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Titolo:
Membrane-associated GAIP is a phosphoprotein and can be phosphorylated by clathrin-coated vesicles
Autore:
Fischer, T; Elenko, E; Wan, L; Thomas, G; Farquhar, MG;
Indirizzi:
Univ Calif San Diego, Dept Cellular & Mol Med, La Jolla, CA 92093 USA UnivCalif San Diego La Jolla CA USA 92093 ol Med, La Jolla, CA 92093 USA Univ Calif San Diego, Dept Pathol, La Jolla, CA 92093 USA Univ Calif San Diego La Jolla CA USA 92093 Pathol, La Jolla, CA 92093 USA Oregon Hlth Sci Univ, Vollum Inst, Portland, OR 97201 USA Oregon Hlth Sci Univ Portland OR USA 97201 m Inst, Portland, OR 97201 USA
Titolo Testata:
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
fascicolo: 8, volume: 97, anno: 2000,
pagine: 4040 - 4045
SICI:
0027-8424(20000411)97:8<4040:MGIAPA>2.0.ZU;2-A
Fonte:
ISI
Lingua:
ENG
Soggetto:
CASEIN KINASE-II; MYRISTOYL-ELECTROSTATIC SWITCH; GTPASE-ACTIVATING PROTEIN; HETEROTRIMERIC G-PROTEINS; ACTIVITY IN-VITRO; BINDING-PROTEIN; PLASMA-MEMBRANE; MAP KINASE; RGS-GAIP; INTERACTS;
Keywords:
G proteins; regulator of G protein signaling; casein kinase 2;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
49
Recensione:
Indirizzi per estratti:
Indirizzo: Farquhar, MG Univ Calif San Diego, Dept Cellular & Mol Med, La Jolla, CA 92093 USA Univ Calif San Diego La Jolla CA USA 92093 lla, CA 92093 USA
Citazione:
T. Fischer et al., "Membrane-associated GAIP is a phosphoprotein and can be phosphorylated by clathrin-coated vesicles", P NAS US, 97(8), 2000, pp. 4040-4045

Abstract

GAIP (G alpha interacting protein) is a member of the RCS (regulators of Gprotein signaling) family and accelerates the turnover of GTP bound to G alpha i, G alpha q, and G alpha 13, There are two pools of GAIP-a soluble and a membrane-anchored pool. The membrane-anchored pool is found on clathrin-coated vesicles (CCVs) and pits in rat liver and AtT-20 pituitary cells. By treatment of a GAIP-enriched rat liver fraction with alkaline phosphatase, we found that membrane-bound GAIP is phosphorylated. By immunoprecipitation carried out on [P-32]orthophosphate-labeled AtT-20 pituitary cells stably expressing GAIP, P-32-labeling was associated exclusively with the membrane pool of GAIP, Phosphoamino acid analysis revealed that phosphorylation of GAIP occurred largely on serine residues. Recombinant GAIP could be phosphorylated at its N terminus with purified casein kinase 2 (CK2). It could also be phosphorylated by isolated CCVs in vitro. Phosphorylation was Mn2+-dependent, using both purified CK2 and CCVs. Ser-24 was identified as one ofthe phosphorylation sites. Our results establish that GAIP is phosphorylated and that only the membrane pool is phosphorylated, suggesting that GAIP can he regulated by phosphorylation events taking place at the level of clathrin-coated pits and vesicles.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 22/01/21 alle ore 04:07:07