PHD3-mediated prolyl hydroxylation of nonmuscle actin impairs polymerization and cell motility-Reference-Cited by-同舟云学术

PHD3-mediated prolyl hydroxylation of nonmuscle actin impairs polymerization and cell motility

Published:2014-09-15 Issue:18 Volume:25 Page:2788-2796
ISSN:1059-1524
Container-title:Molecular Biology of the Cell
language:en
Short-container-title:MBoC

Author:

Luo Weibo¹²,Lin Benjamin¹³,Wang Yingfei⁴,Zhong Jun²,O'Meally Robert²,Cole Robert N.²,Pandey Akhilesh²⁵⁶⁷,Levchenko Andre¹³,Semenza Gregg L.¹²⁵⁷⁸

Affiliation:

1. Vascular Program, Institute for Cell Engineering, Johns Hopkins University School of Medicine, Baltimore, MD 21205

2. Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205

3. Department of Biomedical Engineering, Johns Hopkins University School of Medicine, Baltimore, MD 21205

4. Neuroregeneration Program, Institute for Cell Engineering, Johns Hopkins University School of Medicine, Baltimore, MD 21205

5. Department of Oncology, Johns Hopkins University School of Medicine, Baltimore, MD 21205

6. Department of Pathology, Johns Hopkins University School of Medicine, Baltimore, MD 21205

7. McKusick-Nathans Institute of Genetic Medicine, Johns Hopkins University School of Medicine, Baltimore, MD 21205

8. Department of Pediatrics, Johns Hopkins University School of Medicine, Baltimore, MD 21205

Abstract

Actin filaments play an essential role in cell movement, and many posttranslational modifications regulate actin filament assembly. Here we report that prolyl hydroxylase 3 (PHD3) interacts with nonmuscle actin in human cells and catalyzes hydroxylation of actin at proline residues 307 and 322. Blocking PHD3 expression or catalytic activity by short hairpin RNA knockdown or pharmacological inhibition, respectively, decreased actin prolyl hydroxylation. PHD3 knockdown increased filamentous F-actin assembly, which was reversed by PHD3 overexpression. PHD3 knockdown increased cell velocity and migration distance. Inhibition of PHD3 prolyl hydroxylase activity by dimethyloxalylglycine also increased actin polymerization and cell migration. These data reveal a novel role for PHD3 as a negative regulator of cell motility through posttranslational modification of nonmuscle actins.

Publisher

American Society for Cell Biology (ASCB)

Subject

Cell Biology,Molecular Biology

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