Activity-dependent SUMOylation of the brain-specific scaffolding protein GISP

S Kantamneni, KA Wilkinson, N Jaafari, E Ashikaga, D Rocca, P Rubin, SC Jacobs, A Nishimune, JM Henley

Research output: Contribution to journalArticle (Academic Journal)peer-review

17 Citations (Scopus)


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.
Translated title of the contributionActivity-dependent SUMOylation of the brain-specific scaffolding protein GISP
Original languageEnglish
Pages (from-to)657 - 662
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume409 (4)
Publication statusPublished - Jun 2011


Dive into the research topics of 'Activity-dependent SUMOylation of the brain-specific scaffolding protein GISP'. Together they form a unique fingerprint.

Cite this