Affinage

SASS6

Spindle assembly abnormal protein 6 homolog · UniProt Q6UVJ0

Length
657 aa
Mass
74.4 kDa
Annotated
2026-04-28
53 papers in source corpus 27 papers cited in narrative 27 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

SASS6 (SAS-6) is the master structural scaffold of the centriolar cartwheel, whose self-assembly into 9-fold symmetric ring polymers establishes the fundamental radial symmetry of centrioles and is essential for centriole biogenesis across eukaryotes. The N-terminal globular domain mediates head-to-head dimerization that drives ring formation, while the coiled-coil domain enables asymmetric homo-oligomerization that imparts polarity and supports ring stacking into the cartwheel hub; point mutations at either interface abolish centriole assembly in vivo (PMID:21273447, PMID:35240058, PMID:26002084). SAS-6 is recruited to the mother centriole through direct binding of the ZYG-1/PLK4 kinase and PLK4-phosphorylated SAS-5/Ana2/STIL to its coiled-coil region, and its C-terminal tail anchors the γ-tubulin ring complex to nucleate centriolar microtubules (PMID:23673331, PMID:25264260, PMID:32442461). SAS-6 protein levels are tightly controlled by APC/C-Cdh1 degradation in late mitosis/G1 and FBXW7-mediated ubiquitination of the STIL–SAS-6 complex to prevent centriole overduplication, while CDK-1 phosphorylation of its C-terminus inhibits phase separation to promote timely centriole disassembly during oogenesis (PMID:40825584, PMID:41453690, PMID:40410380).

Mechanistic history

Synthesis pass · year-by-year structured walk · 19 steps
  1. 2005 High

    Establishing SAS-6 as a conserved centrosome duplication factor resolved the question of which proteins are essential for new centriole formation: SAS-6 is required for centrosome duplication in human cells and C. elegans, and its centriolar recruitment depends on ZYG-1 and SAS-5.

    Evidence siRNA knockdown in U2OS cells, co-IP and genetic epistasis in C. elegans

    PMID:15665853

    Open questions at the time
    • Structural role of SAS-6 at the centriole was unknown
    • Mechanism of SAS-6 self-organization not addressed
    • Whether SAS-6 dictates centriole symmetry was untested
  2. 2007 High

    Determining that SAS-6 localizes specifically to the cartwheel hub and is required for 9-fold symmetry answered the long-standing question of what specifies centriole radial architecture: loss of SAS-6 produces centrioles with variable triplet numbers.

    Evidence Immunolocalization and EM of Chlamydomonas bld12 null mutants

    PMID:18082404

    Open questions at the time
    • Molecular basis of 9-fold symmetry specification unknown
    • Whether SAS-6 alone is sufficient for symmetry establishment untested
  3. 2009 High

    Identifying ZYG-1 phosphorylation of SAS-6 at S123 as essential for centriole formation established that kinase signaling directly regulates the cartwheel scaffold, not just its upstream recruitment factors.

    Evidence In vitro kinase assay with phospho-site mutagenesis and in vivo centriole formation in C. elegans

    PMID:20059959

    Open questions at the time
    • Whether phosphorylation affects SAS-6 self-assembly or protein interactions was unclear
    • Mammalian equivalent phosphosite not identified
  4. 2010 High

    Reconstituting SAS-6 self-assembly into tetramers in vitro demonstrated that SAS-6 is an intrinsic building block of the cartwheel, shifting the model from a passively recruited scaffold to a self-organizing polymer.

    Evidence Recombinant Drosophila SAS-6 size-exclusion chromatography and EM

    PMID:20083610

    Open questions at the time
    • Atomic-resolution structure of self-assembly interface not yet available
    • Whether 9-fold ring forms spontaneously in vitro was unknown
  5. 2011 High

    Solving the crystal structure of the SAS-6 N-terminal domain and showing that mutations at the dimerization interface block centriole formation provided the first atomic-level explanation of how SAS-6 self-assembly builds the cartwheel.

    Evidence X-ray crystallography of zebrafish SAS-6 with in vitro assembly and in vivo mutagenesis

    PMID:21273447

    Open questions at the time
    • Full-ring structure not yet solved
    • Coiled-coil contribution to stacking unknown
    • Species-specific variations in symmetry not addressed
  6. 2013 High

    Demonstrating that ZYG-1 directly binds the SAS-6 coiled coil independently of kinase activity, and that SAS-5 binds the same domain, resolved how SAS-6 is physically delivered to the mother centriole through a two-factor recruitment mechanism.

    Evidence Direct binding assays, reciprocal co-IP, and in vivo recruitment in C. elegans

    PMID:23673331

    Open questions at the time
    • Whether PLK4 uses the same binding mode in mammals was untested
    • Stoichiometry of the recruitment complex unknown
  7. 2013 High

    Solving the C. elegans SAS-6 structure as a spiral rather than a planar ring revealed species-specific assembly variants consistent with the nematode central tube architecture, broadening the structural paradigm.

    Evidence X-ray crystallography and EM of C. elegans SAS-6

    PMID:23798409

    Open questions at the time
    • How the spiral converts to an in vivo-functional central tube was unclear
    • Relationship between spiral and ring assembly pathways unresolved
  8. 2014 High

    Crystallizing the Leishmania SAS-6 as a complete 9-fold symmetric cartwheel proved that SAS-6 self-assembly alone can dictate cartwheel symmetry, and identification of a small-molecule oligomerization inhibitor opened a pharmacological approach.

    Evidence 3.5 Å X-ray crystal structure plus in vitro small-molecule inhibition

    PMID:24596152

    Open questions at the time
    • In vivo efficacy of the small-molecule inhibitor not tested
    • Whether mammalian SAS-6 forms equivalent complete rings in vitro was unknown
  9. 2014 High

    Showing that PLK4 phosphorylation of Ana2/STIL's STAN motif is the switch enabling SAS-6 recruitment defined the upstream signaling event that licenses cartwheel initiation at the procentriole.

    Evidence In vitro kinase assay, phospho-site mutagenesis, in vivo duplication assay in Drosophila; complemented by human S-phase SAS-6 dynamics

    PMID:25017693 PMID:25264260

    Open questions at the time
    • Order of Ana2 phosphorylation events relative to SAS-6 ring assembly not resolved
    • Whether SAS-6 luminal recruitment and outer-wall assembly involve different SAS-6 pools was unclear
  10. 2015 High

    Identifying that the SAS-6 C-terminal tail directly binds tubulin and nucleates microtubule polymerization revealed a second functional domain beyond the cartwheel-forming N-terminus, linking the cartwheel scaffold to centriolar microtubule wall formation.

    Evidence In vitro microtubule polymerization, ITC, co-IP from HeLa lysates

    PMID:26422590

    Open questions at the time
    • Structural basis of C-tail–tubulin interaction not resolved
    • Whether γ-TuRC or free tubulin is the physiological target was unclear
  11. 2015 High

    Demonstrating that centrioles can form de novo without SAS-6 self-oligomerization but with frequent structural errors, while template-directed duplication always preserves 9-fold symmetry, established that the mother centriole provides an essential fidelity mechanism beyond SAS-6 intrinsic self-assembly.

    Evidence Reconstitution of de novo centriole synthesis in human cells with oligomerization-dead SAS-6 mutants and EM analysis

    PMID:26609813

    Open questions at the time
    • Nature of the template-based error-correction mechanism unknown
    • Whether other cartwheel components compensate in the absence of SAS-6 oligomerization unclear
  12. 2016 High

    Engineering SAS-6 variants with altered symmetry properties demonstrated that SAS-6 self-assembly directly instructs cartwheel symmetry and that cartwheel and microtubule wall assembly are interdependent, resolving whether symmetry is SAS-6-intrinsic or templated.

    Evidence Symmetry-altering SAS-6 mutations tested in vitro and in vivo in Chlamydomonas and human cells

    PMID:26999736

    Open questions at the time
    • How the microtubule wall feeds back on cartwheel symmetry is mechanistically unclear
  13. 2017 Medium

    Identifying CDC6 as a negative regulator that binds SAS-6 and prevents STIL–SAS-6 complex formation until PLK4 phosphorylates CDC6 established a licensing checkpoint coupling DNA replication and centrosome duplication through SAS-6.

    Evidence Co-IP, centrosome localization, overexpression/knockdown, PLK4 phosphorylation assay in human cells

    PMID:28447620

    Open questions at the time
    • Single-lab study; independent validation needed
    • Structural basis of CDC6–SAS-6 interaction unknown
    • Whether CDC6 regulation is conserved beyond mammals untested
  14. 2018 High

    Real-time visualization of SAS-6 ring assembly by high-speed AFM revealed that multiple kinetically distinct assembly intermediates converge on 9-fold symmetric rings, demonstrating robust self-assembly through parallel pathways.

    Evidence Photothermal off-resonance AFM with kinetic analysis of Chlamydomonas SAS-6

    PMID:29784964

    Open questions at the time
    • In vivo relevance of alternative assembly routes not established
    • Whether accessory factors constrain assembly pathways in cells unknown
  15. 2019 Medium

    Identifying pericentrin as a direct SAS-6-binding partner that recruits SAS-6 to the pericentriolar material revealed an additional, PCM-based route for SAS-6 centriolar loading conserved from fission yeast to animals.

    Evidence Yeast two-hybrid, co-IP, ectopic expression in fission yeast, centriole elongation assay

    PMID:31182187

    Open questions at the time
    • Relative contribution of pericentrin- versus STIL-mediated recruitment unclear
    • Single-lab finding; independent confirmation in mammalian cells needed
  16. 2020 High

    Mapping the SAS-6 C-terminus–γ-TuRC interaction and showing that C-terminal deletion prevents daughter centriole microtubule nucleation unified the cartwheel scaffold and microtubule nucleation functions of SAS-6, while HDX-MS of Sas6–Gorab and Sas6–Ana2 complexes defined separable binding interfaces on the coiled-coil allowing simultaneous partner engagement.

    Evidence Co-IP, deletion mutagenesis, super-resolution microscopy (human cells); HDX-MS and EM of Drosophila complexes

    PMID:32442461 PMID:33171067 PMID:33704067

    Open questions at the time
    • Atomic structure of SAS-6 C-tail–γ-TuRC complex not determined
    • Whether Gorab interaction is conserved in mammals unknown
  17. 2022 High

    Solving crystal structures of SAS-6 coiled-coil complexes revealed an asymmetric homo-oligomerization that imparts polarity to the cartwheel stack, explaining how directional growth of the cartwheel is encoded in SAS-6 itself.

    Evidence X-ray crystallography and cryo-EM reconstitution of Chlamydomonas SAS-6 coiled-coil with mutagenesis

    PMID:35240058

    Open questions at the time
    • How polarity information is read out by downstream assembly factors is unknown
    • In vivo consequences of polarity disruption not tested in animal cells
  18. 2024 High

    Genetic knockout in mouse demonstrated that SAS-6 is essential for centriole formation in embryos (causing mid-gestation arrest) but dispensable in mESCs where elevated PLK4 enables a SAS-6-independent pathway, revealing context-dependent essentiality.

    Evidence Mouse genetic knockout, embryo phenotyping, mESC culture with PLK4 manipulation

    PMID:38407237

    Open questions at the time
    • Mechanism of PLK4-dependent SAS-6-independent centriole assembly unknown
    • Whether SAS-6-independent pathway operates in any normal physiological context untested
  19. 2025 High

    Identifying FBXW7-mediated degradation of the STIL–SAS-6 complex as a PLK4-dependent opposing mechanism and APC/C-Cdh1 as a cell-cycle-timed SAS-6 degradation pathway, together with CDK-1 phosphorylation that inhibits SAS-6 phase separation, defined three layers of post-translational control ensuring centriole number fidelity and developmental centriole disassembly.

    Evidence FBXW7 siRNA/co-IP/ubiquitination assays in human cells; non-degradable SAS-6 mutant with YAP/TAZ pathway analysis; in vitro phase separation plus CDK-1 kinase assay and C. elegans oogenesis phenotypes

    PMID:40410380 PMID:40825584 PMID:41453690

    Open questions at the time
    • Structural basis of APC/C-Cdh1 recognition of SAS-6 not defined
    • How CDK-1 phosphorylation coordinates with FBXW7 and APC/C pathways is unknown
    • Whether SAS-6 phase separation occurs in somatic mammalian cells in vivo remains untested

Open questions

Synthesis pass · forward-looking unresolved questions
  • Key unresolved questions include the complete atomic structure of a stacked mammalian cartwheel in situ, the mechanism by which the mother centriole templates structural fidelity, and how the PLK4-dependent SAS-6-independent centriole assembly pathway operates at the molecular level.
  • No in situ atomic-resolution structure of the assembled mammalian cartwheel
  • Template-based error-correction mechanism during canonical duplication undefined
  • SAS-6-independent centriole biogenesis pathway molecularly uncharacterized

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0005198 structural molecule activity 8 GO:0008092 cytoskeletal protein binding 2
Localization
GO:0005815 microtubule organizing center 5
Pathway
R-HSA-1852241 Organelle biogenesis and maintenance 5 R-HSA-1640170 Cell Cycle 4
Partners
CDC6FBXW7GORABPCNTPLK4STILTUBG1
Complex memberships
STIL-SAS-6 complexcartwheel

Evidence

Reading pass · 27 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2005 HsSAS-6 (human SASS6) localizes to centrosomes and is required for centrosome duplication: siRNA-mediated inactivation in U2OS cells abrogates centrosome overduplication following aphidicolin treatment and interferes with the normal centrosome duplication cycle. In C. elegans, SAS-6 and SAS-5 associate, and this interaction as well as ZYG-1 function is required for SAS-6 centriolar recruitment. siRNA knockdown, GFP localization, co-immunoprecipitation, genetic analysis in C. elegans Nature cell biology High 15665853
2007 SAS-6 localizes to the central part of the centriolar cartwheel and is required to establish the 9-fold symmetry of centrioles; null mutants in Chlamydomonas (bld12) lack the central cartwheel hub and frequently produce centrioles with aberrant triplet numbers (7, 8, 10, or 11 instead of 9). Immunolocalization, genetic null mutant analysis, electron microscopy Current biology : CB High 18082404
2009 ZYG-1 kinase phosphorylates SAS-6 at serine 123 in vitro, and this phosphorylation is required for centriole formation in C. elegans embryos in vivo; phosphorylation maintains SAS-6 at the emerging centriole. In vitro kinase assay, phospho-site mutagenesis, in vivo centriole formation assay in C. elegans Developmental cell High 20059959
2010 Drosophila SAS-6 self-assembles into stable tetramers in vitro that serve as building blocks for the cartwheel central tubule; EM of centrosomes identifies SAS-6 concentrating at the core of the cartwheel. Biochemistry (size exclusion chromatography), electron microscopy, recombinant protein assembly assay The Journal of biological chemistry High 20083610
2011 The X-ray crystal structure of the SAS-6 N-terminal domain from zebrafish reveals that SAS-6 self-associates in vitro into assemblies resembling cartwheel centers; point mutations at the self-assembly interfaces block centriole formation in vivo, establishing these interactions as essential for cartwheel organization. X-ray crystallography, in vitro self-assembly assay, point mutagenesis with in vivo functional validation Science (New York, N.Y.) High 21273447
2013 ZYG-1 directly binds the SAS-6 coiled coil and recruits SAS-6 to the mother centriole independently of its kinase activity; ZYG-1 kinase activity is subsequently required for cartwheel assembly. The SAS-6 coiled coil also interacts with SAS-5, and both interactions are required for SAS-6 centriolar recruitment. Direct binding assay, reciprocal co-immunoprecipitation, mutagenesis, in vivo recruitment assay in C. elegans Developmental cell High 23673331
2013 C. elegans SAS-6 self-assembles into a spiral arrangement (rather than a ring) in vitro, as revealed by X-ray crystallography and EM; the spiral is consistent with 9-fold symmetry and provides a structural basis for the central tube found in nematode centriole assembly. X-ray crystallography, electron microscopy, structural analysis Proceedings of the National Academy of Sciences of the United States of America High 23798409
2014 Leishmania major SAS-6 crystallizes as a 9-fold symmetric cartwheel; the X-ray structure demonstrates that SAS-6 self-assembly alone can dictate cartwheel symmetry. SAS-6 oligomerization can be inhibited by a small molecule in vitro. X-ray crystallography (3.5 Å resolution), small-molecule inhibition of oligomerization in vitro eLife High 24596152
2014 In Drosophila, PLK4 phosphorylates four conserved serines in the STAN motif of Ana2 (the SAS-6 recruitment factor) to enable Ana2 to bind and recruit Sas6 to the procentriole; non-phosphorylatable Ana2 localizes to the centriole but cannot recruit Sas6, blocking centriole duplication. In vitro kinase assay, phospho-site mutagenesis, in vivo centriole duplication assay, co-immunoprecipitation Current biology : CB High 25264260
2014 During S phase, SAS-6 is first recruited to the proximal lumen of the mother centriole, adopting a cartwheel-like organization through interactions with the luminal wall rather than via self-oligomerization; removal of luminal SAS-6 requires PLK4 and STIL, and abolishing either recruitment or removal hinders SAS-6 assembly at the outer wall. Live-cell imaging, FRAP, siRNA knockdown, structured illumination microscopy Developmental cell High 25017693
2015 The C-terminal tail of human SAS-6 (residues 470–657) nucleates and promotes microtubule polymerization in vitro, binds microtubules and tubulin dimers directly, and co-precipitates with microtubules from S-phase synchronized HeLa cell lysates; the N-terminal domain does not affect microtubule polymerization. In vitro microtubule polymerization assay, microtubule pulldown, co-immunoprecipitation, isothermal titration calorimetry, size exclusion chromatography Biochemistry High 26422590
2015 De novo centriole formation in human cells can occur in the absence of SAS-6 self-oligomerization, whereas canonically duplicated centrioles always form correctly; de novo centrioles are structurally error-prone even with SAS-6 self-oligomerization, indicating a template/mother-centriole requirement for structural fidelity. Reconstitution of de novo centriole synthesis in human cells, mutagenesis of SAS-6 self-oligomerization interface, EM structural analysis eLife High 26609813
2015 Drosophila Sas-6 N-terminal domain forms higher-order oligomers through canonical interactions (crystal structure at 2.9 Å); point mutations that perturb Sas-6 homo-oligomerization in vitro strongly impair centriole assembly in vivo. X-ray crystallography, in vitro oligomerization assay, in vivo centriole assembly assay with point mutants eLife High 26002084
2016 Engineering Chlamydomonas SAS-6 to form different symmetry oligomers in vitro reveals that SAS-6 self-assembly properties instruct cartwheel symmetry, and that the cartwheel and microtubule wall assemble interdependently. Expressing analogous SAS-6 mutations in human cells produced 9-fold symmetric centrioles with impaired length and organization. SAS-6 mutagenesis, in vitro oligomerization assay, in vivo centriole symmetry analysis by EM, human cell expression Nature cell biology High 26999736
2017 In Drosophila, PLK4 performs two-step phosphorylation of Ana2: first at S38 in the ANST motif to promote Ana2 centriolar recruitment, then at four serines in the STAN motif to enable Ana2 to recruit Sas6. Mutation of S38 to alanine blocks Ana2 loading and centriole duplication. In vitro kinase assay, phospho-site mutagenesis, in vivo centriole duplication assay, live-cell imaging Open biology High 29263250
2017 CDC6, a DNA replication licensing factor, is recruited to the proximal centriole via cyclin A and inhibits centrosome duplication by binding SAS-6 and preventing formation of a stable SAS-6–STIL complex; PLK4 phosphorylates CDC6 to disrupt the CDC6–SAS-6 interaction, relieving inhibition. Co-immunoprecipitation, centrosome localization assay, overexpression/knockdown experiments, phosphorylation assay Nature communications Medium 28447620
2018 High-speed photothermal off-resonance AFM (PORT) reveals the kinetics of SAS-6 ring formation in real time and demonstrates that distinct biogenesis routes (different assembly intermediates) can converge to produce a 9-fold symmetric ring structure. High-speed atomic force microscopy (PORT), real-time self-assembly monitoring Nature nanotechnology High 29784964
2019 Pericentrin (Pcp1) interacts with and recruits SAS-6 to the pericentriolar material; this interaction is conserved between fission yeast SPB and animal centrosomes and is important for centriole assembly, particularly elongation. The calmodulin-binding region of pericentrin is critical for SAS-6 interaction. Yeast two-hybrid, co-immunoprecipitation, ectopic expression in fission yeast, functional centriole elongation assay eLife Medium 31182187
2020 Human SAS-6 C-terminus interacts with the γ-tubulin ring complex (γ-TuRC) at the centrosome; deletion of the SAS-6 C-terminus disrupts microtubule formation in daughter centrioles causing failure to form new centrioles. High-resolution microscopy reveals γ-tubulin localizing as multiple lobes surrounding the SAS-6-containing central hub. Co-immunoprecipitation, deletion mutagenesis, super-resolution microscopy, siRNA knockdown with phenotypic readout Current biology : CB High 32442461
2020 The Drosophila Golgi protein Gorab binds as a monomer to the parallel coiled-coil dimer of Sas6, forming a stable heterotrimer visualized by EM; mutation of a single leucine in Sas6's Gorab-binding domain reduces affinity 16-fold and abolishes centriole duplication, revealing a functional Sas6–Gorab interaction required for duplication. Hydrogen-deuterium exchange mass spectrometry, electron microscopy, mutagenesis, in vivo centriole duplication assay eLife High 33704067
2020 HDX-MS of the Drosophila Ana2–Sas6 complex identifies short critical regions in the C-terminal parts of both proteins as the interaction interface; phosphomimetic Ana2 (Ana2-4D) forms a complex with Sas6 in vitro and in vivo, and mutations in these regions disrupt the Ana2–Sas6 interaction. The Sas6 site for Ana2 binding is distinct from the Gorab-binding site, allowing simultaneous binding. Hydrogen-deuterium exchange mass spectrometry, co-immunoprecipitation in vitro and in vivo, mutagenesis Open biology High 33171067
2021 Monobodies developed against Chlamydomonas SAS-6 (characterized by X-ray crystallography, AFM, and cryo-EM) reveal distinct interaction modes; one monobody (MBCRS6-15) induces a conformational change causing SAS-6 to form a helix instead of a ring, and expression of this monobody in human cells impairs centriole biogenesis. X-ray crystallography, atomic force microscopy, cryo-EM, human cell centriole biogenesis assay Nature communications High 34155202
2022 Crystal structures of Chlamydomonas SAS-6 coiled-coil complexes reveal an asymmetric homo-oligomerization interaction that imparts polarity to the cartwheel; cryo-EM reconstitution assay demonstrates that amino acid substitutions disrupting this asymmetric association impair SAS-6 ring stacking. X-ray crystallography, cryo-EM reconstitution assay, mutagenesis of coiled-coil Structure (London, England : 1993) High 35240058
2024 In mouse embryos, Sass6 (SASS6) is essential for centriole formation; Sass6-mutant embryos lack centrioles, activate the mitotic surveillance cell death pathway, and arrest at mid-gestation. In mouse embryonic stem cells (mESCs), SAS-6 is not required for centriole formation but is essential for centriole architecture maintenance; elevated PLK4 activity in mESCs enables a SAS-6-independent centriole biogenesis pathway. Genetic knockout in mouse, embryo phenotypic analysis, mESC culture, PLK4 activity manipulation, centrosome/centriole imaging eLife High 38407237
2025 FBXW7 E3 ubiquitin ligase mediates degradation of the STIL–SAS6 cartwheel assembly in a PLK4 kinase activity-dependent manner; PLK4 phosphorylation of STIL drives both STIL–SAS6 interaction (promoting new centriole assembly) and FBXW7 binding to STIL (promoting STIL–SAS6 degradation), creating an opposing mechanism that prevents centriole overduplication. siRNA knockdown of FBXW7, co-immunoprecipitation, ubiquitination assay, PLK4 kinase inhibition The Journal of biological chemistry Medium 41453690
2025 SAS-6 levels are controlled by APC/C-Cdh1-targeted degradation at the end of mitosis/G1; expression of a non-degradable SAS-6 mutant (SAS-6ND) increases ciliation and cell invasion through activation of the YAP/TAZ pathway and nuclear YAP translocation leading to TEAD-dependent transcription. SAS-6-mediated invasion is blocked by YAP downregulation or by blocking ciliogenesis. Non-degradable SAS-6 mutant expression, siRNA knockdown, invasion assay, YAP/TAZ pathway analysis, ciliogenesis assay Life science alliance Medium 40825584
2025 SAS-6 undergoes phase separation in vitro; CDK-1 directly phosphorylates SAS-6 at its C-terminus in cells and in vivo, and this phosphorylation inhibits SAS-6 phase separation and weakens interactions between centriolar proteins. Phospho-mimetic and phospho-deficient SAS-6 mutants demonstrate that dynamic phosphorylation controls centrosome assembly during oogenesis and timely centriole disassembly in C. elegans. In vitro phase separation assay, mass spectrometry, in vitro kinase assay, phospho-site mutagenesis, in vivo oogenesis phenotype analysis in C. elegans EMBO reports High 40410380

Source papers

Stage 0 corpus · 53 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2005 SAS-6 defines a protein family required for centrosome duplication in C. elegans and in human cells. Nature cell biology 329 15665853
2011 Structures of SAS-6 suggest its organization in centrioles. Science (New York, N.Y.) 263 21273447
2007 SAS-6 is a cartwheel protein that establishes the 9-fold symmetry of the centriole. Current biology : CB 217 18082404
2014 Plk4 phosphorylates Ana2 to trigger Sas6 recruitment and procentriole formation. Current biology : CB 147 25264260
2016 The PLK4-STIL-SAS-6 module at the core of centriole duplication. Biochemical Society transactions 120 27911707
2018 High-speed photothermal off-resonance atomic force microscopy reveals assembly routes of centriolar scaffold protein SAS-6. Nature nanotechnology 85 29784964
2007 The zebrafish maternal-effect gene cellular atoll encodes the centriolar component sas-6 and defects in its paternal function promote whole genome duplication. Developmental biology 68 17950723
2016 SAS-6 engineering reveals interdependence between cartwheel and microtubules in determining centriole architecture. Nature cell biology 61 26999736
2014 Structure of the SAS-6 cartwheel hub from Leishmania major. eLife 58 24596152
2013 A SAS-6-like protein suggests that the Toxoplasma conoid complex evolved from flagellar components. Eukaryotic cell 58 23687115
2017 Two-step phosphorylation of Ana2 by Plk4 is required for the sequential loading of Ana2 and Sas6 to initiate procentriole formation. Open biology 55 29263250
2014 SAS-6 assembly templated by the lumen of cartwheel-less centrioles precedes centriole duplication. Developmental cell 54 25017693
2013 Direct binding of SAS-6 to ZYG-1 recruits SAS-6 to the mother centriole for cartwheel assembly. Developmental cell 53 23673331
2013 Caenorhabditis elegans centriolar protein SAS-6 forms a spiral that is consistent with imparting a ninefold symmetry. Proceedings of the National Academy of Sciences of the United States of America 52 23798409
2009 Phosphorylation of SAS-6 by ZYG-1 is critical for centriole formation in C. elegans embryos. Developmental cell 52 20059959
2015 The homo-oligomerisation of both Sas-6 and Ana2 is required for efficient centriole assembly in flies. eLife 48 26002084
2015 De novo centriole formation in human cells is error-prone and does not require SAS-6 self-assembly. eLife 46 26609813
2015 The Centriole Cartwheel Protein SAS-6 in Trypanosoma brucei Is Required for Probasal Body Biogenesis and Flagellum Assembly. Eukaryotic cell 38 26116214
2017 DNA replication licensing factor Cdc6 and Plk4 kinase antagonistically regulate centrosome duplication via Sas-6. Nature communications 36 28447620
2010 Self-assembling SAS-6 multimer is a core centriole building block. The Journal of biological chemistry 36 20083610
2014 An essential role of the basal body protein SAS-6 in Plasmodium male gamete development and malaria transmission. Cellular microbiology 32 25154861
2016 SAS6-like protein in Plasmodium indicates that conoid-associated apical complex proteins persist in invasive stages within the mosquito vector. Scientific reports 28 27339728
2019 Pericentrin-mediated SAS-6 recruitment promotes centriole assembly. eLife 23 31182187
2024 Mouse SAS-6 is required for centriole formation in embryos and integrity in embryonic stem cells. eLife 14 38407237
2019 Poc1B and Sas-6 Function Together during the Atypical Centriole Formation in Drosophila melanogaster. Cells 13 31387336
2020 Drosophila Sas-6, Ana2 and Sas-4 self-organise into macromolecular structures that can be used to probe centriole and centrosome assembly. Journal of cell science 11 32409564
2020 SAS-6 Association with γ-Tubulin Ring Complex Is Required for Centriole Duplication in Human Cells. Current biology : CB 11 32442461
2019 Novel SASS6 compound heterozygous mutations in a Chinese family with primary autosomal recessive microcephaly. Clinica chimica acta; international journal of clinical chemistry 11 30639237
2024 The Ruminococcus bromii amylosome protein Sas6 binds single and double helical α-glucan structures in starch. Nature structural & molecular biology 10 38177679
2020 CCDC61/VFL3 Is a Paralog of SAS6 and Promotes Ciliary Functions. Structure (London, England : 1993) 10 32375023
2023 A primary microcephaly-associated sas-6 mutation perturbs centrosome duplication, dendrite morphogenesis, and ciliogenesis in Caenorhabditis elegans. Genetics 9 37279547
2022 The chromatin remodeling protein CHD-1 and the EFL-1/DPL-1 transcription factor cooperatively down regulate CDK-2 to control SAS-6 levels and centriole number. PLoS genetics 9 35377871
2021 SASS6 promotes proliferation of esophageal squamous carcinoma cells by inhibiting the p53 signaling pathway. Carcinogenesis 9 32671379
2015 Human SAS-6 C-Terminus Nucleates and Promotes Microtubule Assembly in Vitro by Binding to Microtubules. Biochemistry 9 26422590
2021 Knockdown of SASS6 reduces growth of MDA‑MB‑231 triple‑negative breast cancer cells through arrest of the cell cycle at the G2/M phase. Oncology reports 8 33907854
2009 Centriole assembly in CHO cells expressing Plk4/SAS6/SAS4 is similar to centriogenesis in ciliated epithelial cells. Cell motility and the cytoskeleton 8 19402176
2022 Structures of SAS-6 coiled coil hold implications for the polarity of the centriolar cartwheel. Structure (London, England : 1993) 7 35240058
2021 Tuning SAS-6 architecture with monobodies impairs distinct steps of centriole assembly. Nature communications 7 34155202
2018 Identification and localization of SAS-6 in the microsporidium Nosema bombycis. Infection, genetics and evolution : journal of molecular epidemiology and evolutionary genetics in infectious diseases 5 30244093
2021 The dimeric Golgi protein Gorab binds to Sas6 as a monomer to mediate centriole duplication. eLife 4 33704067
2020 Identification of compounds that bind the centriolar protein SAS-6 and inhibit its oligomerization. The Journal of biological chemistry 4 32873708
2020 Interaction interface in the C-terminal parts of centriole proteins Sas6 and Ana2. Open biology 4 33171067
2020 The Singularity of the Drosophila Male Germ Cell Centriole: The Asymmetric Distribution of Sas4 and Sas6. Cells 3 31947732
2019 A dynamically interacting flexible loop assists oligomerisation of the Caenorhabditis elegans centriolar protein SAS-6. Scientific reports 3 30837637
2025 Dynamic SAS-6 phosphorylation aids centrosome duplication and elimination in C. elegans oogenesis. EMBO reports 2 40410380
2024 Novel biallelic SASS6 variants associated with primary microcephaly and fetal growth restriction. American journal of medical genetics. Part A 2 38501757
2023 Case Report: Prenatal Recurrent Microcephaly and Corpus Callosum Abnormalities in a Chinese Family with Novel Biallelic SASS6 Mutations. Fetal diagnosis and therapy 2 36739862
2021 Optimization strategies for expression and purification of soluble N-terminal domain of human centriolar protein SAS-6 in Escherichia coli. Protein expression and purification 2 33640460
2025 Dysregulated SASS6 expression promotes increased ciliogenesis and cell invasion phenotypes. Life science alliance 1 40825584
2022 Targeting Drosophila Sas6 to mitochondria reveals its high affinity for Gorab. Biology open 1 36331102
2025 CDT1 induces the formation of polyploid giant cancer cells and promotes centrosome amplification through the PLK4/SASS6 axis. Cancer letters 0 41319860
2025 FBXW7 E3 ligase prevents centriole overduplication by degrading the Plk4 phosphorylated STIL-SAS6 cartwheel assembly. The Journal of biological chemistry 0 41453690
2023 Grand canonical Brownian dynamics simulations of adsorption and self-assembly of SAS-6 rings on a surface. The Journal of chemical physics 0 36859084