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Threonine 89 Is an Important Residue of Profilin-1 That Is Phosphorylatable by Protein Kinase A

Threonine 89 Is an Important Residue of Profilin-1 That Is Phosphorylatable by Protein Kinase A

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_1791869535

Threonine 89 Is an Important Residue of Profilin-1 That Is Phosphorylatable by Protein Kinase A

About this item

Full title

Threonine 89 Is an Important Residue of Profilin-1 That Is Phosphorylatable by Protein Kinase A

Publisher

United States: Public Library of Science

Journal title

PloS one, 2016-05, Vol.11 (5), p.e0156313-e0156313

Language

English

Formats

Publication information

Publisher

United States: Public Library of Science

More information

Scope and Contents

Contents

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.
We performed in vitro protein kinase assay followed by mass-spectrometry to identify Protein Kinase...

Alternative Titles

Full title

Threonine 89 Is an Important Residue of Profilin-1 That Is Phosphorylatable by Protein Kinase A

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_plos_journals_1791869535

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_1791869535

Other Identifiers

ISSN

1932-6203

E-ISSN

1932-6203

DOI

10.1371/journal.pone.0156313

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