Content area

Abstract

Issue Title: SUMOylation in Neuroplasticity and Neurological Disorders

Small ubiquitin-like modifiers (SUMOs) are polypeptides resembling ubiquitin that are covalently attached to specific lysine residue of target proteins through a specific enzymatic pathway. Sumoylation is now seen as a key posttranslational modification involved in many biological processes, but little is known about how this highly dynamic protein modification is regulated in the brain. Disruption of the sumoylation enzymatic pathway during the embryonic development leads to lethality revealing a pivotal role for this protein modification during development. The main aim of this review is to briefly describe the SUMO pathway and give an overview of the sumoylation regulations occurring in brain development, neuronal morphology and synapse formation. [PUBLICATION ABSTRACT]

Details

Title
Protein Sumoylation in Brain Development, Neuronal Morphology and Spinogenesis
Author
Gwizdek, Carole; Cassé, Frédéric; Martin, Stéphane
Pages
677-91
Publication year
2013
Publication date
Dec 2013
Publisher
Springer Nature B.V.
ISSN
15351084
e-ISSN
15591174
Source type
Scholarly Journal
Language of publication
English
ProQuest document ID
1449256209
Copyright
Springer Science+Business Media New York 2013