Biology:Adapter molecule crk
Generic protein structure example |
Adapter molecule crk also known as proto-oncogene c-Crk is a protein that in humans is encoded by the CRK gene.[1]
The CRK protein participates in the Reelin signaling cascade downstream of DAB1.[2][3]
Function
Adapter molecule crk is a member of an adapter protein family that binds to several tyrosine-phosphorylated proteins. This protein has several SH2 and SH3 domains (src-homology domains) and is involved in several signaling pathways, recruiting cytoplasmic proteins in the vicinity of tyrosine kinase through SH2-phosphotyrosine interaction. The N-terminal SH2 domain of this protein functions as a positive regulator of transformation whereas the C-terminal SH3 domain functions as a negative regulator of transformation. Two alternative transcripts encoding different isoforms with distinct biological activity have been described.[4]
Crk together with CrkL participates in the Reelin signaling cascade downstream of DAB1.[2][3]
v-Crk, a transforming oncoprotein from avian sarcoma viruses, is a fusion of viral "gag" protein with the SH2 and SH3 domains of cellular Crk.[5] The name Crk is from "CT10 Regulator of Kinase" where CT10 is the avian virus from which was isolated a protein, lacking kinase domains, but capable of stimulating phosphorylation of tyrosines in cells.[6]
Crk should not be confused with Src, which also has cellular (c-Src) and viral (v-Src) forms and is involved in some of the same signaling pathways but is a protein tyrosine-kinase.
Interactions
CRK (gene) has been shown to interact with:
- BCAR1,[7][8][9][10][11][12][13][14][15]
- Cbl gene,[16][17]
- Dock180,[18][9][10][19][20]
- EPS15,[21]
- Epidermal growth factor receptor,[22][23]
- Grb2,[24][18][25]
- IRS4,[26][27]
- MAP4K1,[28][29][30]
- MAPK8,[31]
- NEDD9,[32][33]
- PDGFRA,[34][35]
- PDGFRB,[34]
- PTK2,[9][12]
- Paxillin[12][36]
- RAPGEF1,[37]
- RICS,[38][39]
- SH3KBP1,[40] and
- SOS1.[25]
See also
- CrkL, "Crk-like" protein
References
- ↑ "Association of the v-crk oncogene product with phosphotyrosine-containing proteins and protein kinase activity.". Proc Natl Acad Sci U S A 87 (7): 2638–42. 1990. doi:10.1073/pnas.87.7.2638. PMID 1690891. Bibcode: 1990PNAS...87.2638M.
- ↑ 2.0 2.1 "Reduction of Crk and CrkL expression blocks reelin-induced dendritogenesis". J. Cell Sci. 121 (Pt 11): 1869–75. June 2008. doi:10.1242/jcs.027334. PMID 18477607.
- ↑ 3.0 3.1 "Crk and Crk-like play essential overlapping roles downstream of disabled-1 in the Reelin pathway". J. Neurosci. 28 (50): 13551–62. December 2008. doi:10.1523/JNEUROSCI.4323-08.2008. PMID 19074029.
- ↑ "Entrez Gene: CRK v-crk sarcoma virus CT10 oncogene homolog (avian)". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1398.
- ↑ Tetsuya Nakamoto; Ryuichi Sakai; Keiya Ozawa; Yoshio Yazaki; Hisamaru Hirai (1996). "Direct Binding of C-terminal Region of p130Graphic to SH2 and SH3 Domains of Src Kinase". J. Biol. Chem. 271 (15): 8959–8965. doi:10.1074/jbc.271.15.8959. PMID 8621540.
- ↑ "A novel viral oncogene with structural similarity to phospholipase C". Nature 332 (6161): 272–5. March 1988. doi:10.1038/332272a0. PMID 2450282. Bibcode: 1988Natur.332..272M.
- ↑ "The palmitoylation of metastasis suppressor KAI1/CD82 is important for its motility- and invasiveness-inhibitory activity". Cancer Res. 64 (20): 7455–63. 2004. doi:10.1158/0008-5472.CAN-04-1574. PMID 15492270.
- ↑ "P130Cas-associated protein (p140Cap) as a new tyrosine-phosphorylated protein involved in cell spreading". Mol. Biol. Cell 15 (2): 787–800. 2004. doi:10.1091/mbc.E03-09-0689. PMID 14657239.
- ↑ 9.0 9.1 9.2 "Differential regulation of cell motility and invasion by FAK". J. Cell Biol. 160 (5): 753–67. 2003. doi:10.1083/jcb.200212114. PMID 12615911.
- ↑ 10.0 10.1 "Laminin-10/11 and fibronectin differentially regulate integrin-dependent Rho and Rac activation via p130(Cas)-CrkII-DOCK180 pathway". J. Biol. Chem. 276 (29): 27090–7. 2001. doi:10.1074/jbc.M102284200. PMID 11369773.
- ↑ "Regulation of fibroblast motility by the protein tyrosine phosphatase PTP-PEST". J. Biol. Chem. 274 (6): 3811–8. 1999. doi:10.1074/jbc.274.6.3811. PMID 9920935.
- ↑ 12.0 12.1 12.2 "Protein tyrosine phosphatase-PEST regulates focal adhesion disassembly, migration, and cytokinesis in fibroblasts". J. Cell Biol. 144 (5): 1019–31. 1999. doi:10.1083/jcb.144.5.1019. PMID 10085298.
- ↑ "Inhibition of p130cas tyrosine phosphorylation by calyculin A". J. Leukoc. Biol. 63 (5): 631–5. 1998. doi:10.1002/jlb.63.5.631. PMID 9581808.
- ↑ "Adaptor proteins Grb2 and Crk couple Pyk2 with activation of specific mitogen-activated protein kinase cascades". J. Biol. Chem. 274 (21): 14893–901. 1999. doi:10.1074/jbc.274.21.14893. PMID 10329689.
- ↑ "Stromal cell-derived factor-1alpha stimulates tyrosine phosphorylation of multiple focal adhesion proteins and induces migration of hematopoietic progenitor cells: roles of phosphoinositide-3 kinase and protein kinase C". Blood 95 (8): 2505–13. 2000. doi:10.1182/blood.V95.8.2505. PMID 10753828.
- ↑ "Interleukin-2 stimulation induces tyrosine phosphorylation of p120-Cbl and CrkL and formation of multimolecular signaling complexes in T lymphocytes and natural killer cells". J. Biol. Chem. 273 (7): 3986–93. 1998. doi:10.1074/jbc.273.7.3986. PMID 9461587.
- ↑ "CSF-1 stimulation induces the formation of a multiprotein complex including CSF-1 receptor, c-Cbl, PI 3-kinase, Crk-II and Grb2". Oncogene 14 (19): 2331–8. 1997. doi:10.1038/sj.onc.1201074. PMID 9178909.
- ↑ 18.0 18.1 "Interaction between the amino-terminal SH3 domain of CRK and its natural target proteins". J. Biol. Chem. 271 (24): 14468–72. 1996. doi:10.1074/jbc.271.24.14468. PMID 8662907.
- ↑ "Non-adherent cell-specific expression of DOCK2, a member of the human CDM-family proteins". Biochim. Biophys. Acta 1452 (2): 179–87. 1999. doi:10.1016/S0167-4889(99)00133-0. PMID 10559471.
- ↑ "DOCK180, a major CRK-binding protein, alters cell morphology upon translocation to the cell membrane". Mol. Cell. Biol. 16 (4): 1770–6. 1996. doi:10.1128/MCB.16.4.1770. PMID 8657152.
- ↑ "The SH3 domain of Crk binds specifically to a conserved proline-rich motif in Eps15 and Eps15R". J. Biol. Chem. 270 (25): 15341–7. 1995. doi:10.1074/jbc.270.25.15341. PMID 7797522.
- ↑ 9614078 "Phosphotyrosine interactome of the ErbB-receptor kinase family". Mol. Syst. Biol. 1 (1): E1–E13. 2005. doi:10.1038/msb4100012. PMID 16729043.
- ↑ "Phosphorylation of CrkII adaptor protein at tyrosine 221 by epidermal growth factor receptor". J. Biol. Chem. 273 (27): 17186–91. 1998. doi:10.1074/jbc.273.27.17186. PMID 9642287.
- ↑ "The beta-subunit of the hepatocyte growth factor/scatter factor (HGF/SF) receptor phosphorylates and associates with CrkII: expression of CrkII enhances HGF/SF-induced mitogenesis". Biochem. J. 350 (3): 925–32. 2000. doi:10.1042/0264-6021:3500925. PMID 10970810.
- ↑ 25.0 25.1 "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. 1996. doi:10.1074/jbc.271.41.25533. PMID 8810325.
- ↑ "The insulin-like growth factor I receptor-induced interaction of insulin receptor substrate-4 and Crk-II". Endocrinology 142 (5): 1835–40. 2001. doi:10.1210/endo.142.5.8135. PMID 11316748.
- ↑ "Interplay of the proto-oncogene proteins CrkL and CrkII in insulin-like growth factor-I receptor-mediated signal transduction". J. Biol. Chem. 273 (24): 14780–7. 1998. doi:10.1074/jbc.273.24.14780. PMID 9614078.
- ↑ "The germinal center kinase (GCK)-related protein kinases HPK1 and KHS are candidates for highly selective signal transducers of Crk family adapter proteins". Oncogene 17 (15): 1893–901. 1998. doi:10.1038/sj.onc.1202108. PMID 9788432.
- ↑ "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. 1999. doi:10.1128/MCB.19.2.1359. PMID 9891069.
- ↑ "Involvement of hematopoietic progenitor kinase 1 in T cell receptor signaling". J. Biol. Chem. 276 (22): 18908–14. 2001. doi:10.1074/jbc.M101485200. PMID 11279207.
- ↑ "A direct interaction between JNK1 and CrkII is critical for Rac1-induced JNK activation". EMBO J. 20 (13): 3437–46. 2001. doi:10.1093/emboj/20.13.3437. PMID 11432831.
- ↑ "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. 1996. doi:10.1084/jem.184.4.1365. PMID 8879209.
- ↑ "T cell receptor-mediated tyrosine phosphorylation of Cas-L, a 105-kDa Crk-associated substrate-related protein, and its association of Crk and C3G". J. Biol. Chem. 273 (11): 6446–51. 1998. doi:10.1074/jbc.273.11.6446. PMID 9497377.
- ↑ 34.0 34.1 "Differential interaction of CrkII adaptor protein with platelet-derived growth factor alpha- and beta-receptors is determined by its internal tyrosine phosphorylation". Biochem. Biophys. Res. Commun. 270 (1): 28–33. 2000. doi:10.1006/bbrc.2000.2374. PMID 10733900.
- ↑ "Identification of Tyr-762 in the platelet-derived growth factor alpha-receptor as the binding site for Crk proteins". Oncogene 16 (10): 1229–39. 1998. doi:10.1038/sj.onc.1201641. PMID 9546424.
- ↑ "Tyrosine 221 in Crk regulates adhesion-dependent membrane localization of Crk and Rac and activation of Rac signaling". EMBO J. 21 (17): 4571–82. 2002. doi:10.1093/emboj/cdf446. PMID 12198159.
- ↑ "C3G, a guanine nucleotide-releasing protein expressed ubiquitously, binds to the Src homology 3 domains of CRK and GRB2/ASH proteins". Proc. Natl. Acad. Sci. U.S.A. 91 (8): 3443–7. 1994. doi:10.1073/pnas.91.8.3443. PMID 7512734. Bibcode: 1994PNAS...91.3443T.
- ↑ "GC-GAP, a Rho family GTPase-activating protein that interacts with signaling adapters Gab1 and Gab2". J. Biol. Chem. 278 (36): 34641–53. 2003. doi:10.1074/jbc.M304594200. PMID 12819203.
- ↑ "Characterization of a brain-specific Rho GTPase-activating protein, p200RhoGAP". J. Biol. Chem. 278 (6): 4151–9. 2003. doi:10.1074/jbc.M207789200. PMID 12454018.
- ↑ "Characterization of the CIN85 adaptor protein and identification of components involved in CIN85 complexes". Biochem. Biophys. Res. Commun. 278 (1): 167–74. 2000. doi:10.1006/bbrc.2000.3760. PMID 11071869. https://zenodo.org/record/1229524.
Further reading
- "SH2 and SH3 domains as molecular adhesives: the interactions of Crk and Abl.". Trends Biochem. Sci. 19 (11): 453–8. 1995. doi:10.1016/0968-0004(94)90129-5. PMID 7855886.
- "Physiological signals and oncogenesis mediated through Crk family adapter proteins.". J. Cell. Physiol. 177 (4): 535–52. 1999. doi:10.1002/(SICI)1097-4652(199812)177:4<535::AID-JCP5>3.0.CO;2-E. PMID 10092207.
- "Insulin and EGF receptors integrate the Ras and Rap signaling pathways.". Endocr. J. 46 Suppl: S11–6. 2002. doi:10.1507/endocrj.46.suppl_s11. PMID 12054111.
- "Identification of a protein that binds to the SH3 region of Abl and is similar to Bcr and GAP-rho.". Science 257 (5071): 803–6. 1992. doi:10.1126/science.1379745. PMID 1379745. Bibcode: 1992Sci...257..803C.
- "Two species of human CRK cDNA encode proteins with distinct biological activities.". Mol. Cell. Biol. 12 (8): 3482–9. 1992. doi:10.1128/MCB.12.8.3482. PMID 1630456.
- "Binding of SH2 domains of phospholipase C gamma 1, GAP, and Src to activated growth factor receptors.". Science 250 (4983): 979–82. 1990. doi:10.1126/science.2173144. PMID 2173144. Bibcode: 1990Sci...250..979A.
- "Autophosphorylation of the focal adhesion kinase, pp125FAK, directs SH2-dependent binding of pp60src.". Mol. Cell. Biol. 14 (3): 1680–8. 1994. doi:10.1128/MCB.14.3.1680. PMID 7509446.
- "Expression of the v-crk oncogene product in PC12 cells results in rapid differentiation by both nerve growth factor- and epidermal growth factor-dependent pathways.". Mol. Cell. Biol. 14 (3): 1964–71. 1994. doi:10.1128/MCB.14.3.1964. PMID 7509449.
- "C3G, a guanine nucleotide-releasing protein expressed ubiquitously, binds to the Src homology 3 domains of CRK and GRB2/ASH proteins.". Proc. Natl. Acad. Sci. U.S.A. 91 (8): 3443–7. 1994. doi:10.1073/pnas.91.8.3443. PMID 7512734. Bibcode: 1994PNAS...91.3443T.
- "Tyrosine phosphorylation of focal adhesion kinase at sites in the catalytic domain regulates kinase activity: a role for Src family kinases.". Mol. Cell. Biol. 15 (2): 954–63. 1995. doi:10.1128/MCB.15.2.954. PMID 7529876.
- "v-Crk modulation of growth factor-induced PC12 cell differentiation involves the Src homology 2 domain of v-Crk and sustained activation of the Ras/mitogen-activated protein kinase pathway.". J. Biol. Chem. 270 (35): 20677–85. 1995. doi:10.1074/jbc.270.35.20677. PMID 7657647.
- "The SH3 domain of Crk binds specifically to a conserved proline-rich motif in Eps15 and Eps15R.". J. Biol. Chem. 270 (25): 15341–7. 1995. doi:10.1074/jbc.270.25.15341. PMID 7797522.
- "CRK protein binds to two guanine nucleotide-releasing proteins for the Ras family and modulates nerve growth factor-induced activation of Ras in PC12 cells.". Mol. Cell. Biol. 14 (8): 5495–500. 1994. doi:10.1128/MCB.14.8.5495. PMID 8035825.
- "c-Abl kinase regulates the protein binding activity of c-Crk.". EMBO J. 13 (10): 2341–51. 1994. doi:10.1002/j.1460-2075.1994.tb06518.x. PMID 8194526.
- "CRK proto-oncogene maps to human chromosome band 17p13.". Oncogene 8 (10): 2853–5. 1993. PMID 8378094.
- "Sos, Vav, and C3G participate in B cell receptor-induced signaling pathways and differentially associate with Shc-Grb2, Crk, and Crk-L adaptors.". J. Biol. Chem. 271 (15): 8564–9. 1996. doi:10.1074/jbc.271.15.8564. PMID 8621483.
- "The proto-oncogene product c-Crk associates with insulin receptor substrate-1 and 4PS. Modulation by insulin growth factor-I (IGF) and enhanced IGF-I signaling.". J. Biol. Chem. 271 (16): 9287–90. 1996. doi:10.1074/jbc.271.16.9287. PMID 8621590.
- "DOCK180, a major CRK-binding protein, alters cell morphology upon translocation to the cell membrane.". Mol. Cell. Biol. 16 (4): 1770–6. 1996. doi:10.1128/MCB.16.4.1770. PMID 8657152.
External links
- Crk Info with links in the Cell Migration Gateway
- Proto-Oncogene+Proteins+c-crk at the US National Library of Medicine Medical Subject Headings (MeSH)
- Oncogene+Protein+v-crk at the US National Library of Medicine Medical Subject Headings (MeSH)
- Human CRK genome location and CRK gene details page in the UCSC Genome Browser.
Original source: https://en.wikipedia.org/wiki/Adapter molecule crk.
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