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

Thomas Hubert (UGent) , Katrien Van Impe (UGent) , Joël Vandekerckhove (UGent) and Jan Gettemans (UGent)
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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. (C)
Keywords
GTPase, CapG, Actin, Nucleolus, Ran

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Chicago
Hubert, Thomas, Katrien Van Impe, Joël Vandekerckhove, and Jan Gettemans. 2008. “The F-actin Filament Capping Protein CapG Is a Bona Fide Nucleolar Protein.” Biochemical and Biophysical Research Communications 377 (2): 699–704.
APA
Hubert, T., Van Impe, K., Vandekerckhove, J., & Gettemans, J. (2008). The F-actin filament capping protein CapG is a bona fide nucleolar protein. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 377(2), 699–704.
Vancouver
1.
Hubert T, Van Impe K, Vandekerckhove J, Gettemans J. The F-actin filament capping protein CapG is a bona fide nucleolar protein. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS. SAN DIEGO, CA 92101-4495 USA: ACADEMIC PRESS INC ELSEVIER SCIENCE; 2008;377(2):699–704.
MLA
Hubert, Thomas et al. “The F-actin Filament Capping Protein CapG Is a Bona Fide Nucleolar Protein.” BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS 377.2 (2008): 699–704. Print.
@article{513969,
  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. (C)},
  author       = {Hubert, Thomas and Van Impe, Katrien and Vandekerckhove, Jo{\"e}l and Gettemans, Jan},
  issn         = {0006-291X},
  journal      = {BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS},
  language     = {eng},
  number       = {2},
  pages        = {699--704},
  publisher    = {ACADEMIC PRESS INC ELSEVIER SCIENCE},
  title        = {The F-actin filament capping protein CapG is a bona fide nucleolar protein},
  url          = {http://dx.doi.org/10.1016/j.bbrc.2008.10.048},
  volume       = {377},
  year         = {2008},
}

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