Phostensin caps to the pointed end of actin filaments and modulates actin dynamics

Ning Sheng Lai, Tzu Fan Wang, Shiu Lan Wang, Chun Yu Chen, Jia yi Yen, Hsien lu Huang, Chin Li, Kuang Yung Huang, Su Qin Liu, Ta Hsien Lin*, Hsien bin Huang

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

19 Scopus citations

Abstract

Phostensin, a protein phosphatase 1 F-actin cytoskeleton targeting subunit encoded by KIAA1949, consists of 165 amino acids and is located between HLA-C and HLA-E gene clusters on human chromosome 6. In this current study, we characterized the biochemical functions of phostensin. Actin dynamics assays using gelsolin-actin seeds showed that phostensin decreases the elongation and depolymerization rates of actin filament pointed ends. The feature of phostensin that binds to the pointed ends of actin filaments was observed through fluorescent single filament binding assay. Taken together, our results suggested that phostensin is an actin filament pointed end-capping protein that is capable of modulating actin dynamics.

Original languageEnglish
Pages (from-to)676-681
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume387
Issue number4
DOIs
StatePublished - 2 Oct 2009

Keywords

  • Actin filament
  • KIAA1949
  • Phostensin
  • Protein phosphatase 1
  • Tropomodulin

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