Protein SUMOylation in spine structure and function

TJ Craig, JM Henley

Research output: Contribution to journalArticle (Academic Journal)

25 Citations (Scopus)

Abstract

The active regulation of spine structure and function is of fundamental importance for information storage in the brain. Many proteins involved in spine development and activitydependent remodelling are potential or validated substrates for modification by the Small Ubiquitin-like Modifier (SUMO). The functional consequences of neuronal protein SUMOylation appear diverse and, in many cases, have not yet been determined. However, for several proteins SUMOylation has been shown to be a key regulator, which has a profound impact on spine dynamics and protein trafficking and function. Here we provide an overview of neuronal SUMOylation and discuss how greater understanding of this relatively recently discovered posttranslational modification will provide insight into the complexity of protein interactions that control synaptic activity and dysfunction.
Translated title of the contributionProtein SUMOylation in spine structure and function
Original languageEnglish
JournalCurrent Opinion in Neurobiology
DOIs
Publication statusPublished - 2012

Bibliographical note

Other: In Press

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