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Reliable, easy-to-read patient information on common medical conditions — written in plain language, free of jargon, and grounded in current evidence. Browse the most frequent diagnoses, understand what they mean for everyday life, and learn which steps and questions help you have a focused conversation with your doctor.

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CRK (gene)

Introduction

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]

References

References

  1. ↑ “Entrez Gene: CRK v-crk sarcoma virus CT10 oncogene homolog (avian)”.
Further reading

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.
External links

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