Structural basis for the transforming activity of human cancer-related signaling adaptor protein CRK.

Structural basis for the transforming activity of human cancer-related signaling adaptor protein CRK. Research Abstract Details 

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Structural basis for the transforming activity of human cancer-related signaling adaptor protein CRK. Abstract Text:

Yoshihiro Kobashigawa,Mieko Sakai,Masato Naito,Masashi Yokochi,Hiroyuki Kumeta,Yoshinori Makino,Kenji Ogura,Shinya Tanaka,Fuyuhiko Inagaki,

CRKI (SH2-SH3) and CRKII (SH2-SH3-SH3) are splicing isoforms of the oncoprotein CRK that regulate transcription and cytoskeletal reorganization for cell growth and motility by linking tyrosine kinases to small G proteins. CRKI shows substantial transforming activity, whereas the activity of CRKII is low, and phosphorylated CRKII has no biological activity whatsoever. The molecular mechanisms underlying the distinct biological activities of the CRK proteins remain elusive. We determined the solution structures of CRKI, CRKII and phosphorylated CRKII by NMR and identified the molecular mechanism that gives rise to their activities. Results from mutational analysis using rodent 3Y1 fibroblasts were consistent with those from the structural studies. Together, these data suggest that the linker region modulates the binding of CRKII to its targets, thus regulating cell growth and motility.

Structural basis for the transforming activity of human cancer-related signaling adaptor protein CRK. Publishing Authors By Initials

Y Kobashigawa,M Sakai,M Naito,M Yokochi,H Kumeta,Y Makino,K Ogura,S Tanaka,F Inagaki,

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Structural basis for the transforming activity of human cancer-related signaling adaptor protein CRK. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Nature structural & molecular biology

VOLUME: 14

Page Numbers: 503-10

Journal Abbreviation: Nat. Struct. Mol. Biol.

ISSN: 1545-9993

DAY: 21

MONTH: 05

YEAR: 2007

Structural basis for the transforming activity of human cancer-related signaling adaptor protein CRK. Information

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LANGUAGE: eng

NlmUniqueID: 101186374

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AFFILIATION: Department of Structural Biology, Graduate School of Pharmaceutical Sciences, Hokkaido University, Sapporo, Hokkaido 060-0810, Japan.

Country: United States

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MEDLINETA: Nat Struct Mol Biol

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