 Lgl regulates Notch signaling via endocytosis, independently of the apical aPKC-Par6-Baz polarity complex. Current biology : CB 34 25220057
2017 Downregulation of PKCζ/Pard3/Pard6b is responsible for lung adenocarcinoma cell EMT and invasion. Cellular signalling 33 28652146
2015 Regulation of epithelial cell polarity by PAR-3 depends on Girdin transcription and Girdin-Gαi3 signaling. Journal of cell science 33 25977476

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