Affinage

BNIP2

BCL2/adenovirus E1B 19 kDa protein-interacting protein 2 · UniProt Q12982

Length
314 aa
Mass
36.0 kDa
Annotated
2026-04-28
38 papers in source corpus 18 papers cited in narrative 18 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

BNIP-2 is a BCH-domain scaffold protein that coordinates Rho GTPase signaling with cell differentiation, morphogenesis, migration, and apoptosis. Its C-terminal BCH domain directly binds Cdc42 and stimulates its GTPase activity via an arginine-patch motif, while also engaging RhoA and presenting it to regulators such as GEF-H1 and p50RhoGAP to control RhoA activation states (PMID:10799524, PMID:32789168, PMID:20660160). BNIP-2 traffics on microtubule-based vesicles through phosphatidylserine binding by its CRAL-TRIO domain and kinesin-1 (KIF5B/KLC) interaction via a WED motif, coupling its signaling scaffold function to intracellular transport required for myoblast differentiation (via Cdo–Cdc42–p38 MAPK) and cardiomyoblast differentiation (via LATS1–YAP) (PMID:25378581, PMID:25472445, PMID:18678706, PMID:35975420). BNIP-2 is a substrate of FGFR1 tyrosine kinase, which phosphorylates it to abolish its Cdc42 GAP activity, and is proteolytically cleaved by granzyme B and caspases during apoptosis, generating pro-apoptotic BCH-domain fragments (PMID:10551883, PMID:20704564, PMID:17961507).

Mechanistic history

Synthesis pass · year-by-year structured walk · 11 steps
  1. 1999 High

    Establishing that BNIP-2 is a signaling target of receptor tyrosine kinases resolved its upstream regulation: FGFR1 phosphorylates BNIP-2 on tyrosine, and this phosphorylation switches off BNIP-2's GAP-like activity toward Cdc42 and prevents its binding to Cdc42GAP.

    Evidence Yeast two-hybrid, co-IP with kinase-dead FGFR1, in vitro kinase assay with recombinant proteins, GTPase activity assay

    PMID:10551883

    Open questions at the time
    • Specific tyrosine phosphorylation sites on BNIP-2 not mapped
    • Physiological context of FGFR1–BNIP-2 signaling in tissue not established
  2. 2000 High

    Defining the BCH domain as a novel GTPase-regulatory and protein-interaction module established the core molecular mechanism of BNIP-2: the BCH domain binds Cdc42 via a 285VPMEYVGI292 motif, stimulates GTPase activity through an arginine-patch (R235/R238), and mediates homophilic and heterophilic BCH–BCH interactions through a distinct 217RRKMP221 site.

    Evidence GST pulldown, GTPase activity assay, site-directed mutagenesis, yeast two-hybrid, molecular modeling

    PMID:10799524 PMID:10954711

    Open questions at the time
    • No crystal structure of the BCH domain–Cdc42 complex
    • Whether BCH homodimerization regulates GAP activity in cells not tested
  3. 2005 High

    Demonstrating that BNIP-2 drives Cdc42-dependent cell elongation and membrane protrusions linked its biochemical activities to cell morphogenesis, establishing the BCH domain's Cdc42-binding motif as essential for morphological output.

    Evidence Overexpression with deletion/mutagenesis, dominant-negative Cdc42 blockade, fluorescence microscopy in cultured cells

    PMID:15652341

    Open questions at the time
    • Downstream effectors of Cdc42 mediating protrusion not identified
    • Endogenous loss-of-function not performed
  4. 2006 High

    Work on the BNIP-2 homolog BNIP-Sα revealed that BCH domains can also bind and activate RhoA by displacing p50RhoGAP, establishing that the BCH domain family modulates multiple Rho GTPases through sequestration of GAPs.

    Evidence Overexpression/mutagenesis, co-IP, dominant-negative RhoA rescue, cell rounding and apoptosis assays

    PMID:16331259

    Open questions at the time
    • Whether BNIP-2 itself uses the same RhoA-sequestration mechanism in the same cell types not directly shown
  5. 2007 Medium

    Identification of caspase cleavage within BNIP-2's N-terminal EF-hand motif connected BNIP-2 to apoptotic signaling, suggesting that proteolytic release of BCH-domain fragments contributes to pro-apoptotic activity.

    Evidence In vitro caspase cleavage assay, cell-based apoptosis assays, site mapping by deletion/mutagenesis

    PMID:17961507

    Open questions at the time
    • Pro-apoptotic activity of the cleaved fragment not reconstituted in isolation
    • Physiological relevance of caspase cleavage of BNIP-2 not validated in vivo
  6. 2008 High

    Placing BNIP-2 in the Cdo receptor signaling complex resolved how extracellular cues activate Cdc42–p38 MAPK to drive myogenic differentiation, establishing BNIP-2 as a differentiation scaffold bridging a cell-surface receptor to an intracellular GTPase.

    Evidence Reciprocal co-IP, siRNA knockdown and overexpression, Cdc42 and p38 activity assays, myogenic differentiation assays in C2C12 myoblasts

    PMID:18678706

    Open questions at the time
    • Structural basis of Cdo–BNIP-2 interaction unknown
    • In vivo muscle phenotype of BNIP-2 loss not assessed
  7. 2008 High

    Discovery that the BNIP-2 family member BNIPXL binds specific RhoA conformers and inhibits Lbc-driven oncogenic transformation generalized BCH-domain function to include sequestration of RhoA from RhoGEFs.

    Evidence Co-IP, GST pulldown with RhoA mutants, RhoA activity assay, transformation assay, siRNA knockdown

    PMID:18445682

    Open questions at the time
    • Whether BNIP-2 itself similarly engages Lbc not tested at this stage
  8. 2010 High

    Identification of granzyme B cleavage at IEAD28 revealed a caspase-independent route by which BNIP-2 is activated during immune-mediated killing, with both full-length and truncated BNIP-2 promoting apoptosis that then feeds into caspase-dependent cleavage.

    Evidence In vitro granzyme B cleavage with recombinant BNIP-2, NK cell cytotoxicity assay with endogenous BNIP-2, site mutagenesis, siRNA, apoptosis assays

    PMID:20704564

    Open questions at the time
    • How granzyme B-cleaved BNIP-2 mechanistically induces apoptosis not resolved
    • In vivo relevance in tumor immune surveillance not demonstrated
  9. 2014 High

    Revealing that BNIP-2 is transported by kinesin-1 (KIF5B heavy chain and KLCs) on microtubule-bound vesicles, and that this transport depends on phosphatidylserine binding by its CRAL-TRIO domain and a WED motif for KLC binding, established BNIP-2 as an actively transported signaling scaffold whose vesicular trafficking is essential for p38 MAPK activation and myogenic differentiation.

    Evidence Far-Western blot, co-IP with KIF5B/KLC, lipid-binding assay, live-cell imaging of vesicular transport, organelle marker colocalization, WED/CRAL-TRIO mutagenesis, siRNA knockdown, differentiation assays

    PMID:25378581 PMID:25472445

    Open questions at the time
    • Cargo identity of BNIP-2-containing vesicles beyond BNIP-2 itself not defined
    • Whether phosphatidylserine binding is regulated by signaling not tested
  10. 2020 High

    Demonstrating that BNIP-2 scaffolds GEF-H1 and RhoA on microtubules and that microtubule disassembly enhances BNIP-2–GEF-H1 interaction to activate RhoA resolved how BNIP-2 couples microtubule dynamics to Rho signaling, with functional consequences for cell migration.

    Evidence siRNA knockdown, co-IP, RhoA activity assay, nocodazole-induced microtubule disassembly, proximity ligation assay, live-cell migration assay in MDA-MB-231 cells

    PMID:32789168

    Open questions at the time
    • Structural basis of the tripartite BNIP-2–GEF-H1–RhoA complex not resolved
    • Whether BNIP-2 regulation of migration is relevant in vivo not assessed
  11. 2022 High

    Showing that BNIP-2 scaffolds LATS1 to phosphorylate and inactivate YAP, coupling RhoA/Myosin II-driven contractility to Hippo pathway output, established BNIP-2 as a mechanotransduction hub that promotes cardiomyoblast differentiation.

    Evidence Turbo-ID proximity labeling, super-resolution microscopy, biochemical pulldown, siRNA/overexpression, YAP phosphorylation assay, cardiomyoblast differentiation markers (cTnT, Myl2)

    PMID:35975420

    Open questions at the time
    • Whether BNIP-2 directly binds LATS1 or acts through an intermediary not fully resolved
    • In vivo cardiac phenotype of BNIP-2 loss not reported

Open questions

Synthesis pass · forward-looking unresolved questions
  • Major open questions include the structural basis of BCH domain interactions with diverse partners, whether BNIP-2 loss produces developmental phenotypes in vivo, the identity and regulation of BNIP-2-containing vesicle cargo, and how FGFR1 phosphorylation integrates with the Cdo, GEF-H1, and LATS1 scaffolding functions of BNIP-2.
  • No structural model of BCH domain with any binding partner
  • No in vivo knockout phenotype reported
  • Integration of FGFR1 phosphorylation with scaffolding functions unresolved

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0098772 molecular function regulator activity 7 GO:0060090 molecular adaptor activity 4 GO:0008289 lipid binding 1
Localization
GO:0005829 cytosol 2 GO:0005856 cytoskeleton 2 GO:0031410 cytoplasmic vesicle 2 GO:0005794 Golgi apparatus 1
Pathway
R-HSA-162582 Signal Transduction 5 R-HSA-1266738 Developmental Biology 2 R-HSA-5357801 Programmed Cell Death 2
Partners
ARHGAP1ARHGEF2CDC42CDO1FGFR1KIF5BLATS1RHOA

Evidence

Reading pass · 18 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1999 BNIP-2 is a substrate of FGF receptor-1 (FGFR1) tyrosine kinase; FGFR1 phosphorylates BNIP-2 on tyrosine residues both in cells and in vitro, and tyrosine phosphorylation of BNIP-2 prevents its binding to Cdc42GAP and abolishes its GAP-like activity toward Cdc42. Yeast two-hybrid screen, co-immunoprecipitation 'capture' experiments with kinase-dead FGFR1, in vitro kinase assay with recombinant BNIP-2 and active FGFR1, GST pulldown, GTPase activity assay The Journal of biological chemistry High 10551883
2000 The C-terminal BCH (BNIP-2 and Cdc42GAP Homology) domain of BNIP-2 binds Cdc42 and stimulates its GTPase activity via a novel arginine-patch motif (Arg-235 and Arg-238); site-directed mutagenesis of these arginines abolishes GAP activity without affecting Cdc42 binding, and a sequence 288EYV290 on BNIP-2 plus the Switch I and Rho Insert region on Cdc42 mediate binding. GST pulldown, GTPase activity assay, site-directed mutagenesis, deletion studies The Journal of biological chemistry High 10799524
2000 The BCH domain of BNIP-2 mediates homophilic (BNIP-2:BNIP-2) and heterophilic (BNIP-2:Cdc42GAP) protein-protein interactions; the region 217RRKMP221 is the major BCH–BCH interaction site, distinct from the arginine-patch required for GAP activity and the Cdc42-binding sequence 288EYV290. GST pulldown, co-immunoprecipitation, yeast two-hybrid, deletion mutagenesis, molecular modeling The Journal of biological chemistry High 10954711
2001 The BCH domain of BNIP-Salpha (a BNIP-2 homolog) is a novel apoptosis-inducing sequence; expression of the full BCH domain induces apoptosis, and deletion of the homophilic interaction motif within the BCH domain abrogates this pro-apoptotic effect. Overexpression in cells, deletion mutagenesis, apoptosis assays, co-immunoprecipitation The Journal of biological chemistry Medium 11741952
2003 BPGAP1, a novel RhoGAP containing a BCH domain, forms homophilic and heterophilic complexes with other BCH-domain proteins including BNIP-2 via their BCH domains, as shown by pulldown and co-immunoprecipitation; BPGAP1 selectively stimulates RhoA GTPase activity in vivo and induces pseudopodia and cell migration in MCF7 cells. GST pulldown, co-immunoprecipitation, fluorescence microscopy, cell migration assay, dominant-negative GTPase coexpression The Journal of biological chemistry Medium 12944407
2005 BNIP-2 induces cell elongation and membrane protrusions via its BCH domain by binding Cdc42 through a unique motif 285VPMEYVGI292; cells expressing BNIP-2 mutants lacking this motif fail to produce morphological changes, and the effect is blocked by dominant-negative Cdc42. Transient overexpression, deletion/mutagenesis, GST pulldown, dominant-negative GTPase coexpression, fluorescence microscopy Experimental cell research High 15652341
2006 BNIP-Salpha induces cell rounding and apoptosis by binding RhoA via BCH domain residues 133-177 (overlapping a RhoA switch I homology region and a REM class I RhoA-binding motif), displacing p50RhoGAP/Cdc42GAP from RhoA and thereby restoring RhoA activation; dominant-negative RhoA prevents cell rounding and apoptosis. Overexpression and mutagenesis, co-immunoprecipitation, dominant-negative GTPase coexpression, cell morphology and apoptosis assays Oncogene High 16331259
2006 Brain-specific BNIP-H/Caytaxin (a BNIP-2 family member) directly binds kidney-type glutaminase (KGA), relocalizes KGA from mitochondria to neurite terminals, and reduces steady-state glutamate levels by inhibiting KGA enzyme activity. Protein precipitation, MALDI-MS, co-immunoprecipitation with endogenous proteins, GST pulldown, immunohistochemistry, glutamate measurement in PC12 cells Journal of cell science High 16899818
2007 BNIP-2 and BNIP-XL are cleaved by caspases during apoptosis; the caspase cleavage sites on BNIP-2 are located within its N-terminal EF-hand motif, releasing BCH-domain-containing fragments proposed to contribute to pro-apoptotic activity. In vitro caspase cleavage assay, cell-based apoptosis assays, site mapping by deletion/mutagenesis Biochemical and biophysical research communications Medium 17961507
2008 During myoblast differentiation, BNIP-2 interacts with the cell surface receptor Cdo and the scaffold protein JLP (which also binds p38α/β MAPK), linking Cdo to Cdc42 activation; gain- and loss-of-function experiments show that the Cdo–BNIP-2 interaction stimulates Cdc42 activity, which in turn promotes p38α/β activity and myogenic differentiation. Co-immunoprecipitation, gain- and loss-of-function (siRNA knockdown, overexpression), p38 activity assay, Cdc42 pull-down activity assay, myogenic differentiation assays The Journal of cell biology High 18678706
2008 BNIPXL (BNIP2 Extra Long), the full contig of BMCC1, uses its BCH domain to interact with specific conformers of RhoA (fast-cycling F30L and dominant-negative T19N, but not constitutively active mutants) and with the catalytic DH-PH domains of the RhoGEF Lbc; overexpression of BNIPXL reduces active RhoA levels and inhibits Lbc-induced oncogenic transformation, while knockdown has the reverse effect. Co-immunoprecipitation, GST pulldown, RhoA activity assay, transformation assay, siRNA knockdown Journal of cell science High 18445682
2010 BNIP-2 is cleaved by granzyme B at site IEAD28 during NK cell-mediated killing of tumor cells; cleavage is caspase-independent, occurs on endogenous BNIP-2, and both full-length and the granzyme B-cleaved truncated form of BNIP-2 are pro-apoptotic and trigger subsequent caspase-dependent cleavage of BNIP-2 at a distinct site. In vitro granzyme B cleavage assay with recombinant BNIP-2, NK cell cytotoxicity assay with endogenous BNIP-2, site mutagenesis, siRNA knockdown, apoptosis assays The Biochemical journal High 20704564
2010 The BCH domain of p50RhoGAP/Cdc42GAP sequesters RhoA from inactivation by the adjacent GAP domain in cis; the BCH domain binds RhoA regardless of nucleotide state (GDP or GTP), and a RhoA-binding motif (residues 85-120) plus an intramolecular interaction motif (residues 169-197) within the BCH domain are both required for full suppression of GAP activity; deletion of the BCH domain enhances GAP activity and causes cell rounding prevented by active RhoA. BCH domain deletion mutants, site-directed mutagenesis, cell morphology assays, dominant-active RhoA rescue, co-immunoprecipitation, subcellular localization studies Molecular biology of the cell High 20660160
2014 KIF5B (kinesin-1 heavy chain) directly interacts with BNIP-2 via BNIP-2's BCH domain (binding both motor and tail domains of KIF5B); KIF5B mediates anterograde endosomal transport of BNIP-2 along microtubules, and KIF5B knockdown causes aberrant BNIP-2 aggregation and impairs p38MAPK activation and myogenic differentiation. Co-immunoprecipitation, far-Western blot, live-cell microscopy with organelle markers, dominant-negative KIF5B, siRNA knockdown, p38 activity assay, myogenic differentiation assays Molecular biology of the cell High 25378581
2014 The CRAL-TRIO/BCH domain of BNIP-2 specifically binds phosphatidylserine; this lipid interaction is required for vesicular localization of BNIP-2 (to Golgi, early and recycling endosomes, mitochondria) and for its ability to induce cell elongation and processes. BNIP-2 also interacts with kinesin light chains (KLCs) via a conserved WED motif in its N-terminal region, and KLC interaction plus kinesin-1 transport are required for BNIP-2-induced cell morphological changes. Lipid-binding assay, co-immunoprecipitation with KLC, subcellular fractionation, organelle marker colocalization, live imaging for transport speed, mutagenesis of WED motif and CRAL-TRIO domain Genes to cells High 25472445
2014 Granzyme B cleaves BNIP-2 at the IEAD28 tetrapeptide motif; extended substrate context beyond P4-P1 (particularly P1' and P3' positions) determines differential cleavage efficiency between mouse and human granzyme B, with murine granzyme B cleaving BNIP-2 more efficiently than human granzyme B despite identical IEAD tetrapeptide. In vitro kinetic degradome analysis, site-directed mutagenesis of primed-site residues, comparative cleavage assays BMC biochemistry Medium 25208769
2020 BNIP-2 scaffolds GEF-H1 and RhoA on microtubules via binding to both; upon microtubule disassembly, BNIP-2–GEF-H1 interaction increases and BNIP-2 facilitates GEF-H1-driven RhoA activation. Depletion of BNIP-2 in MDA-MB-231 breast cancer cells decreases RhoA activity, uncouples RhoA–GEF-H1 interaction, and promotes cell migration. BNIP-2 also traffics with kinesin-1 on microtubules. siRNA knockdown, co-immunoprecipitation, RhoA activity assay, nocodazole-induced microtubule disassembly, live-cell migration assay, proximity ligation assay Science advances High 32789168
2022 BNIP-2 promotes cardiomyoblast differentiation by scaffolding LATS1 to phosphorylate and inactivate YAP (increasing cytosolic YAP retention), and this requires BNIP-2-mediated activation of cellular contractility (RhoA/Myosin II). Turbo-ID proximity labeling, super-resolution imaging, and biochemical pulldown together demonstrate the BNIP-2–LATS1 scaffolding interaction. Turbo-ID proximity labeling, super-resolution microscopy, biochemical pulldown, siRNA knockdown/overexpression, YAP phosphorylation assay, cardiomyoblast differentiation assay (cTnT, Myl2 expression) Advanced science High 35975420

Source papers

Stage 0 corpus · 38 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2007 Arabidopsis NIP2;1, a major intrinsic protein transporter of lactic acid induced by anoxic stress. The Journal of biological chemistry 116 17584741
2008 A Cdo-Bnip-2-Cdc42 signaling pathway regulates p38alpha/beta MAPK activity and myogenic differentiation. The Journal of cell biology 91 18678706
2011 miR-20a targets BNIP2 and contributes chemotherapeutic resistance in colorectal adenocarcinoma SW480 and SW620 cell lines. Acta biochimica et biophysica Sinica 87 21242194
2007 Characterization of NIP2/centrobin, a novel substrate of Nek2, and its potential role in microtubule stabilization. Journal of cell science 74 17535851
2017 Monodispersed Carbon-Coated Cubic NiP2 Nanoparticles Anchored on Carbon Nanotubes as Ultra-Long-Life Anodes for Reversible Lithium Storage. ACS nano 58 28323408
2006 Brain-specific BNIP-2-homology protein Caytaxin relocalises glutaminase to neurite terminals and reduces glutamate levels. Journal of cell science 54 16899818
2020 Astrocyte-derived exosomes carry microRNA-17-5p to protect neonatal rats from hypoxic-ischemic brain damage via inhibiting BNIP-2 expression. Neurotoxicology 53 33309839
2006 Aquaporin NIP2;1 is mainly localized to the ER membrane and shows root-specific accumulation in Arabidopsis thaliana. Plant & cell physiology 45 16954136
2003 Concerted regulation of cell dynamics by BNIP-2 and Cdc42GAP homology/Sec14p-like, proline-rich, and GTPase-activating protein domains of a novel Rho GTPase-activating protein, BPGAP1. The Journal of biological chemistry 44 12944407
1999 Tyrosine phosphorylation of the Bcl-2-associated protein BNIP-2 by fibroblast growth factor receptor-1 prevents its binding to Cdc42GAP and Cdc42. The Journal of biological chemistry 42 10551883
2000 The BNIP-2 and Cdc42GAP homology domain of BNIP-2 mediates its homophilic association and heterophilic interaction with Cdc42GAP. The Journal of biological chemistry 39 10954711
2008 BNIP2 extra long inhibits RhoA and cellular transformation by Lbc RhoGEF via its BCH domain. Journal of cell science 38 18445682
2001 The BNIP-2 and Cdc42GAP homology/Sec14p-like domain of BNIP-Salpha is a novel apoptosis-inducing sequence. The Journal of biological chemistry 38 11741952
2006 BNIP-Salpha induces cell rounding and apoptosis by displacing p50RhoGAP and facilitating RhoA activation via its unique motifs in the BNIP-2 and Cdc42GAP homology domain. Oncogene 36 16331259
2000 Oestrogen prevention of neural cell death correlates with decreased expression of mRNA for the pro-apoptotic protein nip-2. Journal of neuroendocrinology 33 11069120
2005 BNIP-2 induces cell elongation and membrane protrusions by interacting with Cdc42 via a unique Cdc42-binding motif within its BNIP-2 and Cdc42GAP homology domain. Experimental cell research 32 15652341
2000 Evidence for a novel Cdc42GAP domain at the carboxyl terminus of BNIP-2. The Journal of biological chemistry 32 10799524
2001 Estrogen neuroprotection: the involvement of the Bcl-2 binding protein BNIP2. Brain research. Brain research reviews 30 11744098
2021 Aquaporin family lactic acid channel NIP2;1 promotes plant survival under low oxygen stress in Arabidopsis. Plant physiology 27 34890456
2020 BNIP-2 retards breast cancer cell migration by coupling microtubule-mediated GEF-H1 and RhoA activation. Science advances 24 32789168
2010 Centrobin/NIP2 is a microtubule stabilizer whose activity is enhanced by PLK1 phosphorylation during mitosis. The Journal of biological chemistry 24 20511645
2010 The BNIP-2 and Cdc42GAP homology (BCH) domain of p50RhoGAP/Cdc42GAP sequesters RhoA from inactivation by the adjacent GTPase-activating protein domain. Molecular biology of the cell 24 20660160
2003 BNIPL-2, a novel homologue of BNIP-2, interacts with Bcl-2 and Cdc42GAP in apoptosis. Biochemical and biophysical research communications 23 12901880
2012 Functional plasticity of the BNIP-2 and Cdc42GAP Homology (BCH) domain in cell signaling and cell dynamics. FEBS letters 22 22710163
2012 Cross-species analyses identify the BNIP-2 and Cdc42GAP homology (BCH) domain as a distinct functional subclass of the CRAL_TRIO/Sec14 superfamily. PloS one 20 22479462
2009 Nip2/centrobin may be a substrate of Nek2 that is required for proper spindle assembly during mitosis in early mouse embryos. Molecular reproduction and development 20 19117032
2020 The grapevine NIP2;1 aquaporin is a silicon channel. Journal of experimental botany 17 32584998
2007 Cleavage of BNIP-2 and BNIP-XL by caspases. Biochemical and biophysical research communications 17 17961507
2014 KIF5B transports BNIP-2 to regulate p38 mitogen-activated protein kinase activation and myoblast differentiation. Molecular biology of the cell 16 25378581
2010 Nek2 and its substrate, centrobin/Nip2, are required for proper meiotic spindle formation of the mouse oocytes. Zygote (Cambridge, England) 15 20569513
2010 Identification of the BCL2/adenovirus E1B-19K protein-interacting protein 2 (BNIP-2) as a granzyme B target during human natural killer cell-mediated killing. The Biochemical journal 12 20704564
2000 Expression of the estrogen-regulated gene Nip2 during rat brain maturation. International journal of developmental neuroscience : the official journal of the International Society for Developmental Neuroscience 12 10715586
2022 BNIP-2 Activation of Cellular Contractility Inactivates YAP for H9c2 Cardiomyoblast Differentiation. Advanced science (Weinheim, Baden-Wurttemberg, Germany) 11 35975420
2009 Pro-apoptotic activity of mBNIP-21 depends on its BNIP-2 and Cdc42GAP homology (BCH) domain and is enhanced by coxsackievirus B3 infection. Cellular microbiology 10 19951366
2022 Superhydrophilic/Superaerophobic Hierarchical NiP2@MoO2/Co(Ni)MoO4 Core-Shell Array Electrocatalysts for Efficient Hydrogen Production at Large Current Densities. ACS applied materials & interfaces 9 35469395
2009 Centrobin/Nip2 expression in vivo suggests its involvement in cell proliferation. Molecules and cells 6 19533028
2014 Importance of extended protease substrate recognition motifs in steering BNIP-2 cleavage by human and mouse granzymes B. BMC biochemistry 4 25208769
2014 BNIP-2 binds phosphatidylserine, localizes to vesicles, and is transported by kinesin-1. Genes to cells : devoted to molecular & cellular mechanisms 3 25472445