Review
Nature Reviews Neuroscience 8, 948-959 (December 2007) | doi:10.1038/nrn2276
Emerging extranuclear roles of protein SUMOylation in neuronal function and dysfunction
Stéphane Martin1, Kevin A. Wilkinson1, Atsushi Nishimune1 & Jeremy M. Henley1 About the authors
Abstract
Post-translational protein modifications are integral components of signalling cascades that enable cells to efficiently, rapidly and reversibly respond to extracellular stimuli. These modifications have crucial roles in the CNS, where the communication between neurons is particularly complex. SUMOylation is a post-translational modification in which a member of the small ubiquitin-like modifier (SUMO) family of proteins is conjugated to lysine residues in target proteins. It is well established that SUMOylation controls many aspects of nuclear function, but it is now clear that it is also a key determinant in many extranuclear neuronal processes, and it has also been implicated in a wide range of neuropathological conditions.
- View At a Glance
Author affiliations
- MRC Centre for Synaptic Plasticity, Department of Anatomy, School of Medical Sciences, University of Bristol, University Walk, Bristol, BS8 1TD, UK
Correspondence to: Jeremy M. Henley1 Email: J.M.Henley@bristol.ac.uk
MORE ARTICLES LIKE THIS
These links to content published by NPG are automatically generated.
NEWS AND VIEWS
Beginning at the end with SUMONature Structural & Molecular Biology News and Views (01 Jul 2005)
Breaking up with a kinky SUMONature Structural & Molecular Biology News and Views (01 Dec 2006)
See all 6 matches for News And ViewsRESEARCH
Unconventional tethering of Ulp1 to the transport channel of the nuclear pore complex by karyopherinsNature Cell Biology Article (01 Jan 2003)
See all 58 matches for Research
