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

First published online July 5, 2006
doi: 10.1242/10.1242/jcs03034

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 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 Martin, K. H. Articles by Parsons, J. T. Search for Related Content PubMed PubMed Citation Articles by Martin, K. H. Articles by Parsons, J. T.

Cortactin phosphorylation sites mapped by mass spectrometry

Karen H. Martin^1,*, Erin D. Jeffery^2,*, Pablo R. Grigera^1,*, Jeffrey Shabanowitz², Donald F. Hunt^2,3 and J. Thomas Parsons^1,

¹ Department of Microbiology, University of Virginia, Charlottesville, VA 22908, 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 (9K): [in a new window]   Fig. 1. Distribution of phosphorylation sites in cortactin. The domain structure of cortactin is shown with the mapped sites of serine (blue stars), threonine (green stars), and tyrosine (red stars) phosphorylation shown below.

View larger version (42K): [in a new window]   Fig. 2. Identified sites of phosphorylation in cortactin. (A) The sequence of mouse cortactin (GenBank accession no. BC011434) is shown with the amino acids that were identified by mass spectrometry (MS) shown in capital letters. Peptides representing 93% of the cortactin protein were identified. Phosphorylated residues identified by the MS analysis are shown in red. Bracketed residues contain a phosphorylation site that could not be specified unambiguously. (B) The 37 amino acid Repeats are aligned showing the sites of phosphorylation (red).