TY  - JOUR
A1  - Fernow, Inga Susanne
A1  - Tomasovic, Ana
A1  - Siehoff-Icking, Ann
A1  - Tikkanen, Ritva
T1  - Cbl-associated protein is tyrosine phosphorylated by c-Abl and c-Src kinases
T2  - BMC cell biology
N2  - Background: The c-Cbl-associated protein (CAP), also known as ponsin, localizes to focal adhesions and stress fibers and is involved in signaling events. Phosphorylation has been described for the other two members of the sorbin homology family, vinexin and ArgBP2, but no data exist about the putative phosphorylation of CAP. According to previous findings, CAP binds to tyrosine kinase c-Abl. However, it is not known if CAP is a substrate of c-Abl or other tyrosine kinases or if phosphorylation regulates its localization.
Results: We here show that CAP is Tyr phosphorylated by and interacts with both c-Abl and c-Src. One major phosphorylation site, Tyr360, and two minor contributors Tyr326 and Tyr632 were identified as Abl phosphorylation sites, whereas Src preferentially phosphorylates Tyr326 and Tyr360. Phosphorylation of CAP was not necessary for its localization to focal adhesions and stress fibers, but Tyr326Phe substitution alters the function of CAP during cell spreading.
Conclusion: This is the first demonstration of phosphorylation of CAP by any kinase. Our findings suggest that coordinated action of Src and Abl might regulate the function of CAP and reveal a functional role especially for the Src-mediated Tyr phosphorylation of CAP in cell spreading.
Y1  - 2009
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/7281
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30-72403
SN  - 1471-2121
N1  - © 2009 Fernow et al; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
VL  - 10
IS  - Art. 80
SP  - 1
EP  - 14
PB  - BioMed Central ; Springer
CY  - London ; Berlin ; Heidelberg
ER  -