title: Activity-dependent SUMOylation of the brain-specific scaffolding protein GISP.
abstract: G-protein coupled receptor interacting scaffold protein (GISP) is a multi-domain, brain-specific protein derived from the A-kinase anchoring protein (AKAP)-9 gene. Using yeast two-hybrid screens to identify GISP interacting proteins we isolated the SUMO conjugating enzyme Ubc9. GISP interacts with Ubc9 in vitro, in heterologous cells and in neurons. SUMOylation is a post-translational modification in which the small protein SUMO is covalently conjugated to target proteins, modulating their function. Consistent with its interaction with Ubc9, we show that GISP is SUMOylated by both SUMO-1 and SUMO-2 in both in vitro SUMOylation assays and in mammalian cells. Intriguingly, SUMOylation of GISP in neurons occurs in an activity-dependent manner in response to chemical LTP. These data suggest that GISP is a novel neuronal SUMO substrate whose SUMOylation status is modulated by neuronal activity.
authors: MRC Centre for Synaptic Plasticity, School of Biochemistry, Medical Sciences Building, University of Bristol, Bristol BS8 1TD, UK.
authors: Sriharsha
authors: S
authors: Kantamneni
authors: Kevin A
authors: KA
authors: Wilkinson
authors: Nadia
authors: N
authors: Jaafari
authors: Emi
authors: E
authors: Ashikaga
authors: Daniel
authors: D
authors: Rocca
authors: Philip
authors: P
authors: Rubin
authors: Susan C
authors: SC
authors: Jacobs
authors: Atsushi
authors: A
authors: Nishimune
authors: Jeremy M
authors: JM
authors: Henley
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