Role of palladin phosphorylation by extracellular signal-regulated kinase in cell migration

Eri Asano, Masao Maeda, Hitoki Hasegawa, Satoko Ito, Toshinori Hyodo, Hong Yuan, Masahide Takahashi, Michinari Hamaguchi, Takeshi Senga

Research output: Contribution to journalArticlepeer-review

15 Citations (Scopus)

Abstract

Phosphorylation of actin-binding proteins plays a pivotal role in the remodeling of the actin cytoskeleton to regulate cell migration. Palladin is an actin-binding protein that is phosphorylated by growth factor stimulation; however, the identity of the involved protein kinases remains elusive. In this study, we report that palladin is a novel substrate of extracellular signal-regulated kinase (ERK). Suppression of ERK activation by a chemical inhibitor reduced palladin phosphorylation, and expression of active MEK alone was sufficient for phosphorylation. In addition, an in vitro kinase assay demonstrated direct palladin phosphorylation by ERK. We found that Ser77 and Ser197 are essential residues for phosphorylation. Although the phosphorylation of these residues was not required for actin cytoskeletal organization, we found that expression of non-phosphorylated palladin enhanced cell migration. Finally, we show that phosphorylation inhibits the palladin association with Abl tyrosine kinase. Taken together, our results indicate that palladin phosphorylation by ERK has an anti-migratory function, possibly by modulating interactions with molecules that regulate cell migration.

Original languageEnglish
Article numbere29338
JournalPloS one
Volume6
Issue number12
DOIs
Publication statusPublished - 28-12-2011
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biochemistry, Genetics and Molecular Biology(all)
  • Agricultural and Biological Sciences(all)
  • General

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