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Adapter molecule crk

From Wikipedia, the free encyclopedia

CRK
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesCRK, CRKII, p38, v-crk avian sarcoma virus CT10 oncogene homolog, CRK proto-oncogene, adaptor protein
External IDsOMIM: 164762; MGI: 88508; HomoloGene: 81850; GeneCards: CRK; OMA:CRK - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_016823
NM_005206

NM_001277219
NM_001277221
NM_133656

RefSeq (protein)

NP_005197
NP_058431

NP_001264148
NP_001264150
NP_598417

Location (UCSC)Chr 17: 1.42 – 1.46 MbChr 11: 75.57 – 75.6 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Adapter molecule crk also known as proto-oncogene c-Crk is a protein that in humans is encoded by the CRK gene.[5]

The CRK protein participates in the Reelin signaling cascade downstream of DAB1.[6][7]

Function

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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.[8]

Crk together with CrkL participates in the Reelin signaling cascade downstream of DAB1.[6][7]

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.[9] 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.[10]

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

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CRK (gene) has been shown to interact with:

See also

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  • CrkL, "Crk-like" protein

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000167193Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000017776Ensembl, 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. ^ 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. Bibcode:1990PNAS...87.2638M. doi:10.1073/pnas.87.7.2638. PMC 53745. PMID 1690891.
  6. ^ a b Matsuki T, Pramatarova A, Howell BW (June 2008). "Reduction of Crk and CrkL expression blocks reelin-induced dendritogenesis". J. Cell Sci. 121 (Pt 11): 1869–75. doi:10.1242/jcs.027334. PMC 2430739. PMID 18477607.
  7. ^ a b Park TJ, Curran T (December 2008). "Crk and Crk-like play essential overlapping roles downstream of disabled-1 in the Reelin pathway". J. Neurosci. 28 (50): 13551–62. doi:10.1523/JNEUROSCI.4323-08.2008. PMC 2628718. PMID 19074029.
  8. ^ "Entrez Gene: CRK v-crk sarcoma virus CT10 oncogene homolog (avian)".
  9. ^ 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.
  10. ^ Mayer BJ, Hamaguchi M, Hanafusa H (March 1988). "A novel viral oncogene with structural similarity to phospholipase C". Nature. 332 (6161): 272–5. Bibcode:1988Natur.332..272M. doi:10.1038/332272a0. PMID 2450282. S2CID 4352676.
  11. ^ Zhou B, Liu L, Reddivari M, Zhang XA (2004). "The palmitoylation of metastasis suppressor KAI1/CD82 is important for its motility- and invasiveness-inhibitory activity". Cancer Res. 64 (20): 7455–63. doi:10.1158/0008-5472.CAN-04-1574. PMID 15492270.
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  23. ^ Nishihara H, Kobayashi S, Hashimoto Y, Ohba F, Mochizuki N, Kurata T, Nagashima K, Matsuda M (1999). "Non-adherent cell-specific expression of DOCK2, a member of the human CDM-family proteins". Biochim. Biophys. Acta. 1452 (2): 179–87. doi:10.1016/S0167-4889(99)00133-0. PMID 10559471.
  24. ^ Hasegawa H, Kiyokawa E, Tanaka S, Nagashima K, Gotoh N, Shibuya M, Kurata T, Matsuda M (1996). "DOCK180, a major CRK-binding protein, alters cell morphology upon translocation to the cell membrane". Mol. Cell. Biol. 16 (4): 1770–6. doi:10.1128/MCB.16.4.1770. PMC 231163. PMID 8657152.
  25. ^ Schumacher C, Knudsen BS, Ohuchi T, Di Fiore PP, Glassman RH, Hanafusa H (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. doi:10.1074/jbc.270.25.15341. PMID 7797522.
  26. ^ 9614078 Schulze WX, Deng L, Mann M (2005). "Phosphotyrosine interactome of the ErbB-receptor kinase family". Mol. Syst. Biol. 1 (1): E1–E13. doi:10.1038/msb4100012. PMC 1681463. PMID 16729043.
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  29. ^ a b 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.
  30. ^ Karas M, Koval AP, Zick Y, LeRoith D (2001). "The insulin-like growth factor I receptor-induced interaction of insulin receptor substrate-4 and Crk-II". Endocrinology. 142 (5): 1835–40. doi:10.1210/endo.142.5.8135. PMID 11316748.
  31. ^ Koval AP, Karas M, Zick Y, LeRoith D (1998). "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. doi:10.1074/jbc.273.24.14780. PMID 9614078.
  32. ^ Oehrl W, Kardinal C, Ruf S, Adermann K, Groffen J, Feng GS, Blenis J, Tan TH, Feller SM (1998). "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. doi:10.1038/sj.onc.1202108. PMID 9788432.
  33. ^ Ling P, Yao Z, Meyer CF, Wang XS, Oehrl W, Feller SM, Tan TH (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.
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  35. ^ Girardin SE, Yaniv M (2001). "A direct interaction between JNK1 and CrkII is critical for Rac1-induced JNK activation". EMBO J. 20 (13): 3437–46. doi:10.1093/emboj/20.13.3437. PMC 125507. PMID 11432831.
  36. ^ 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.
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Further reading

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