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Am J Physiol Gastrointest Liver Physiol 297: G806-G813, 2009. First published August 13, 2009; doi:10.1152/ajpgi.00279.2009 Free Article
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NEUROREGULATION AND MOTILITY

Role of PSD95 in membrane association and catalytic activity of nNOS{alpha} in nitrergic varicosities in mice gut

Arun Chaudhury, Xue-Dao He, and Raj K. Goyal

Center for Swallowing and Motility Disorders, Gastrointestinal Division, Veterans Affairs Boston Healthcare System and Harvard Medical School, Boston, Massachusetts

Submitted July 14, 2009 ; accepted in final form August 13, 2009

We have recently shown that membrane association of neuronal nitric oxide synthase-{alpha} (nNOS{alpha}) is critical in the regulation of synthesis of NO during nitrergic neurotransmission. The purpose of this study was to examine the role of the synapse-associated proteins (SAPs) in membrane association of nNOS{alpha}. Varicosities (swellings on terminal axons) were isolated from mice gastrointestinal tract and examined for nNOS{alpha}, postsynaptic density protein 95 (PSD95), and membrane interactions by coimmunoprecipitation and SDS-PAGE. Our results show that PSD95 protein was present in the membrane fraction of the nerve varicosity, whereas both PSD95 and SAP97 were present in the cytosol. nNOS{alpha} was associated with PSD95 but not SAP97. nNOS{alpha}-PSD95 complex was bound to the membrane via palmitoylation of PSD95. Depalmitoylation of PSD95 with 2-bromopalmitate dislocates nNOS{alpha} and PSD95 from the varicosity membrane and abolishes NO production. These studies show that palmitoylation of PSD95 anchors nNOS{alpha} to the varicosity membrane and that it is obligatory for NO production by the enzyme. Palmitoylation of PSD95 may provide a novel target for regulation of nitrergic neurotransmission.

postsynaptic density protein; palmitoylation; synapse-associated protein; neuronal nitric oxide synthase; membrane-bound nNOS


Address for reprint requests and other correspondence: R. Goyal, VA Medical Ctr., 1400 VFW Parkway, West Roxbury, MA 02132, (e-mail: raj_goyal{at}hms.harvard.edu).






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