NCK belongs to family of adaptor proteins,There are two mammalian NCK genes, NCK1 and NCK2. NCK1 is located in chromosome 3 and NCK2 is located in chromosome 2. 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 transcriptionalsplice variants, encoding different isoforms, have been characterized.[3]
↑ 1.01.11.2Chen M, She H, Davis EM, Spicer CM, Kim L, Ren R, Le Beau MM, Li W (Sep 1998). "Identification of Nck family genes, chromosomal localization, expression, and signaling specificity". The Journal of Biological Chemistry. 273 (39): 25171–8. doi:10.1074/jbc.273.39.25171. PMID9737977.
↑Liu J, Li M, Ran X, Fan JS, Song J (Jun 2006). "Structural insight into the binding diversity between the human Nck2 SH3 domains and proline-rich proteins". Biochemistry. 45 (23): 7171–84. doi:10.1021/bi060091y. PMID16752908.
↑ 5.05.1Braverman LE, Quilliam LA (Feb 1999). "Identification of Grb4/Nckbeta, a src homology 2 and 3 domain-containing adapter protein having similar binding and biological properties to Nck". The Journal of Biological Chemistry. 274 (9): 5542–9. doi:10.1074/jbc.274.9.5542. PMID10026169.
↑Goicoechea SM, Tu Y, Hua Y, Chen K, Shen TL, Guan JL, Wu C (Jul 2002). "Nck-2 interacts with focal adhesion kinase and modulates cell motility". The International Journal of Biochemistry & Cell Biology. 34 (7): 791–805. doi:10.1016/s1357-2725(02)00002-x. PMID11950595.
↑Gil D, Schamel WW, Montoya M, Sánchez-Madrid F, Alarcón B (Jun 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. doi:10.1016/S0092-8674(02)00799-7. PMID12110186.
↑Suzuki S, Mizutani M, Suzuki K, Yamada M, Kojima M, Hatanaka H, Koizumi S (Jun 2002). "Brain-derived neurotrophic factor promotes interaction of the Nck2 adaptor protein with the TrkB tyrosine kinase receptor". Biochemical and Biophysical Research Communications. 294 (5): 1087–92. doi:10.1016/S0006-291X(02)00606-X. PMID12074588.
Braverman LE, Quilliam LA (Feb 1999). "Identification of Grb4/Nckbeta, a src homology 2 and 3 domain-containing adapter protein having similar binding and biological properties to Nck". The Journal of Biological Chemistry. 274 (9): 5542–9. doi:10.1074/jbc.274.9.5542. PMID10026169.
Coutinho S, Jahn T, Lewitzky M, Feller S, Hutzler P, Peschel C, Duyster J (Jul 2000). "Characterization of Ggrb4, an adapter protein interacting with Bcr-Abl". Blood. 96 (2): 618–24. PMID10887126.
Tu Y, Kucik DF, Wu C (Mar 2001). "Identification and kinetic analysis of the interaction between Nck-2 and DOCK180". FEBS Letters. 491 (3): 193–9. doi:10.1016/S0014-5793(01)02195-0. PMID11240126.
Jahn T, Seipel P, Coutinho S, Miething C, Peschel C, Duyster J (Nov 2001). "Grb4/Nckbeta acts as a nuclear repressor of v-Abl-induced transcription from c-jun/c-fos promoter elements". The Journal of Biological Chemistry. 276 (46): 43419–27. doi:10.1074/jbc.M107030200. PMID11514578.
Cowan CA, Henkemeyer M (Sep 2001). "The SH2/SH3 adaptor Grb4 transduces B-ephrin reverse signals". Nature. 413 (6852): 174–9. doi:10.1038/35093123. PMID11557983.
Goicoechea SM, Tu Y, Hua Y, Chen K, Shen TL, Guan JL, Wu C (Jul 2002). "Nck-2 interacts with focal adhesion kinase and modulates cell motility". The International Journal of Biochemistry & Cell Biology. 34 (7): 791–805. doi:10.1016/S1357-2725(02)00002-X. PMID11950595.
Suzuki S, Mizutani M, Suzuki K, Yamada M, Kojima M, Hatanaka H, Koizumi S (Jun 2002). "Brain-derived neurotrophic factor promotes interaction of the Nck2 adaptor protein with the TrkB tyrosine kinase receptor". Biochemical and Biophysical Research Communications. 294 (5): 1087–92. doi:10.1016/S0006-291X(02)00606-X. PMID12074588.
Gil D, Schamel WW, Montoya M, Sánchez-Madrid F, Alarcón B (Jun 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. doi:10.1016/S0092-8674(02)00799-7. PMID12110186.
Song J, Vranken W, Xu P, Gingras R, Noyce RS, Yu Z, Shen SH, Ni F (Sep 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. doi:10.1021/bi025815u. PMID12206665.
Aspenström P (Sep 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". Experimental Cell Research. 279 (1): 21–33. doi:10.1006/excr.2002.5576. PMID12213210.
Hafizi S, Alindri F, Karlsson R, Dahlbäck B (Dec 2002). "Interaction of Axl receptor tyrosine kinase with C1-TEN, a novel C1 domain-containing protein with homology to tensin". Biochemical and Biophysical Research Communications. 299 (5): 793–800. doi:10.1016/S0006-291X(02)02718-3. PMID12470648.
Velyvis A, Vaynberg J, Yang Y, Vinogradova O, Zhang Y, Wu C, Qin J (Jul 2003). "Structural and functional insights into PINCH LIM4 domain-mediated integrin signaling". Nature Structural Biology. 10 (7): 558–64. doi:10.1038/nsb938. PMID12794636.
Hu Y, Fang X, Dunham SM, Prada C, Stachowiak EK, Stachowiak MK (Jul 2004). "90-kDa ribosomal S6 kinase is a direct target for the nuclear fibroblast growth factor receptor 1 (FGFR1): role in FGFR1 signaling". The Journal of Biological Chemistry. 279 (28): 29325–35. doi:10.1074/jbc.M311144200. PMID15117958.
Ran X, Song J (May 2005). "Structural insight into the binding diversity between the Tyr-phosphorylated human ephrinBs and Nck2 SH2 domain". The Journal of Biological Chemistry. 280 (19): 19205–12. doi:10.1074/jbc.M500330200. PMID15764601.
Song J (Jul 2003). "Tyrosine phosphorylation of the well packed ephrinB cytoplasmic beta-hairpin for reverse signaling. Structural consequences and binding properties". The Journal of Biological Chemistry. 278 (27): 24714–20. doi:10.1074/jbc.M210625200. PMID12606549.