NCK1

Cytoplasmic protein NCK1 is a protein that in humans is encoded by the NCK1 gene.[5][6]

NCK1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2CI8, 2CI9, 2JS0, 2JS2, 2JW4
Identifiers
Aliases	NCK1, NCK, NCKalpha, nck-1, NCK adaptor protein 1
External IDs	OMIM: 600508 MGI: 109601 HomoloGene: 38148 GeneCards: NCK1
Gene location (Human) Chr. Chromosome 3 (human)[1] Band 3q22.3 Start 136,862,208 bp[1] End 136,951,606 bp[1]
Gene location (Mouse) Chr. Chromosome 9 (mouse)[2] Band 9|9 E3.3 Start 100,492,293 bp[2] End 100,546,134 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • protein binding, bridging • protein domain specific binding • receptor tyrosine kinase binding • protein kinase inhibitor activity • GO:0001948 protein binding • cytoskeletal adaptor activity • receptor signaling complex scaffold activity • receptor binding • eukaryotic initiation factor eIF2 binding • ephrin receptor binding • cadherin binding • GO:0032947 molecular adaptor activity Cellular component • cytosol • ribosome • intercellular junction • vesicle membrane • protein phosphatase type 1 complex • endoplasmic reticulum • cell nucleus • cytoplasm • cell membrane Biological process • positive regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway • Fc-gamma receptor signaling pathway involved in phagocytosis • actin filament organization • positive regulation of translation in response to endoplasmic reticulum stress • substrate-dependent cell migration, cell extension • signal complex assembly • negative regulation of cell death • positive regulation of cap-independent translational initiation • positive regulation of cap-dependent translational initiation • peptidyl-serine dephosphorylation • vascular endothelial growth factor receptor signaling pathway • response to other organism • positive regulation of T cell proliferation • negative regulation of peptidyl-serine phosphorylation • negative regulation of endoplasmic reticulum stress-induced eIF2 alpha phosphorylation • T cell receptor signaling pathway • negative regulation of PERK-mediated unfolded protein response • cell migration • negative regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress • regulation of translation • T cell activation • lamellipodium assembly • positive regulation of transcription from RNA polymerase II promoter • negative regulation of protein kinase activity • positive regulation of actin filament polymerization • regulation of cell migration • ephrin receptor signaling pathway • positive regulation of neuron projection development • negative regulation of insulin receptor signaling pathway Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	4690	17973
Ensembl	ENSG00000158092	ENSMUSG00000032475
UniProt	P16333	Q99M51
RefSeq (mRNA)	NM_006153 NM_001190796 NM_001291999	NM_010878 NM_001324530
RefSeq (protein)	NP_001177725 NP_001278928 NP_006144	NP_001311459 NP_035008
Location (UCSC)	Chr 3: 136.86 – 136.95 Mb	Chr 9: 100.49 – 100.55 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Gene

The Nck (non-catalytic region of tyrosine kinase adaptor protein 1) belongs to the adaptor family of proteins. The nck gene was initially isolated from a human melanoma cDNA library using a monoclonal antibody produced against the human melanoma-associated antigen. The Nck family has two known members in human cells (Nck-1/Nckalpha and NcK2/NcKbeta), two in mouse cells (mNckalpha and mNckbeta/Grb4) and one in drosophila (Dock means dreadlocks-ortholog).

The two murine gene products exhibit 68% amino acid identity to one another, with most of the sequence variation being located to the linker regions between the SH3 and SH2 domains, and are 96% identical to their human counterparts. While human nck-1 gene has been localised to the 3q21 locus of chromosome 3, the nck-2 gene can be found on chromosome 2 at the 2q12 locus.

Function

The protein encoded by this gene is one of the signaling and transforming proteins containing Src homology 2 and 3 (SH2 and SH3) domains. It is located in the cytoplasm and is an adaptor protein involved in transducing signals from receptor tyrosine kinases to downstream signal recipients such as RAS.[7]

Nck1 has been linked to glucose tolerance and insulin signaling within certain tissues, namely the liver, in obese mice. A deletion of the protein also causes a decrease of ER stress signaling within these obese cells, which is normally increased by the excessive fat. This stress causes expression of the unfolded protein response pathway, which leads to a decrease in glucose tolerance and inactivation of insulin signaling in certain cell types. This renewed glucose tolerance and insulin signaling is caused by the inhibition of the unfolded protein response pathway, particularly the protein IRE1alpha, and its subsequent phosphorylation of IRS-1 that causes insulin signaling to be blocked. IRE1alpha is involved with the JNK pathway that is responsible for the phosphorylation of IRS-1. Nck1 regulates the activation of IRE1alpha within the pathway and when removed from the pathway disrupts activation. This means that Nck1 has an interaction with the UPR and that a deletion can cause a decrease in the stress pathway from the ER in the mice. These deficient, obese mice also show increased insulin-induced phosphorylation of PKB within the liver but do not possess the same expression in adipose tissues or skeletal muscles. This evidence points to the pathway being ER stress induced within liver tissue.[8]

Nck1 has been shown to be associated with bone mass. A deficiency in Nck1, which is shown to reduce ER stress in obese mice, also accelerates unloading-induced osteoporosis caused by mechanical stress. This seems to suggest that would be a crucial protein involved with bone metabolism and that retention of bone tissue by a protein as yet unknown. Nck1 expression increased twofold when involved with neurectomy-based unloading osteoporosis. This then follows that in a deficient organism this upregulation would not be possible and thus the body would have increased bone loss due to the lack of expression of Nck1 to deal with the stress, which is what happens in vivo. This acceleration of bone loss leads researchers to believe that the pathway for bone metabolism is highly regulated by several proteins that have yet to be discovered or incorporated into a schema.[9]

Nck1 is involved with cellular remodeling via the WASp/Arp2/3 complex to coordinate actin cytoskeletal remodeling. The WASp binds to the SH3 domains within the N-terminus of the protein and after Nck1 has been activated by the signal from the ligand binding to a receptor tyrosine kinase and then uses the WASp/Arp2/3 complex to reorganize the actin cytoskeleton and cause the polarization of the cell as well as promote directional migration via pseudopodia. The reorganization of this cytoskeleton is caused by different Rho GTPases being moved to different locations within the cell, primarily to the leading edge, and strengthening the bonds with extracellular matrix components to induce motion.[10]

Interactions

NCK1 has been shown to interact with:

• ABL1,[11][12]
• CBL,[11][13]
• DNM1,[14]
• DAG1,[15]
• EIF2B2,[16]
• EPHB1,[17]
• EGFR,[18][19]
• KHDRBS1,[18][20]
• LCP2,[21][22]
• MAP4K1,[23][24]
• MAP4K4,[25]
• MINK1,[26]
• NCKIPSD,[27]
• NEDD9,[28]
• PAK1,[29][30][31]
• PDGFRB,[19][29]
• PKN2,[29][32]
• PTK2,[28][33]
• RASA1,[34]
• RICS,[35]
• RRAS,[36]
• SOCS7,[17]
• SOS1,[14][29][37][38]
• TBK1,[39]
• WASL,[40]
• WIPF1,[41] and
• WAS.[29][42][43][44]

See also

• Signal transducing adaptor protein
• Receptor tyrosine kinase
• Ras superfamily

References

1. GRCh38: Ensembl release 89: ENSG00000158092 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000032475 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Huebner K, Kastury K, Druck T, Salcini AE, Lanfrancone L, Pelicci G, Lowenstein E, Li W, Park SH, Cannizzaro L (January 1995). "Chromosome locations of genes encoding human signal transduction adapter proteins, Nck (NCK), Shc (SHC1), and Grb2 (GRB2)". Genomics. 22 (2): 281–7. doi:10.1006/geno.1994.1385. PMID 7806213.
6. Chen M, She H, Davis EM, Spicer CM, Kim L, Ren R, Le Beau MM, Li W (October 1998). "Identification of Nck family genes, chromosomal localization, expression, and signaling specificity". J Biol Chem. 273 (39): 25171–8. doi:10.1074/jbc.273.39.25171. PMID 9737977.
7. "Entrez Gene: NCK1 NCK adaptor protein 1".
8. Latreille , M., Laberge, M., Bourret, G., Yamani, L., & Larose, L. (2011). Deletion of Nck1 attenuates hepatic ER stress signaling and improves glucose tolerance and insulin signaling in liver of obese mice. American Journal of Physiology, 300(3), 423-424-434.
9. Aryal, A. C., Miyai, K., Hayata, T., Notomi, T., Nakamoto, T., Pawson, T., et al. (2013). Nck1 deficiency accelerates unloading-induced bone loss.. Journal of Cell Physiology, 228(7), 1397-1398-1403.
10. Chaki, S. P., & Rivera, G. M. (2013 May-Jun). Integration of signaling and cytoskeletal remodeling by nck in directional cell migration. [Integration of signaling and cytoskeletal remodeling by Nck in directional cell migration.] Bioarchitecture, 3(3), 57-58-63.
11. Miyoshi-Akiyama T, Aleman LM, Smith JM, Adler CE, Mayer BJ (July 2001). "Regulation of Cbl phosphorylation by the Abl tyrosine kinase and the Nck SH2/SH3 adaptor". Oncogene. 20 (30): 4058–69. doi:10.1038/sj.onc.1204528. PMID 11494134.
12. Ren R, Ye ZS, Baltimore D (April 1994). "Abl protein-tyrosine kinase selects the Crk adapter as a substrate using SH3-binding sites". Genes Dev. 8 (7): 783–95. doi:10.1101/gad.8.7.783. PMID 7926767.
13. Erdreich-Epstein A, Liu M, Kant AM, Izadi KD, Nolta JA, Durden DL (April 1999). "Cbl functions downstream of Src kinases in Fc gamma RI signaling in primary human macrophages". J. Leukoc. Biol. 65 (4): 523–34. doi:10.1002/jlb.65.4.523. PMID 10204582. S2CID 18340540.
14. Wunderlich L, Faragó A, Buday L (January 1999). "Characterization of interactions of Nck with Sos and dynamin". Cell. Signal. 11 (1): 25–9. doi:10.1016/S0898-6568(98)00027-8. PMID 10206341.
15. Sotgia F, Lee H, Bedford MT, Petrucci T, Sudol M, Lisanti MP (December 2001). "Tyrosine phosphorylation of beta-dystroglycan at its WW domain binding motif, PPxY, recruits SH2 domain containing proteins". Biochemistry. 40 (48): 14585–92. doi:10.1021/bi011247r. PMID 11724572.
16. Kebache S, Zuo D, Chevet E, Larose L (April 2002). "Modulation of protein translation by Nck-1". Proc. Natl. Acad. Sci. U.S.A. 99 (8): 5406–11. Bibcode:2002PNAS...99.5406K. doi:10.1073/pnas.082483399. PMC 122782. PMID 11959995.
17. Matuoka K, Miki H, Takahashi K, Takenawa T (October 1997). "A novel ligand for an SH3 domain of the adaptor protein Nck bears an SH2 domain and nuclear signaling motifs". Biochem. Biophys. Res. Commun. 239 (2): 488–92. doi:10.1006/bbrc.1997.7492. PMID 9344857.
18. Tang J, Feng GS, Li W (October 1997). "Induced direct binding of the adapter protein Nck to the GTPase-activating protein-associated protein p62 by epidermal growth factor". Oncogene. 15 (15): 1823–32. doi:10.1038/sj.onc.1201351. PMID 9362449.
19. Li W, Hu P, Skolnik EY, Ullrich A, Schlessinger J (December 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. doi:10.1128/MCB.12.12.5824. PMC 360522. PMID 1333047.
20. Lawe DC, Hahn C, Wong AJ (January 1997). "The Nck SH2/SH3 adaptor protein is present in the nucleus and associates with the nuclear protein SAM68". Oncogene. 14 (2): 223–31. doi:10.1038/sj.onc.1200821. PMID 9010224.
21. Shim EK, Moon CS, Lee GY, Ha YJ, Chae SK, Lee JR (September 2004). "Association of the Src homology 2 domain-containing leukocyte phosphoprotein of 76 kD (SLP-76) with the p85 subunit of phosphoinositide 3-kinase". FEBS Lett. 575 (1–3): 35–40. doi:10.1016/j.febslet.2004.07.090. PMID 15388330. S2CID 24678709.
22. Wunderlich L, Faragó A, Downward J, Buday L (April 1999). "Association of Nck with tyrosine-phosphorylated SLP-76 in activated T lymphocytes". Eur. J. Immunol. 29 (4): 1068–75. doi:10.1002/(SICI)1521-4141(199904)29:04<1068::AID-IMMU1068>3.0.CO;2-P. PMID 10229072.
23. Ling P, Yao Z, Meyer CF, Wang XS, Oehrl W, Feller SM, Tan TH (February 1999). "Interaction of hematopoietic progenitor kinase 1 with adapter proteins Crk and CrkL leads to synergistic activation of c-Jun N-terminal kinase". Mol. Cell. Biol. 19 (2): 1359–68. doi:10.1128/MCB.19.2.1359. PMC 116064. PMID 9891069.
24. Ling P, Meyer CF, Redmond LP, Shui JW, Davis B, Rich RR, Hu MC, Wange RL, Tan TH (June 2001). "Involvement of hematopoietic progenitor kinase 1 in T cell receptor signaling". J. Biol. Chem. 276 (22): 18908–14. doi:10.1074/jbc.M101485200. PMID 11279207.
25. Su YC, Han J, Xu S, Cobb M, Skolnik EY (March 1997). "NIK is a new Ste20-related kinase that binds NCK and MEKK1 and activates the SAPK/JNK cascade via a conserved regulatory domain". EMBO J. 16 (6): 1279–90. doi:10.1093/emboj/16.6.1279. PMC 1169726. PMID 9135144.
26. Hu Y, Leo C, Yu S, Huang BC, Wang H, Shen M, Luo Y, Daniel-Issakani S, Payan DG, Xu X (December 2004). "Identification and functional characterization of a novel human misshapen/Nck interacting kinase-related kinase, hMINK beta". J. Biol. Chem. 279 (52): 54387–97. doi:10.1074/jbc.M404497200. PMID 15469942.
27. Lim CS, Park ES, Kim DJ, Song YH, Eom SH, Chun JS, Kim JH, Kim JK, Park D, Song WK (April 2001). "SPIN90 (SH3 protein interacting with Nck, 90 kDa), an adaptor protein that is developmentally regulated during cardiac myocyte differentiation". J. Biol. Chem. 276 (16): 12871–8. doi:10.1074/jbc.M009411200. PMID 11278500.
28. Minegishi M, Tachibana K, Sato T, Iwata S, Nojima Y, Morimoto C (October 1996). "Structure and function of Cas-L, a 105-kD Crk-associated substrate-related protein that is involved in beta 1 integrin-mediated signaling in lymphocytes". J. Exp. Med. 184 (4): 1365–75. doi:10.1084/jem.184.4.1365. PMC 2192828. PMID 8879209.
29. Braverman LE, Quilliam LA (February 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. doi:10.1074/jbc.274.9.5542. PMID 10026169.
30. Ku GM, Yablonski D, Manser E, Lim L, Weiss A (February 2001). "A PAK1-PIX-PKL complex is activated by the T-cell receptor independent of Nck, Slp-76 and LAT". EMBO J. 20 (3): 457–65. doi:10.1093/emboj/20.3.457. PMC 133476. PMID 11157752.
31. Bokoch GM, Wang Y, Bohl BP, Sells MA, Quilliam LA, Knaus UG (October 1996). "Interaction of the Nck adapter protein with p21-activated kinase (PAK1)". J. Biol. Chem. 271 (42): 25746–9. doi:10.1074/jbc.271.42.25746. PMID 8824201.
32. Quilliam LA, Lambert QT, Mickelson-Young LA, Westwick JK, Sparks AB, Kay BK, Jenkins NA, Gilbert DJ, Copeland NG, Der CJ (November 1996). "Isolation of a NCK-associated kinase, PRK2, an SH3-binding protein and potential effector of Rho protein signaling". J. Biol. Chem. 271 (46): 28772–6. doi:10.1074/jbc.271.46.28772. PMID 8910519.
33. Goicoechea SM, Tu Y, Hua Y, Chen K, Shen TL, Guan JL, Wu C (July 2002). "Nck-2 interacts with focal adhesion kinase and modulates cell motility". Int. J. Biochem. Cell Biol. 34 (7): 791–805. doi:10.1016/S1357-2725(02)00002-X. PMID 11950595.
34. Ger M, Zitkus Z, Valius M (October 2011). "Adaptor protein Nck1 interacts with p120 Ras GTPase-activating protein and regulates its activity". Cell. Signal. 23 (10): 1651–8. doi:10.1016/j.cellsig.2011.05.019. PMID 21664272.
35. Zhao C, Ma H, Bossy-Wetzel E, Lipton SA, Zhang Z, Feng GS (September 2003). "GC-GAP, a Rho family GTPase-activating protein that interacts with signaling adapters Gab1 and Gab2". J. Biol. Chem. 278 (36): 34641–53. doi:10.1074/jbc.M304594200. PMID 12819203.
36. Wang B, Zou JX, Ek-Rylander B, Ruoslahti E (February 2000). "R-Ras contains a proline-rich site that binds to SH3 domains and is required for integrin activation by R-Ras". J. Biol. Chem. 275 (7): 5222–7. doi:10.1074/jbc.275.7.5222. PMID 10671570.
37. Hu Q, Milfay D, Williams LT (March 1995). "Binding of NCK to SOS and activation of ras-dependent gene expression". Mol. Cell. Biol. 15 (3): 1169–74. doi:10.1128/MCB.15.3.1169. PMC 230339. PMID 7862111.
38. Okada S, Pessin JE (October 1996). "Interactions between Src homology (SH) 2/SH3 adapter proteins and the guanylnucleotide exchange factor SOS are differentially regulated by insulin and epidermal growth factor". J. Biol. Chem. 271 (41): 25533–8. doi:10.1074/jbc.271.41.25533. PMID 8810325.
39. Chou MM, Hanafusa H (March 1995). "A novel ligand for SH3 domains. The Nck adaptor protein binds to a serine/threonine kinase via an SH3 domain". J. Biol. Chem. 270 (13): 7359–64. doi:10.1074/jbc.270.13.7359. PMID 7706279.
40. Rohatgi R, Nollau P, Ho HY, Kirschner MW, Mayer BJ (July 2001). "Nck and phosphatidylinositol 4,5-bisphosphate synergistically activate actin polymerization through the N-WASP-Arp2/3 pathway". J. Biol. Chem. 276 (28): 26448–52. doi:10.1074/jbc.M103856200. PMID 11340081.
41. Antón IM, Lu W, Mayer BJ, Ramesh N, Geha RS (August 1998). "The Wiskott-Aldrich syndrome protein-interacting protein (WIP) binds to the adaptor protein Nck". J. Biol. Chem. 273 (33): 20992–5. doi:10.1074/jbc.273.33.20992. PMID 9694849.
42. Krause M, Sechi AS, Konradt M, Monner D, Gertler FB, Wehland J (April 2000). "Fyn-binding protein (Fyb)/SLP-76-associated protein (SLAP), Ena/vasodilator-stimulated phosphoprotein (VASP) proteins and the Arp2/3 complex link T cell receptor (TCR) signaling to the actin cytoskeleton". J. Cell Biol. 149 (1): 181–94. doi:10.1083/jcb.149.1.181. PMC 2175102. PMID 10747096.
43. Okabe S, Fukuda S, Broxmeyer HE (July 2002). "Activation of Wiskott-Aldrich syndrome protein and its association with other proteins by stromal cell-derived factor-1alpha is associated with cell migration in a T-lymphocyte line". Exp. Hematol. 30 (7): 761–6. doi:10.1016/S0301-472X(02)00823-8. PMID 12135674.
44. Rivero-Lezcano OM, Marcilla A, Sameshima JH, Robbins KC (October 1995). "Wiskott-Aldrich syndrome protein physically associates with Nck through Src homology 3 domains". Mol. Cell. Biol. 15 (10): 5725–31. doi:10.1128/MCB.15.10.5725. PMC 230823. PMID 7565724.

Further reading

• Iwata S, Ohashi Y, Kamiguchi K, Morimoto C (2000). "Beta 1-integrin-mediated cell signaling in T lymphocytes". J. Dermatol. Sci. 23 (2): 75–86. doi:10.1016/S0923-1811(99)00096-1. PMID 10808124.
• Park D, Rhee SG (1992). "Phosphorylation of Nck in response to a variety of receptors, phorbol myristate acetate, and cyclic AMP". Mol. Cell. Biol. 12 (12): 5816–23. doi:10.1128/MCB.12.12.5816. PMC 360521. PMID 1333046.
• Meisenhelder J, Hunter T (1992). "The SH2/SH3 domain-containing protein Nck is recognized by certain anti-phospholipase C-gamma 1 monoclonal antibodies, and its phosphorylation on tyrosine is stimulated by platelet-derived growth factor and epidermal growth factor treatment". Mol. Cell. Biol. 12 (12): 5843–56. doi:10.1128/MCB.12.12.5843. PMC 360524. PMID 1448108.
• Lehmann JM, Riethmüller G, Johnson JP (1990). "Nck, a melanoma cDNA encoding a cytoplasmic protein consisting of the src homology units SH2 and SH3". Nucleic Acids Res. 18 (4): 1048. doi:10.1093/nar/18.4.1048. PMC 330365. PMID 2107526.
• Rivero-Lezcano OM, Sameshima JH, Marcilla A, Robbins KC (1994). "Physical association between Src homology 3 elements and the protein product of the c-cbl proto-oncogene". J. Biol. Chem. 269 (26): 17363–6. PMID 7517397.
• Rivero-Lezcano OM, Marcilla A, Sameshima JH, Robbins KC (1995). "Wiskott-Aldrich syndrome protein physically associates with Nck through Src homology 3 domains". Mol. Cell. Biol. 15 (10): 5725–31. doi:10.1128/MCB.15.10.5725. PMC 230823. PMID 7565724.
• Chou MM, Hanafusa H (1995). "A novel ligand for SH3 domains. The Nck adaptor protein binds to a serine/threonine kinase via an SH3 domain". J. Biol. Chem. 270 (13): 7359–64. doi:10.1074/jbc.270.13.7359. PMID 7706279.
• Hu Q, Milfay D, Williams LT (1995). "Binding of NCK to SOS and activation of ras-dependent gene expression". Mol. Cell. Biol. 15 (3): 1169–74. doi:10.1128/MCB.15.3.1169. PMC 230339. PMID 7862111.
• Vorobieva N, Protopopov A, Protopopova M, Kashuba V, Allikmets RL, Modi W, Zabarovsky ER, Klein G, Kisselev L, Graphodatsky A (1994). "Localization of human ARF2 and NCK genes and 13 other NotI-linking clones to chromosome 3 by fluorescence in situ hybridization". Cytogenet. Cell Genet. 68 (1–2): 91–4. doi:10.1159/000133898. PMID 7956370.
• Kitamura T, Kitamura Y, Yonezawa K, Totty NF, Gout I, Hara K, Waterfield MD, Sakaue M, Ogawa W, Kasuga M (1996). "Molecular cloning of p125Nap1, a protein that associates with an SH3 domain of Nck". Biochem. Biophys. Res. Commun. 219 (2): 509–14. doi:10.1006/bbrc.1996.0264. PMID 8605018.
• Okada S, Pessin JE (1996). "Interactions between Src homology (SH) 2/SH3 adapter proteins and the guanylnucleotide exchange factor SOS are differentially regulated by insulin and epidermal growth factor". J. Biol. Chem. 271 (41): 25533–8. doi:10.1074/jbc.271.41.25533. PMID 8810325.
• Bokoch GM, Wang Y, Bohl BP, Sells MA, Quilliam LA, Knaus UG (1996). "Interaction of the Nck adapter protein with p21-activated kinase (PAK1)". J. Biol. Chem. 271 (42): 25746–9. doi:10.1074/jbc.271.42.25746. PMID 8824201.
• Minegishi M, Tachibana K, Sato T, Iwata S, Nojima Y, Morimoto C (1996). "Structure and function of Cas-L, a 105-kD Crk-associated substrate-related protein that is involved in beta 1 integrin-mediated signaling in lymphocytes". J. Exp. Med. 184 (4): 1365–75. doi:10.1084/jem.184.4.1365. PMC 2192828. PMID 8879209.
• Roche S, McGlade J, Jones M, Gish GD, Pawson T, Courtneidge SA (1996). "Requirement of phospholipase C gamma, the tyrosine phosphatase Syp and the adaptor proteins Shc and Nck for PDGF-induced DNA synthesis: evidence for the existence of Ras-dependent and Ras-independent pathways". EMBO J. 15 (18): 4940–8. doi:10.1002/j.1460-2075.1996.tb00874.x. PMC 452231. PMID 8890167.
• Quilliam LA, Lambert QT, Mickelson-Young LA, Westwick JK, Sparks AB, Kay BK, Jenkins NA, Gilbert DJ, Copeland NG, Der CJ (1997). "Isolation of a NCK-associated kinase, PRK2, an SH3-binding protein and potential effector of Rho protein signaling". J. Biol. Chem. 271 (46): 28772–6. doi:10.1074/jbc.271.46.28772. PMID 8910519.
• Lussier G, Larose L (1997). "A casein kinase I activity is constitutively associated with Nck". J. Biol. Chem. 272 (5): 2688–94. doi:10.1074/jbc.272.5.2688. PMID 9006905.
• Lawe DC, Hahn C, Wong AJ (1997). "The Nck SH2/SH3 adaptor protein is present in the nucleus and associates with the nuclear protein SAM68". Oncogene. 14 (2): 223–31. doi:10.1038/sj.onc.1200821. PMID 9010224.
• Lu W, Katz S, Gupta R, Mayer BJ (1997). "Activation of Pak by membrane localization mediated by an SH3 domain from the adaptor protein Nck". Curr. Biol. 7 (2): 85–94. doi:10.1016/S0960-9822(06)00052-2. PMID 9024622. S2CID 16173970.
• Su YC, Han J, Xu S, Cobb M, Skolnik EY (1997). "NIK is a new Ste20-related kinase that binds NCK and MEKK1 and activates the SAPK/JNK cascade via a conserved regulatory domain". EMBO J. 16 (6): 1279–90. doi:10.1093/emboj/16.6.1279. PMC 1169726. PMID 9135144.

External links

• Nck1 Info with links in the Cell Migration Gateway