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Titolo:
Roles of the cytoplasmic and transmembrane domains of syntaxins in intracellular localization and trafficking
Autore:
Kasai, K; Akagawa, K;
Indirizzi:
Kyorin Univ, Dept Physiol, Tokyo 1818611, Japan Kyorin Univ Tokyo Japan 1818611 Univ, Dept Physiol, Tokyo 1818611, Japan Toyama Chem Co Ltd, Sinju Ku, Tokyo 1600023, Japan Toyama Chem Co Ltd Tokyo Japan 1600023 d, Sinju Ku, Tokyo 1600023, Japan
Titolo Testata:
JOURNAL OF CELL SCIENCE
fascicolo: 17, volume: 114, anno: 2001,
pagine: 3115 - 3124
SICI:
0021-9533(200109)114:17<3115:ROTCAT>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
TRANS-GOLGI NETWORK; DI-LEUCINE MOTIF; INTEGRAL MEMBRANE-PROTEIN; ENDOPLASMIC-RETICULUM; BREFELDIN-A; T-SNARE; VESICULAR TRANSPORT; SORTING SIGNALS; PLASMA-MEMBRANE; LATE ENDOSOMES;
Keywords:
syntaxin; cytoplasmic domain; transmembrane domain; di-leucine-based motif; intracellular localization; antibody uptake experiment;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
57
Recensione:
Indirizzi per estratti:
Indirizzo: Akagawa, K Kyorin Univ, Dept Physiol, Tokyo 1818611, Japan Kyorin Univ Tokyo Japan 1818611 Physiol, Tokyo 1818611, Japan
Citazione:
K. Kasai e K. Akagawa, "Roles of the cytoplasmic and transmembrane domains of syntaxins in intracellular localization and trafficking", J CELL SCI, 114(17), 2001, pp. 3115-3124

Abstract

Syntaxins are target-soluble N-ethylmaleimide-sensitive factor-attachment protein receptors (t-SNAR]Es) involved in docking and fusion of vesicles inexocytosis and endocytosis. Many syntaxin isoforms, have been isolated, and each one displays a distinct intracellular localization pattern. However,the signals that drive the specific intracellular localization of syntaxins are poorly understood. In this study, we used indirect immunofluorescenceanalysis to examine the localization of syntaxin chimeras, each containinga syntaxin transmembrane domain fused to a cytoplasmic domain derived froma different syntaxin. We show that the cytoplasmic domains of syntaxins 5,6, 7 and 8 have important effects on intracellular localization. We also demonstrate that the transmembrane domain of syntaxin 5 is sufficient to localize the chimera to the compartment expected for wild-type syntaxin 5. Additionally, we find that syntaxins 6, 7 and 8, but not syntaxin 5, are present at the plasma membrane, and that these syntaxins cycle through the plasma membrane by virtue of their cytoplasmic domains. Finally, we find that dileucine-based motifs in the cytoplasmic domains of syntaxins 7 and 8 are necessary for their intracellular localization and trafficking via distinct transport pathways. Combined, these results suggest that both the cytoplasmic and the transmembrane domains play important roles in intracellular localization and trafficking of syntaxins.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 15/01/21 alle ore 22:59:10