Activation of the Src-family tyrosine kinase Hck by SH3 domain displacement

Nature

Volumn 385, Issue 6617, 1997, Pages 650-653

  Moarefi, Ismail ^a   LaFevre Bernt, Michelle ^b   Sicheri, Frank ^a   Huse, Morgan ^a   Lee, Chi Hon ^a   Kuriyan, John ^a   Miller, W Todd ^b  

^a ROCKEFELLER UNIVERSITY   (United States)

^b STONY BROOK UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN KINASE P60; PROTEIN TYROSINE KINASE;

ARTICLE; CRYSTAL STRUCTURE; ENZYME ACTIVATION; ENZYME ACTIVITY; HEMATOPOIESIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN;

AMINO ACID SEQUENCE; CATALYSIS; CELL LINE; DOWN-REGULATION; ENZYME ACTIVATION; ENZYME STABILITY; GENE PRODUCTS, NEF; HIV-1; MASS SPECTROMETRY; MODELS, BIOLOGICAL; MOLECULAR SEQUENCE DATA; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN-TYROSINE KINASES; PROTO-ONCOGENE PROTEINS; PROTO-ONCOGENE PROTEINS C-HCK; RECOMBINANT PROTEINS; SRC HOMOLOGY DOMAINS; SRC-FAMILY KINASES;

HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 0031017838     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/385650a0     Document Type: Article

References (24)

1. Ziegler, S. F., Marth, J. C., Lewis, D. B. & Perlmutter, R. M. Novel protein-tyrosine kinase gene (hck) preferentially expressed in cells of hematopoietic origin. Mol. Cell. Biol. 7, 2276-2285 (1987).
2. Quintrell, N. et al. Identification of a human gene (HCK) that encodes a protein-tyrosine kinase and is expressed in hemopoietic cells. Mol. Cell. Biol. 7, 2267-2275 (1987).
3. c-src. Mol. Cell. Biol. 6, 4467-4477 (1986).
4. c-src kinase by middle T antigen binding or by dephosphorylation. EMBO J. 4, 1471-1477 (1985).
5. c-src transforming ability by mutation of its primary sites of tyrosine phosphorylation. Cell 49, 65-73 (1987).
6. c-src. Cell 49, 75-82 (1987).
7. c-src mutated in the carboxy-terminal regulatory domain. Cell 49, 83-91 (1987).
8. Cooper, J. A. & Howell, B. The when and how of Src regulation. Cell 93, 1051-1054 (1993).
9. Superti-Furga, G. & Courtneidge, S. A. Structure-function relationships in Src family and related protein tyrosine kinases. BioEssays 17, 321-330 (1995).
10. c-src. Proc. Natl Acad. Sci. USA 88, 10690-10700 (1991).
11. Liu, X. et al. Regulation of c-Src tyrosine kinase activity by the Sec SH2 domain. Oncogene 8, 1119-1126 (1993).
12. Sichert, F., Moarefi, I. & Kuriyan, J. Crystal structure of the Src-family tyrosine kinase Hck. Nature 385, 602-609 (1997).
13. c-src by intermolecular autophosphorylation. Proc. Natl. Acad. Sci. USA 85, 4232-4236 (1988).
14. c-src tyrosine kinase activities using a continuous assay: autoactivation of the enzyme is an intermolecular autophosphorylation process. Biochemistry 34, 14843-14851 (1995).
15. c-src with tyrosine kinase activity: the intramolecular pY530-SH2 complex retains significant activity if Y419 is phosphorylated. Biochemistry 35, 9519-9525 (1996).
16. Trono, D. HIV accessory proteins: leading roles for the supporting cast. Cell 82, 189-192 (1995).
17. + viruses but not for down-regulation of CD4. EMBO J. 14, 484-491 (1995).
18. Lee, C.-H. et al. A single amino acid in the SH3 domain of Hck determines its high affinity and specificity in binding to HIV-1 Nef protein. EMBO J 14, 5006-5015 (1995).
19. Pleiman, C. M., Hertz, W. M. & Cambier, J. C. Activation of phosphaudylinositol-3′ kinase by Src-family kinase SH3 binding to the p85 subunit. Science 263, 1609-1612 (1994).
20. Johnson, L. N., Noble, M. E. M. & Owen, D. I. Active and inactive protein kinases: structural basis for regulation. Cell 85, 149-158 (1996).
21. Cas-related protein, Sin. Genes Dev. 10, 1341-1355 (1996).
22. Till, J. H., Annan, R. S., Carr, S. A. & Miller, W. T. Use of synthetic peptide libraries and phosphopeptide-selective mass spectrometry to probe protein kinase substrate specificity. J. Biol. Chem. 269, 7423-7428 (1994).
23. Casnellie, J. H. Assay of protein kinases using peptides with basic residues for phosphocellulose binding. Meth. Enzymol. 200, 115-120 (1991).
24. Feng, S., Chen, J. K., Yu, H., Simon, J. A. & Schreiber, S. L. Two binding orientations for peptides to the Src SH3 domain: development of a general model for SH3-ligand interactions. Science 266, 1241-1247 (1994).