Phosphorylation-regulated inhibition of the Gz GTPase-activating protein activity of RGS proteins by synapsin I.

Phosphorylation-regulated inhibition of the Gz GTPase-activating protein activity of RGS proteins by synapsin I. Research Abstract Details 

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Phosphorylation-regulated inhibition of the Gz GTPase-activating protein activity of RGS proteins by synapsin I. Abstract Text:

Yaping Tu,Surendra K Nayak,Jimmy Woodson,Elliott M Ross,

Synapsins are neuronal proteins that bind and cluster synaptic vesicles in the presynaptic space, presumably by anchoring to actin filaments, but specific regulatory functions of the synapsins are unknown. We found that a sub-population of brain synapsin Ia, a splice variant of one of three synapsin isoforms, inhibits the GTPase-activating protein (GAP) activity of several RGS proteins. Inhibition is highly selective for Galphaz, a member of the Gi family that is found in neurons, platelets, adrenal chromaffin cells, and a few other neurosecretory cells. Gz has been indirectly implicated in the regulation of secretion. Synapsin Ia constitutes a major fraction of the total GAP-inhibitory activity in brain, and its inhibitory activity is absent from the brains of synapsin I(-/-)/II(-/-) mice. Inhibition depends on the cationic D/E domain of synapsin. Phosphorylation of synapsin Ia at serine 9 by either cyclic AMP-dependent protein kinase or p21-activated protein kinase (PAK1) attenuates its potency as a GAP inhibitor more than 7-fold. Synapsin can thus act as a phosphorylation-modulated mediator of feedback regulation of Gz signaling by the synaptic machinery.

Phosphorylation-regulated inhibition of the Gz GTPase-activating protein activity of RGS proteins by synapsin I. Publishing Authors By Initials

Y Tu,SK Nayak,J Woodson,EM Ross,

For similar enzymes and coenzymes: enzymes: transferases: phosphotransferases: phosphotransferases (alcohol group acceptor): protein kinases: protein-serine-threonine kinases: p21-activated kinases research abstracts see: enzymes and coenzymes: enzymes: transferases: phosphotransferases: phosphotransferases (alcohol group acceptor): protein kinases: protein-serine-threonine kinases: p21-activated kinases research

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Phosphorylation-regulated inhibition of the Gz GTPase-activating protein activity of RGS proteins by synapsin I. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: The Journal of biological chemistry

VOLUME: 278

Page Numbers: 52273-81

Journal Abbreviation: J. Biol. Chem.

ISSN: 0021-9258

DAY: 13

MONTH: 10

YEAR: 2003

Phosphorylation-regulated inhibition of the Gz GTPase-activating protein activity of RGS proteins by synapsin I. Information

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LANGUAGE: eng

NlmUniqueID: 2985121

Phosphorylation-regulated inhibition of the Gz GTPase-activating protein activity of RGS proteins by synapsin I. Keywords Mesh Terms:

KEYWORDS: p21-Activated Kinases

MESH TERMS: pharmacology

Chemical & Substance for Abstract: Phosphorylation-regulated inhibition of the Gz GTPase-activating protein activity of RGS proteins by synapsin I. Information

Substance Name: Heterotrimeric GTP-Binding Proteins

Registry Number: EC 3.6.1.46

Grant and Affiliation Information for Phosphorylation-regulated inhibition of the Gz GTPase-activating protein activity of RGS proteins by synapsin I.

AFFILIATION: Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, Texas 75390-9041, USA.

Country: United States

AGENCY: United States NIGMS

GRANT: GM30355

ACRONYM: GM

MEDLINETA: J Biol Chem

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