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Title

Multimeric and differential binding of CIN85/CD2AP with two atypical proline-rich sequences from CD2 and Cbl-b*

AuthorsCeregido, M. Angeles; Garcia-Pino, Abel; Ortega-Roldan, Jose Luis; Casares, Salvador; López Mayorga, Obdulio; Bravo, Jerónimo ; Nuland, Nico A.J. van; Azuaga, Ana I.
KeywordsCIN85/CD2AP
ITC
NMR
SAXS
SH3 domain
Issue DateJul-2013
PublisherWiley-Blackwell
Federation of European Biochemical Societies
CitationFEBS Journal 280(14):3399-415 (2013)
AbstractThe CD2AP (CD2-associated protein) and CIN85 (Cbl-interacting protein of 85 kDa) adaptor proteins each employ three Src homology 3 (SH3) domains to cluster protein partners and ensure efficient signal transduction and down-regulation of tyrosine kinase receptors. Using NMR, isothermal titration calorimetry and small-angle X-ray scattering methods, we have characterized several binding modes of the N-terminal SH3 domain (SH3A) of CD2AP and CIN85 with two natural atypical proline-rich regions in CD2 (cluster of differentiation 2) and Cbl-b (Casitas B-lineage lymphoma), and compared these data with previous studies and published crystal structures. Our experiments show that the CD2AP-SH3A domain forms a type II dimer with CD2 and both type I and type II dimeric complexes with Cbl-b. Like CD2AP, the CIN85-SH3A domain forms a type II complex with CD2, but a trimeric complex with Cbl-b, whereby the type I and II interactions take place at the same time. Together, these results explain how multiple interactions among similar SH3 domains and ligands produce a high degree of diversity in tyrosine kinase, cell adhesion or T-cell signaling pathways.
Description17 páginas, 8 figuras, 1 tabla. Este fichero contiene 5 figuras y 3 tablas de material suplementario
Publisher version (URL)http://dx.doi.org/10.1111/febs.12333
URIhttp://hdl.handle.net/10261/176448
DOI10.1111/febs.12333
ISSN1742-464X
E-ISSN1742-4658
Appears in Collections:(IBV) Artículos
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