QUICK SEARCH:   [advanced] Author: Keyword(s):
Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents

First published online October 27, 2005
doi: 10.1242/10.1242/jcs.02682

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Ratnikov, B. Articles by Ginsberg, M. H. Search for Related Content PubMed PubMed Citation Articles by Ratnikov, B. Articles by Ginsberg, M. H.

Talin phosphorylation sites mapped by mass spectrometry

Boris Ratnikov^1,*,, Celeste Ptak^2,*, Jaewon Han¹, Jeffrey Shabanowitz^2,3, Donald F. Hunt^2,3 and Mark H. Ginsberg¹

¹ Department of Medicine, University of California San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0726 USA
² Department of Chemistry, University of Virginia, Charlottesville, VA 22908, USA
³ Department of Pathology, University of Virginia, Charlottesville, VA 22908, USA

View larger version (24K): [in a new window]   Fig. 1. Domain structure of talin. The three modules comprising the FERM domain (F1, F2, F3), calpain cleavage site and rod domain are depicted. The locations of binding sites for actin, focal adhesion kinase (FAK), layilin, integrin b3 and vinculin are shown. Sites of high stoichiometry phosphorylation (Thr144, Thr150 and Ser446) are indicated by red stars.