Protein Sumoylation in Brain Development, Neuronal Morphology and Spinogenesis

被引：26
|
作者：
Gwizdek, Carole [1 ]
Casse, Frederic [1 ]
Martin, Stephane [1 ]
机构：
[1] Univ Nice Sophia Antipolis, Ctr Natl Rech Sci, Inst Pharmacol Mole & Cellulaire,UMR7275, Lab Excellence Network Innovat Signal Transduct P, F-06560 Valbonne, France
来源：
NEUROMOLECULAR MEDICINE | 2013年 / 15卷 / 04期
关键词：
Posttranslational modification; Sumoylation; Brain development; Synapse formation; SUMO E3 LIGASE; UBIQUITIN LIGASE; TRANSCRIPTIONAL ACTIVITY; IN-VITRO; GENE; CONJUGATION; RECEPTOR; BINDING; PIAS1; UBC9;
D O I：
10.1007/s12017-013-8252-z
中图分类号：
Q189 [神经科学];
学科分类号：
071006 ;
摘要：
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.
引用
收藏
页码：677 / 691
页数：15
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