NCK2

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NCK adaptor protein 2
File:PBB Protein NCK2 image.jpg
PDB rendering based on 1u5s.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols NCK2 ; GRB4; NCKbeta
External IDs Template:OMIM5 Template:MGI HomoloGene20794
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

NCK adaptor protein 2, also known as NCK2, is a human gene.[1]

This gene encodes a member of the NCK family of adaptor proteins. The protein contains three SH3 domains and one SH2 domain. The protein has no known catalytic function but has been shown to bind and recruit various proteins involved in the regulation of receptor protein tyrosine kinases. It is through these regulatory activities that this protein is believed to be involved in cytoskeletal reorganization. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.[1]

References

  1. 1.0 1.1 "Entrez Gene: NCK2 NCK adaptor protein 2".

Further reading

  • Li W, Hu P, Skolnik EY; et al. (1992). "The SH2 and SH3 domain-containing Nck protein is oncogenic and a common target for phosphorylation by different surface receptors". Mol. Cell. Biol. 12 (12): 5824–33. PMID 1333047.
  • Chen M, She H, Davis EM; et al. (1998). "Identification of Nck family genes, chromosomal localization, expression, and signaling specificity". J. Biol. Chem. 273 (39): 25171–8. PMID 9737977.
  • Tu Y, Li F, Wu C (1999). "Nck-2, a novel Src homology2/3-containing adaptor protein that interacts with the LIM-only protein PINCH and components of growth factor receptor kinase-signaling pathways". Mol. Biol. Cell. 9 (12): 3367–82. PMID 9843575.
  • Tu Y, Li F, Goicoechea S, Wu C (1999). "The LIM-only protein PINCH directly interacts with integrin-linked kinase and is recruited to integrin-rich sites in spreading cells". Mol. Cell. Biol. 19 (3): 2425–34. PMID 10022929.
  • Braverman LE, Quilliam LA (1999). "Identification of Grb4/Nckbeta, a src homology 2 and 3 domain-containing adapter protein having similar binding and biological properties to Nck". J. Biol. Chem. 274 (9): 5542–9. PMID 10026169.
  • Coutinho S, Jahn T, Lewitzky M; et al. (2000). "Characterization of Ggrb4, an adapter protein interacting with Bcr-Abl". Blood. 96 (2): 618–24. PMID 10887126.
  • Chen M, She H, Kim A; et al. (2000). "Nckbeta adapter regulates actin polymerization in NIH 3T3 fibroblasts in response to platelet-derived growth factor bb". Mol. Cell. Biol. 20 (21): 7867–80. PMID 11027258.
  • Tu Y, Kucik DF, Wu C (2001). "Identification and kinetic analysis of the interaction between Nck-2 and DOCK180". FEBS Lett. 491 (3): 193–9. PMID 11240126.
  • Jahn T, Seipel P, Coutinho S; et al. (2001). "Grb4/Nckbeta acts as a nuclear repressor of v-Abl-induced transcription from c-jun/c-fos promoter elements". J. Biol. Chem. 276 (46): 43419–27. doi:10.1074/jbc.M107030200. PMID 11514578.
  • Cowan CA, Henkemeyer M (2001). "The SH2/SH3 adaptor Grb4 transduces B-ephrin reverse signals". Nature. 413 (6852): 174–9. doi:10.1038/35093123. PMID 11557983.
  • Goicoechea SM, Tu Y, Hua Y; et al. (2002). "Nck-2 interacts with focal adhesion kinase and modulates cell motility". Int. J. Biochem. Cell Biol. 34 (7): 791–805. PMID 11950595.
  • Suzuki S, Mizutani M, Suzuki K; et al. (2002). "Brain-derived neurotrophic factor promotes interaction of the Nck2 adaptor protein with the TrkB tyrosine kinase receptor". Biochem. Biophys. Res. Commun. 294 (5): 1087–92. doi:10.1016/S0006-291X(02)00606-X. PMID 12074588.
  • Gil D, Schamel WW, Montoya M; et al. (2002). "Recruitment of Nck by CD3 epsilon reveals a ligand-induced conformational change essential for T cell receptor signaling and synapse formation". Cell. 109 (7): 901–12. PMID 12110186.
  • Song J, Vranken W, Xu P; et al. (2002). "Solution structure and backbone dynamics of the functional cytoplasmic subdomain of human ephrin B2, a cell-surface ligand with bidirectional signaling properties". Biochemistry. 41 (36): 10942–9. PMID 12206665.
  • Aspenström P (2002). "The WASP-binding protein WIRE has a role in the regulation of the actin filament system downstream of the platelet-derived growth factor receptor". Exp. Cell Res. 279 (1): 21–33. PMID 12213210.
  • Hafizi S, Alindri F, Karlsson R, Dahlbäck B (2003). "Interaction of Axl receptor tyrosine kinase with C1-TEN, a novel C1 domain-containing protein with homology to tensin". Biochem. Biophys. Res. Commun. 299 (5): 793–800. PMID 12470648.
  • Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
  • Velyvis A, Vaynberg J, Yang Y; et al. (2003). "Structural and functional insights into PINCH LIM4 domain-mediated integrin signaling". Nat. Struct. Biol. 10 (7): 558–64. doi:10.1038/nsb938. PMID 12794636.
  • Hu Y, Fang X, Dunham SM; et al. (2004). "90-kDa ribosomal S6 kinase is a direct target for the nuclear fibroblast growth factor receptor 1 (FGFR1): role in FGFR1 signaling". J. Biol. Chem. 279 (28): 29325–35. doi:10.1074/jbc.M311144200. PMID 15117958.
  • Liu J, Li M, Ran X, Fan JS, Song J. (2006). "Structural insight into the binding diversity between the human Nck2 SH3 domains and proline-rich proteins". Biochemistry. 45 (23): 7171-84. PMID 16752908.
  • Ran X, Song J. (2005). "Structural insight into the binding diversity between the Tyr-phosphorylated human ephrinBs and Nck2 SH2 domain". J Biol Chem. 280 (19): 19205-12. PMID 15764601.
  • Song J. (2003). "Tyrosine phosphorylation of the well packed ephrinB cytoplasmic beta-hairpin for reverse signaling. Structural consequences and binding properties". J Biol Chem. 278 (27): 24714-20. PMID 12606549.

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