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Titolo:
Recruitment of coat-protein-complex proteins on to phagosomal membranes isregulated by a brefeldin A-sensitive ADP-ribosylation factor
Autore:
Beron, W; Mayorga, LS; Colombo, MI; Stahl, PD;
Indirizzi:
Univ Nacl Cuyo, CONICET, Inst Histol & Embriol, RA-5500 Mendoza, ArgentinaUniv Nacl Cuyo Mendoza Argentina RA-5500 iol, RA-5500 Mendoza, Argentina Washington Univ, Sch Med, Dept Cell Biol & Physiol, St Louis, MO 63110 USAWashington Univ St Louis MO USA 63110 l & Physiol, St Louis, MO 63110 USA
Titolo Testata:
BIOCHEMICAL JOURNAL
, volume: 355, anno: 2001,
parte:, 2
pagine: 409 - 415
SICI:
0264-6021(20010415)355:<409:ROCPOT>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
GTP-BINDING PROTEINS; CELL-FREE SYSTEM; GOLGI MEMBRANES; ENDOPLASMIC-RETICULUM; GUANINE-NUCLEOTIDE; PLASMA-MEMBRANE; BETA-COP; TRANSPORT VESICLES; ENDOSOME FUSION; EPSILON-COP;
Keywords:
phagocytosis; phagosomes; recycling; vesicular transport;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
54
Recensione:
Indirizzi per estratti:
Indirizzo: Beron, W Univ Nacl Cuyo, CONICET, Inst Histol & Embriol, Casilla Correo 56, RA-5500Mendoza, Argentina Univ Nacl Cuyo Casilla Correo 56 Mendoza Argentina RA-5500 ntina
Citazione:
W. Beron et al., "Recruitment of coat-protein-complex proteins on to phagosomal membranes isregulated by a brefeldin A-sensitive ADP-ribosylation factor", BIOCHEM J, 355, 2001, pp. 409-415

Abstract

Particle internalization in macrophages is followed by a complex maturation process. We have previously observed that proteins bound to phagocytosed particles are sorted from phagosomes into a heterogeneous population of vesicles that fuse with endosomes. However, the mechanism and the protein machinery involved in the formation of these phagosome-derived vesicles are largely unknown. It has been shown that vesicles coated with coat protein complex type I (COPI) have a role in both secretion and endocytosis. To addressthe possibility that COPI proteins might participate in the formation of phagosome-derived vesicles we studied the recruitment of beta -COP to highlypurified phagosomes. The binding of beta -COP to phagosomal membranes was regulated by nucleotides and inhibited by brefeldin A (BFA). An ADP-ribosylation factor 1 (ARF1) mutant defective in GTP hydrolysis supported the binding of beta -COP to phagosomes independently of added nucleotide. AlF, and G beta gamma subunits, agents known to modulate heterotrimeric G-protein activity, were tested in the beta -COP binding assay. A1F, increased beta -COP association, whereas binding was inhibited by the addition of G beta gamma subunits. Our results suggest that COP proteins are recruited to phagosomal membranes by a mechanism that involves heterotrimeric GTP-binding proteins and a BFA-sensitive ARF. In addition, our findings indicate that COPI proteins are involved in the recycling of components from phagosomes to the cell surface.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/01/21 alle ore 11:55:34