WWW.JNEUROSCI.ORG
-
The Journal of Neuroscience MBF Stereo Investigator
QUICK SEARCH:   [advanced]


     
-


HOME  |   SEARCH  |   ARCHIVE  |   SUBSCRIBE  |   CONTACT  |   HELP
The Journal of Neuroscience, June 30, 2004, 24(26):5881-5891; doi:10.1523/JNEUROSCI.1037-04.2004

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Submit an eLetter
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via ISI Web of Science (56)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Keller, C. A.
Right arrow Articles by Lüscher, B.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Keller, C. A.
Right arrow Articles by Lüscher, B.

 Previous Article  |  Next Article 

Cellular/Molecular
The {gamma}2 Subunit of GABAA Receptors Is a Substrate for Palmitoylation by GODZ

Cheryl A. Keller,1 Xu Yuan,1 Patrizia Panzanelli,2 Michelle L. Martin,1 Melissa Alldred,1 Marco Sassoè-Pognetto,2 and Bernhard Lüscher1

1Departments of Biology and Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802, 2Department of Anatomy, Pharmacology and Forensic Medicine, and 3Rita Levi Montalcini Center for Brain Repair, University of Turin, I-10126 Turin, Italy

The neurotransmitter GABA activates heteropentameric GABAA receptors, which are composed mostly of {alpha}, {beta}, and {gamma}2 subunits. Regulated membrane trafficking and subcellular targeting of GABAA receptors is important for determining the efficacy of GABAergic inhibitory function. Of special interest is the {gamma}2 subunit, which is mostly dispensable for assembly and membrane insertion of functional receptors but essential for accumulation of GABAA receptors at synapses. In a search for novel receptor trafficking proteins, we have used the SOS-recruitment system and isolated a Golgi-specific DHHC zinc finger protein (GODZ) as a novel {gamma}2 subunit-interacting protein. GODZ is a member of the superfamily of DHHC cysteine-rich domain (DHHC-CRD) polytopic membrane proteins shown recently in yeast to represent palmitoyltransferases. GODZ mRNA is found in many tissues; however, in brain the protein is detected in neurons only and highly concentrated and asymmetrically distributed in the Golgi complex. GODZ interacts with a cysteine-rich 14-amino acid domain conserved specifically in the large cytoplasmic loop of {gamma}1-3 subunits but not in other GABAA receptor subunits. Coexpression of GODZ and GABAA receptors in heterologous cells results in palmitoylation of the {gamma}2 subunit in a cytoplasmic loop domain-dependent manner. Neuronal GABAA receptors are similarly palmitoylated. Thus, GODZ-mediated palmitoylation represents a novel posttranslational modification that is selective for{gamma} subunit-containing GABAA receptor subtypes, a mechanism that is likely to be important for regulated trafficking of these receptors in the secretory pathway.

Key words: PAT; trafficking; exocytosis; palmitoyltransferase; SERZ-{beta}; GABA

Received March 21, 2004; revised April 26, 2004; accepted May 17, 2004.






-

Home  |   Search  |   Archive  |   Subscribe  |   Contact  |   Help
-
Copyright 2008 by Society for Neuroscience ONLINE ISSN: 1529-2401
-