Threonine 89 Is an Important Residue of Profilin-1 That Is Phosphorylatable by Protein Kinase A-Reference-Cited by-同舟云学术

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

Published:2016-05-26 Issue:5 Volume:11 Page:e0156313
ISSN:1932-6203
Container-title:PLOS ONE
language:en
Short-container-title:PLoS ONE

Author:

Gau David,Veon William,Zeng Xuemei,Yates Nathan,Shroff Sanjeev G.,Koes David R.,Roy Partha

Funder

National Institutes of Health

National Science Foundation

Publisher

Public Library of Science (PLoS)

Subject

Multidisciplinary

Reference26 articles.

1. Control of actin filament treadmilling in cell motility;B Bugyi;Annu Rev Biophys,2010

2. Molecular insights on context-specific role of profilin-1 in cell migration;Z Ding;Cell Adh Migr,2012

3. Contribution of Ena/VASP proteins to intracellular motility of Listeria requires phosphorylation and proline-rich core but non F-actin binding or multimerization;M Geese;Molecular Biology of the Cell,2002

4. VASP is a processive actin polymerase that requires monomeric actin for barbed end association;SD Hansen;J Cell Biol,2010

5. The essential role of profilin in the assembly of actin for microspike formation;S Suetsugu;EMBO Journal,1998

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1. The Actin Regulators Involved in the Function and Related Diseases of Lymphocytes;Frontiers in Immunology;2022-03-16

2. Protein Network Analysis Reveals a Functional Connectivity of Dysregulated Processes in ALS and SMA;Neuroscience Insights;2022-01

3. Specificity and Redundancy of Profilin 1 and 2 Function in Brain Development and Neuronal Structure;Cells;2021-09-03

4. Profilin: many facets of a small protein;Biophysical Reviews;2020-07-13

5. Profilin2a‐phosphorylation as a regulatory mechanism for actin dynamics;The FASEB Journal;2019-12-12

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