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Titolo:
Rab2 requires PKC iota/lambda to recruit beta-COP for vesicle formation
Autore:
Tisdale, EJ;
Indirizzi:
Wayne State Univ, Sch Med, Dept Pharmacol, Detroit, MI 48201 USA Wayne State Univ Detroit MI USA 48201 pt Pharmacol, Detroit, MI 48201 USA
Titolo Testata:
TRAFFIC
fascicolo: 9, volume: 1, anno: 2000,
pagine: 702 - 712
SICI:
1398-9219(200009)1:9<702:RRPITR>2.0.ZU;2-M
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN-KINASE-C; ADP-RIBOSYLATION FACTOR; ESTER BINDING DOMAIN; ENDOPLASMIC-RETICULUM; GOLGI-APPARATUS; IN-VITRO; PERMEABILIZED CELLS; TRANSPORT VESICLES; PHOSPHOLIPASE-D; RBL-2H3 CELLS;
Keywords:
COPI; kinase; PKC iota/lambda; Rab2; vesicular transport;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
59
Recensione:
Indirizzi per estratti:
Indirizzo: Tisdale, EJ Wayne State Univ, Sch Med, Dept Pharmacol, 540 E Canfield Ave,Detroit, MI48201 USA Wayne State Univ 540 E Canfield Ave Detroit MI USA 48201 1 USA
Citazione:
E.J. Tisdale, "Rab2 requires PKC iota/lambda to recruit beta-COP for vesicle formation", TRAFFIC, 1(9), 2000, pp. 702-712

Abstract

The small GTPase Rab2 initiates the recruitment of soluble components necessary for protein sorting and recycling from pre-Golgi intermediates. Our previous studies showed that Rab2 required protein kinase C (PKC) or a PKC-like protein to recruit beta-COP to membrane (Tisdale EJ, Jackson NI. Rab2 protein enhances coatomer recruitment to pre-Golgi intermediates. J Bio Chem1998;273: 17269-17277). We investigated the role of PKC in Rab2 function by first determining the active isoform that associates with membranes used in our assay. Western blot analysis detected three isoforms: PKC alpha, gamma and iota/lambda. A quantitative binding assay was used to measure recruitment of these kinases when incubated with Rab2. Only PKC iota/lambda. translocated to membrane in a dose-dependent manner. Microsomes treated with anti-PKC iota/lambda. lost the ability to bind beta-COP, suggesting that Rab2requires PKC iota/lambda for beta-COP recruitment. The recruitment of beta-COP to membranes is not regulated by PKC iota/lambda kinase activity. However, PKC iota/lambda. kinase activity was necessary for Rab2-mediated vesicle budding. We found that the addition of either a kinase-deficient PKC iota/lambda mutant or atypical PKC pseudosubstrate peptide to the binding assay drastically reduced vesicle formation. These data suggest that Rab2 causes translocation of PKC iota/lambda. to vesicular tubular clusters (VTCs), which promotes the recruitment of COPI to generate retrograde-transport vesicles.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 23/01/21 alle ore 03:43:08