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The Microtubule-Associated C-I Subfamily of TRIM Proteins and the Regulation of Polarized Cell Responses

  • Timothy C. Cox
Chapter
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 770)

Abstract

TRIM proteins are multidomain proteins that typically assemble into large molecular complexes, the composition of which likely explains the diverse functions that have been attributed to this group of proteins. Accumulating data on the roles of many TRIM proteins supports the notion that those that share identical C-terminal domain architectures participate in the regulation of similar cellular processes. At least nine different C-terminal domain compositions have been identified. This chapter will focus on one subgroup that possess a COS motif, FNIII and SPRY/B30.2 domain as their C-terminal domain arrangement. This C-terminal domain architecture plays a key role in the interaction of all six members of this subgroup with the microtubule cytoskeleton. Accumulating evidence on the functions of some of these proteins will be discussed to highlight the emerging similarities in the cellular events in which they participate.

Keywords

Snare Complex Microtubule Cytoskeleton Ubiquitin Ligase Activity Trim Protein Vesicle Exocytosis 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Landes Bioscience and Springer Science+Business Media, LLC 2012

Authors and Affiliations

  • Timothy C. Cox
    • 1
    • 2
    • 3
  1. 1.Division of Craniofacial Medicine, Department of PediatricsUniversity of WashingtonUSA
  2. 2.Center for Tissue and Cell SciencesSeattle Children’s Research InstituteSeattleUSA
  3. 3.Department of Anatomy and Developmental BiologyMonash UniversityClaytonAustralia

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