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Titolo:
GAIP IS MEMBRANE-ANCHORED BY PALMITOYLATION AND INTERACTS WITH THE ACTIVATED (GTP-BOUND) FORM OF G-ALPHA(I) SUBUNITS
Autore:
DEVRIES L; ELENKO E; HUBLER L; JONES TLZ; FARQUHAR MG;
Indirizzi:
UNIV CALIF SAN DIEGO,DIV CELLULAR & MOL MED LA JOLLA CA 92093 UNIV CALIF SAN DIEGO,DIV CELLULAR & MOL MED LA JOLLA CA 92093 UNIV CALIF SAN DIEGO,DEPT PATHOL LA JOLLA CA 92093 NIDDK,METAB DIS BRANCH,NIH BETHESDA MD 20892
Titolo Testata:
Proceedings of the National Academy of Sciences of the United Statesof America
fascicolo: 26, volume: 93, anno: 1996,
pagine: 15203 - 15208
SICI:
0027-8424(1996)93:26<15203:GIMBPA>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
CYSTEINE-STRING PROTEIN; NIH 3T3 CELLS; ENDOPLASMIC-RETICULUM; SIGNAL-TRANSDUCTION; CRYSTAL-STRUCTURE; ADENYLYL CYCLASE; ESCHERICHIA-COLI; BETA-COP; GS-ALPHA; MUTATIONS;
Keywords:
G PROTEIN; REGULATOR OF G-PROTEIN SIGNALING; GTPASE-ACTIVATING PROTEIN; CYSTEINE STRING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
56
Recensione:
Indirizzi per estratti:
Citazione:
L. Devries et al., "GAIP IS MEMBRANE-ANCHORED BY PALMITOYLATION AND INTERACTS WITH THE ACTIVATED (GTP-BOUND) FORM OF G-ALPHA(I) SUBUNITS", Proceedings of the National Academy of Sciences of the United Statesof America, 93(26), 1996, pp. 15203-15208

Abstract

GAIP (G Alpha Interacting Protein) is a member of the recently described RGS (Regulators of G-protein Signaling) family that was isolated by interaction cloning with the heterotrimeric G-protein G alpha(i3) and was recently shown to be a GTPase-activating protein (GAP). In AtT-20 cells stably expressing GAIP, we found that GAIP is membrane-anchored and faces the cytoplasm, because it was not released by sodium carbonate treatment but was digested by proteinase K, When Cos cells were transiently transfected with GAIP and metabolically labeled with [S-35]methionine, two pools of GAIP-a soluble and a membrane-anchored pool-were found, Since the N terminus of GAIP contains a cysteine string motif and cysteine string proteins are heavily palmitoylated, we investigated the possibility that membrane-anchored GAIP might be palmitoylated, We found that after labeling with [H-3] palmitic acid, the membrane-anchored pool but not the soluble pool was palmitoylated, In the yeast two-hybrid system, GAIP was found to interact specifically with members of the G alpha(i) subfamily, G alpha(i1), G alpha(i2), G alpha(i3), G alpha(z), and G alpha(o), but not with members of other G alpha subfamilies, G alpha(s), G alpha(q), and G alpha(12/13). The C terminus of G alpha(i3) is important for binding because a 10-aa C-terminal truncation and a point mutant of G alpha(i3) showed significantly diminished interaction, GAIP interacted preferentially with the activated (GTP) form of G alpha(i3), which is in keeping with its GAP activity, We conclude that GAIP is a membrane-anchored GAP with a cysteine string motif, This motif, present in cysteine string proteins found on synaptic vesicles, pancreatic zymogen granules, and chromaffin granules, suggests GAIP's possible involvement in membrane trafficking.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/01/21 alle ore 03:23:56