A new twist to coiled coil

FEBS Letters
Elisabeth Le RumeurSteve J Winder

Abstract

Spectrin repeats have been largely considered as passive linkers or spacers with little functional role other than to convey flexibility to a protein. Whilst this is undoubtedly part of their function, it is by no means all. Whilst the overt structure of all spectrin repeats is a simple triple-helical coiled coil, the linkages between repeats and the surface properties of repeats vary widely. Spectrin repeats in different proteins can act as dimerisation interfaces, platforms for the recruitment of signalling molecules, and as a site for the interaction with cytoskeletal elements and even direct association with membrane lipids. In the case of dystrophin several of these functions overlap in the space of a few repeats.

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Citations

Nov 28, 2012·Proceedings of the National Academy of Sciences of the United States of America·Yi LaiDongsheng Duan
Mar 4, 2014·Human Gene Therapy·William LostalDongsheng Duan
Feb 27, 2014·Cellular & Molecular Biology Letters·Dżamila M BogusławskaAleksander Czogalla
Jan 21, 2014·Biochimica Et Biophysica Acta·Sarah Ameziane-Le HirVéronique Vié
May 15, 2015·Molecular Biology of the Cell·Mirjam KetemaArnoud Sonnenberg
Jul 2, 2016·The FEBS Journal·Katharine M WrightMichael A Massiah

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