The microtubule-associated C-I subfamily of TRIM proteins and the regulation of polarized cell responses

Timothy C. Cox

Research output: Chapter in Book/Report/Conference proceedingChapter (Book)Otherpeer-review

3 Citations (Scopus)

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.

Original languageEnglish
Title of host publicationTRIM/RBCC Proteins
EditorsGermana Meroni
PublisherSpringer
Chapter8
Pages105-118
Number of pages14
Volume770
ISBN (Print)9781461453970
DOIs
Publication statusPublished - 2012

Publication series

NameAdvances in Experimental Medicine and Biology
Volume770
ISSN (Print)00652598

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