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First published online October 27, 2005
doi: 10.1242/10.1242/jcs.02563

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Paxillin phosphorylation sites mapped by mass spectrometry

Donna J. Webb^1,*,,, Melanie J. Schroeder^2,, Cynthia J. Brame⁴, Leanna Whitmore¹, Jeffrey Shabanowitz², Donald F. Hunt^2,3 and A. Rick Horwitz¹

¹ Department of Cell Biology, University of Virginia, 1300 Jefferson Park Avenue, Charlottesville, VA 22908, USA
² Department of Chemistry, University of Virginia, 1300 Jefferson Park Avenue, Charlottesville, VA 22908, USA
³ Department of Pathology, University of Virginia, 1300 Jefferson Park Avenue, Charlottesville, VA 22908, USA
⁴ Department of Biology, Centenary College of Louisiana, 2911 Centenary Avenue, Shreveport, LA 71104, USA

View larger version (45K): [in a new window]   Fig. 1. Phosphorylation sites detected in chicken paxillin. (A) Serine, threonine and tyrosine coverage of the FLAG-GFP-paxillin sequence (tag not shown) generated with trypsin. Peptides were analyzed by nHLPC-µESI MS/MS (LTQ-FTMS). Detected tryptic peptides are bold and alternate between solid and dashed underlines. Residues not covered are shaded in gray. Observed phosphorylation sites are red. Red brackets above residues indicate ambiguity in specific phosphorylation site assignment. Observed GlcNAc site is green. Coverage of the Ser, Thr and Tyr sites is 92%. (B) A schematic of paxillin is shown. The paxillin phosphorylation sites are represented by stars, which show their positions relative to the paxillin domains. The binding sites within paxillin for some adhesion/migration molecules are also shown.