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Titolo:
The GRIP domain is a specific targeting sequence for a population of trans-Golgi network derived tubulo-vesicular carriers
Autore:
Brown, DL; Heimann, K; Lock, J; Kjer-Nielsen, L; van Vliet, C; Stow, JL; Gleeson, PA;
Indirizzi:
Monash Univ, Sch Med, Dept Pathol & Immunol, Prahran, Vic 3181, Australia Monash Univ Prahran Vic Australia 3181 unol, Prahran, Vic 3181, Australia Univ Queensland, Inst Mol Biosci, Brisbane, Qld 4072, Australia Univ Queensland Brisbane Qld Australia 4072 Brisbane, Qld 4072, Australia Univ Queensland, Dept Biochem, Brisbane, Qld 4072, Australia Univ Queensland Brisbane Qld Australia 4072 Brisbane, Qld 4072, Australia
Titolo Testata:
TRAFFIC
fascicolo: 5, volume: 2, anno: 2001,
pagine: 336 - 344
SICI:
1398-9219(200105)2:5<336:TGDIAS>2.0.ZU;2-4
Fonte:
ISI
Lingua:
ENG
Soggetto:
COILED-COIL PROTEINS; PLASMA-MEMBRANE; MOLECULAR CHARACTERIZATION; INTRACELLULAR-TRANSPORT; LIVING CELLS; IN-VIVO; VESICLES; COMPLEX; RAB6; FUSION;
Keywords:
trans-Golgi network; tubulo-vesicular; GRIP; p230; targeting sequence; vesicle budding; tethering;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
43
Recensione:
Indirizzi per estratti:
Indirizzo: Gleeson, PA Monash Univ, Sch Med, Dept Pathol & Immunol, Prahran, Vic 3181, Australia Monash Univ Prahran Vic Australia 3181 n, Vic 3181, Australia
Citazione:
D.L. Brown et al., "The GRIP domain is a specific targeting sequence for a population of trans-Golgi network derived tubulo-vesicular carriers", TRAFFIC, 2(5), 2001, pp. 336-344

Abstract

Vesicular carriers for intracellular transport associate with unique sets of accessory molecules that dictate budding and docking on specific membrane domains. Although many of these accessory molecules are peripheral membrane proteins, in most cases the targeting sequences responsible for their membrane recruitment have yet to be identified. We have previously defined a novel Golgi targeting domain (GRIP) shared by a family of coiled-coil peripheral membrane Golgi proteins implicated in membrane trafficking. We show here that the docking site for the GRIP motif of p230 is a specific domain of Golgi. membranes. By immunoelectron microscopy of HeLa cells stably expressing a green fluorescent protein (GFP)-p230(GRIP) fusion protein, we show binding specifically to a subset of membranes of the trans-Golgi network (TGN). Real-time imaging of live HeLa cells revealed that the GFP-p230(GRIP) was associated with highly dynamic tubular extensions of the TGN, which have the appearance and behaviour of transport carriers. To further define thenature of the GRIP membrane binding site, in vitro budding assays were performed using purified rat liver Golgi membranes and cytosol from GFP-p230(GRIP) transfected cells. Analysis of Golgi-derived vesicles by sucrose gradient fractionation demonstrated that GFP-p230(GRIP) binds to a specific population of vesicles distinct from those labelled for beta -COP or gamma -adaptin. The GFP-p230(GRIP) fusion protein is recruited to the same vesicle population as full-length p230, demonstrating that the GRIP domain is solely proficient as a targeting signal for membrane binding of the native molecule. Therefore, p230 GRIP is a targeting signal for recruitment to a highly selective membrane attachment site on a specific population of trans-Golgi network tubulovesicular carriers.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 08/07/20 alle ore 23:26:56