Microtubule association of EML proteins and the EML4-ALK variant 3 oncoprotein require an N-terminal trimerization domain-Reference-Cited by-同舟云学术

Microtubule association of EML proteins and the EML4-ALK variant 3 oncoprotein require an N-terminal trimerization domain

Published:2015-04-17 Issue:3 Volume:467 Page:529-536
ISSN:0264-6021
Container-title:Biochemical Journal
language:en
Short-container-title:

Author:

Richards Mark W.¹,O'Regan Laura¹,Roth Daniel²,Montgomery Jessica M.¹,Straube Anne²,Fry Andrew M.¹,Bayliss Richard¹

Affiliation:

1. Department of Biochemistry, University of Leicester, Henry Wellcome Building, Lancaster Road, Leicester LE1 9HN, U.K.

2. Centre for Mechanochemical Cell Biology, Warwick Medical School, University of Warwick, Gibbet Hill Road, Coventry CV4 7AL, U.K.

Abstract

We present crystal structures of a trimeric coiled-coil domain found in echinoderm microtubule (MT)-associated protein (EMAP)-like (EML) proteins. This trimerization domain (TD) mediates self-association and interactions between a subset of EML proteins. MT-association of EML proteins requires the TD and an adjacent basic region.

Publisher

Portland Press Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry

Link

https://portlandpress.com/biochemj/article-pdf/467/3/529/682109/bj4670529.pdf

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