Artificial phosphorylation removes gelsolin's dependence on calcium

Kingo Takiguchi, Shigeko Yamashiro-Matsumura, Fumio Matsumura

Research output: Contribution to journalArticle

3 Scopus citations

Abstract

Gelsolin is one of the best known actin-binding proteins with several distinct activities regulated by calcium. Using a kinase fraction isolated from mitotic HeLa cells, we found that the plasma form of gelsolin can be phosphorylated at a site located within the NH2-terminus region which does not exist in the cytoplasmic form. After this phosphorylation, gelsolin no longer requires Ca2+ for activity; it severs and subsequently caps actin filaments, and nucleates filament formation in Ca2+-free solution. These findings may clarify the mechanism of gelsolin regulation by Ca2+, and indicate that changes in electrical interactions between the NH2- and COOH-terminal ends are important for this regulation. Moreover, since only a single site is phosphorylated, and since the phosphorylated region does not contribute to this protein's own activity, the results suggest that a single chemical charge modification at a site away from the protein's core structure, such as this phosphorylation site, is sufficient to alter the protein's function.

Original languageEnglish (US)
Pages (from-to)57-65
Number of pages9
JournalCell Structure and Function
Volume25
Issue number1
DOIs
StatePublished - Jun 5 2000

All Science Journal Classification (ASJC) codes

  • Physiology
  • Molecular Biology
  • Cell Biology

Keywords

  • Actin-severing activity
  • Calcium regulation
  • Flow birefringence
  • Gelsolin
  • Phosphorylation
  • Protein engineering

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