TRIM5 alpha cytoplasmic bodies are highly dynamic structures

Edward M Campbell, Mark P Dodding, Melvyn W Yap, Xiaolu Wu, Sarah Gallois-Montbrun, Michael H Malim, Jonathan P Stoye, Thomas J Hope

Research output: Contribution to journalArticle (Academic Journal)peer-review

55 Citations (Scopus)

Abstract

Tripartite motif (TRIM)5 alpha has recently been identified as a host restriction factor that has the ability to block infection by certain retroviruses in a species-dependent manner. One interesting feature of this protein is that it is localized in distinct cytoplasmic clusters designated as cytoplasmic bodies. The potential role of these cytoplasmic bodies in TRIM5 alpha function remains to be defined. By using fluorescent fusion proteins and live cell microscopy, we studied the localization and dynamics of TRIM5 alpha cytoplasmic bodies. This analysis reveals that cytoplasmic bodies are highly mobile, exhibiting both short saltatory movements and unidirectional long-distance movements along the microtubule network. The morphology of the cytoplasmic bodies is also dynamic. Finally, photobleaching and photoactivation analysis reveals that the TRIM5 alpha protein present in the cytoplasmic bodies is very dynamic, rapidly exchanging between cytoplasmic bodies and a more diffuse cytoplasmic population. Therefore, TRIM5 alpha cytoplasmic bodies are dynamic structures more consistent with a role in function or regulation rather than protein aggregates or inclusion bodies that represent dead-end static structures.

Original languageEnglish
Pages (from-to)2102-11
Number of pages10
JournalMolecular Biology of the Cell
Volume18
Issue number6
DOIs
Publication statusPublished - Jun 2007

Keywords

  • Animals
  • Carrier Proteins
  • Cell Line
  • Cytoplasm
  • Cytoskeleton
  • Fluorescence Recovery After Photobleaching
  • Humans
  • Inclusion Bodies
  • Microscopy, Fluorescence
  • Microtubules
  • Recombinant Fusion Proteins
  • Journal Article
  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

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