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Titolo:
Vam3p structure reveals conserved and divergent properties of syntaxins
Autore:
Dulubova, I; Yamaguchi, T; Wang, Y; Sudhof, TC; Rizo, J;
Indirizzi:
Univ Texas, SW Med Ctr, Dept Biochem, Dallas, TX 75390 USA Univ Texas Dallas TX USA 75390 ed Ctr, Dept Biochem, Dallas, TX 75390 USA Univ Texas, SW Med Ctr, Dept Pharmacol, Dallas, TX 75390 USA Univ Texas Dallas TX USA 75390 Ctr, Dept Pharmacol, Dallas, TX 75390 USA Univ Texas, SW Med Ctr, Ctr Basic Neurosci, Dept Mol Genet, Dallas, TX 75390 USA Univ Texas Dallas TX USA 75390 osci, Dept Mol Genet, Dallas, TX 75390 USA Univ Texas, SW Med Ctr, Howard Hughes Med Inst, Dallas, TX 75390 USA Univ Texas Dallas TX USA 75390 ward Hughes Med Inst, Dallas, TX 75390 USA
Titolo Testata:
NATURE STRUCTURAL BIOLOGY
fascicolo: 3, volume: 8, anno: 2001,
pagine: 258 - 264
SICI:
1072-8368(200103)8:3<258:VSRCAD>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN-PROTEIN INTERACTIONS; SNARE COMPLEX; MEMBRANE-FUSION; VESICLE FUSION; SYNAPTIC EXOCYTOSIS; VACUOLE FUSION; T-SNARE; YEAST; TRAFFICKING; SENSITIVITY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
50
Recensione:
Indirizzi per estratti:
Indirizzo: Rizo, J Univ Texas, SW Med Ctr, Dept Biochem, Dallas, TX 75390 USA Univ Texas Dallas TX USA 75390 Dept Biochem, Dallas, TX 75390 USA
Citazione:
I. Dulubova et al., "Vam3p structure reveals conserved and divergent properties of syntaxins", NAT ST BIOL, 8(3), 2001, pp. 258-264

Abstract

Syntaxins and Sec1/munc18 proteins are central to intracellular membrane fusion. All syntaxins comprise a variable N-terminal region, a conserved SNARE motif that is critical for SNARE complex formation, and a transmembrane region. The N-terminal region of neuronal syntaxin 1A contains a three-helix domain that folds back onto the SNARE motif forming a 'closed' conformation; this conformation is required for munc18-1 binding. We have examined the generality of the structural properties of syntaxins by NMR analysis of Vam3p, a yeast syntaxin essential for vacuolar fusion, Surprisingly, Vam3p also has an N-terminal three-helical domain despite lacking apparent sequence homology with syntaxin 1A in this region. However, Vam3p does not form a closed conformation and its N-terminal domain is not required for binding to the Sec1/munc18 protein Vps33p, suggesting that critical distinctions exist in the mechanisms used by syntaxins to govern different types of membrane fusion.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 08/07/20 alle ore 08:04:15