CRK (gene)

From Wikipedia, the free encyclopedia

V-crk sarcoma virus CT10 oncogene homolog (avian)

PDB rendering based on 1b07.

Available structures: 1b07, 1cka, 1ckb, 1ju5, 1m30, 1m3a, 1m3b, 1m3c, 2dvj, 2eyv, 2eyw, 2eyx, 2eyy, 2eyz, 2ggr

Identifiers

Symbol(s)

CRK; CRKII

External IDs

OMIM: 164762 MGI: 88508 HomoloGene: 81850

Gene ontology
Molecular Function:	• SH3/SH2 adaptor activity • protein binding • SH2 domain binding • protein phosphorylated amino acid binding
Cellular Component:	• nucleus • cytoplasm
Biological Process:	• regulation of transcription from RNA polymerase II promoter • cell motility • intracellular signaling cascade • actin cytoskeleton organization and biogenesis

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_005206 (mRNA)
NP_005197 (protein)

NM_133656 (mRNA)
NP_598417 (protein)

Location

Chr 17: 1.27 - 1.31 Mb

Chr 11: 75.5 - 75.52 Mb

Pubmed search

[1]

[2]

CRK is a gene which codes a protein exhibiting the SH2 domain.

This gene encodes a member of an adapter protein family that binds to several tyrosine-phosphorylated proteins. The product of this gene 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.^[1]

[edit] References

^ Entrez Gene: CRK v-crk sarcoma virus CT10 oncogene homolog (avian).

[edit] Further reading

Feller SM, Ren R, Hanafusa H, Baltimore D (1995). "SH2 and SH3 domains as molecular adhesives: the interactions of Crk and Abl.". Trends Biochem. Sci. 19 (11): 453–8. PMID 7855886.
Feller SM, Posern G, Voss J, et al. (1999). "Physiological signals and oncogenesis mediated through Crk family adapter proteins.". J. Cell. Physiol. 177 (4): 535–52. doi:10.1002/(SICI)1097-4652(199812)177:4<535::AID-JCP5>3.0.CO;2-E. PMID 10092207.
Pessin JE, Okada S (2002). "Insulin and EGF receptors integrate the Ras and Rap signaling pathways.". Endocr. J. 46 Suppl: S11–6. PMID 12054111.
Cicchetti P, Mayer BJ, Thiel G, Baltimore D (1992). "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. PMID 1379745.
Matsuda M, Tanaka S, Nagata S, et al. (1992). "Two species of human CRK cDNA encode proteins with distinct biological activities.". Mol. Cell. Biol. 12 (8): 3482–9. PMID 1630456.
Mayer BJ, Hanafusa H (1990). "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. PMID 1690891.
Anderson D, Koch CA, Grey L, et al. (1990). "Binding of SH2 domains of phospholipase C gamma 1, GAP, and Src to activated growth factor receptors.". Science 250 (4983): 979–82. PMID 2173144.
Schaller MD, Hildebrand JD, Shannon JD, et al. (1994). "Autophosphorylation of the focal adhesion kinase, pp125FAK, directs SH2-dependent binding of pp60src.". Mol. Cell. Biol. 14 (3): 1680–8. PMID 7509446.
Hempstead BL, Birge RB, Fajardo JE, et al. (1994). "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. PMID 7509449.
Tanaka S, Morishita T, Hashimoto Y, et al. (1994). "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. PMID 7512734.
Calalb MB, Polte TR, Hanks SK (1995). "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. PMID 7529876.
Teng KK, Lander H, Fajardo JE, et al. (1995). "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. PMID 7657647.
Schumacher C, Knudsen BS, Ohuchi T, et al. (1995). "The SH3 domain of Crk binds specifically to a conserved proline-rich motif in Eps15 and Eps15R.". J. Biol. Chem. 270 (25): 15341–7. PMID 7797522.
Matsuda M, Hashimoto Y, Muroya K, et al. (1994). "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. PMID 8035825.
Feller SM, Knudsen B, Hanafusa H (1994). "c-Abl kinase regulates the protein binding activity of c-Crk.". EMBO J. 13 (10): 2341–51. PMID 8194526.
Fioretos T, Heisterkamp N, Groffen J, et al. (1993). "CRK proto-oncogene maps to human chromosome band 17p13.". Oncogene 8 (10): 2853–5. PMID 8378094.
Smit L, van der Horst G, Borst J (1996). "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. PMID 8621483.
Beitner-Johnson D, Blakesley VA, Shen-Orr Z, et al. (1996). "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. PMID 8621590.
Hasegawa H, Kiyokawa E, Tanaka S, et al. (1996). "DOCK180, a major CRK-binding protein, alters cell morphology upon translocation to the cell membrane.". Mol. Cell. Biol. 16 (4): 1770–6. PMID 8657152.