The F-actin filament capping protein CapG is a bona fide nucleolar protein

Biochem Biophys Res Commun. 2008 Dec 12;377(2):699-704. doi: 10.1016/j.bbrc.2008.10.048. Epub 2008 Oct 18.

Abstract

Actin works in concert with myosin I to regulate the transcription of ribosomal genes in the nucleolus. Recently, nucleolar actin has been shown to be active in its polymeric form raising the question how actin dynamics is regulated in the nucleolus. Here, we show that the actin capping protein CapG localizes in the nucleolus of cultured cells. CapG transport to the nucleolus is an active and ATP-dependent process. Association of CapG with the nucleolus requires active RNA Polymerase I transcription. In addition, we show that activated Ran GTPase, an interaction partner of CapG, is also transported to the nucleolus. A constitutively active Ran mutant promotes CapG accumulation in the nucleolus indicating that CapG transport to the nucleolus can be supported by Ran. Our results suggest that filamentous actin in the nucleolus might be regulated by actin binding proteins such as CapG.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actin Cytoskeleton / metabolism*
  • Actins / metabolism*
  • Cell Line
  • Cell Nucleolus / metabolism*
  • Humans
  • Microfilament Proteins / genetics
  • Microfilament Proteins / metabolism*
  • Nuclear Proteins / genetics
  • Nuclear Proteins / metabolism*
  • Protein Transport
  • RNA Polymerase I / metabolism
  • ran GTP-Binding Protein / genetics
  • ran GTP-Binding Protein / metabolism

Substances

  • Actins
  • Microfilament Proteins
  • Nuclear Proteins
  • CAPG protein, human
  • RNA Polymerase I
  • ran GTP-Binding Protein