Threonine 89 Is an Important Residue of Profilin-1 That Is Phosphorylatable by Protein Kinase A
Abstract
Objective Dynamic regulation of actin cytoskeleton is at the heart of all actin-based cellular events. In this study, we sought to identify novel post-translational modifications of Profilin-1 (Pfn1), an important regulator of actin polymerization in cells. Methodology We performed in vitro protein kinase assay followed by mass-spectrometry to identify Protein Kinase A (PKA) phosphorylation sites of Pfn1. By two-dimensional gel electrophoresis...
Paper Details
Title
Threonine 89 Is an Important Residue of Profilin-1 That Is Phosphorylatable by Protein Kinase A
Published Date
May 26, 2016
Journal
Volume
11
Issue
5
Pages
e0156313 - e0156313
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