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Titolo:
Functional characterization of novel human ARFGAP3
Autore:
Liu, XQ; Zhang, CG; Xing, GC; Chen, QT; He, HC;
Indirizzi:
Chinese Natl Human Genome Ctr Beijing, Beijing Inst Radiat Med, Dept Genom& Proteom, Beijing 100850, Peoples R China Chinese Natl Human Genome Ctr Beijing Beijing Peoples R China 100850 ina Beijing Univ, Teaching Hosp 1, Dept Neurol, Beijing 100034, Peoples R China Beijing Univ Beijing Peoples R China 100034 jing 100034, Peoples R China
Titolo Testata:
FEBS LETTERS
fascicolo: 1-2, volume: 490, anno: 2001,
pagine: 79 - 83
SICI:
0014-5793(20010209)490:1-2<79:FCONHA>2.0.ZU;2-4
Fonte:
ISI
Lingua:
ENG
Soggetto:
GTPASE-ACTIVATING PROTEIN; ADP-RIBOSYLATION FACTOR; SACCHAROMYCES-CEREVISIAE; GOLGI MEMBRANES; CHOLERA-TOXIN; ARF; HYDROLYSIS; TRANSPORT; COMPLEX; BINDING;
Keywords:
vesicular transport; ADP ribosylation factor; GTPase-activating protein; secreted alkaline phosphatase;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
25
Recensione:
Indirizzi per estratti:
Indirizzo: He, HC Chinese Natl Human Genome Ctr Beijing, Beijing Inst Radiat Med, Dept Genom& Proteom, 27 Taiping Rd, Beijing 100850, Peoples R China Chinese Natl Human Genome Ctr Beijing 27 Taiping Rd Beijing Peoples R China 100850
Citazione:
X.Q. Liu et al., "Functional characterization of novel human ARFGAP3", FEBS LETTER, 490(1-2), 2001, pp. 79-83

Abstract

ADP ribosylation factors (ARFs) are critical in the vesicular trafficking pathway. ARF activity is controlled by GTPase-activating proteins (GAPs). We have identified recently a novel tentative ARF GAP derived from human fetal liver, ARFGAP3 (originally named as ARFGAP1). In the present study, we demonstrated that ARFGAP3 had GAP activity in vitro and remarked that the GAP activity of ARFGAP3 was regulated by phospholipids, i.e. phosphatidylinositol 4,5-diphosphate as agonist and phosphatidylcholine as antagonist. ARFGAP3 is a predominantly cytosolic protein, and concentrated in the perinuclear region. Its transient ectopic overexpression in cultured mammalian cellsreduced the constitutive secretion of secreted alkaline phosphatase, indicating that ectopic overexpression of ARFGAP3 inhibits the early secretory pathway of proteins in vitro. These results demonstrated that ARFGAP3 is a novel GAP for ARF1 and might be involved in intracellular traffic of proteins and vesicular transport as predicted. (C) 2001 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/01/21 alle ore 12:31:03