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Titolo:
The Golgi-associated Hook3 protein is a member of a novel family of microtubule-binding proteins
Autore:
Walenta, JH; Didier, AJ; Liu, XR; Kramer, H;
Indirizzi:
Univ Texas, SW Med Ctr, Ctr Basic Neurosci, Dallas, TX 75390 USA Univ Texas Dallas TX USA 75390 , Ctr Basic Neurosci, Dallas, TX 75390 USA Univ Texas, SW Med Ctr, Dept Cell Biol, Dallas, TX 75390 USA Univ Texas Dallas TX USA 75390 Ctr, Dept Cell Biol, Dallas, TX 75390 USA
Titolo Testata:
JOURNAL OF CELL BIOLOGY
fascicolo: 5, volume: 152, anno: 2001,
pagine: 923 - 934
SICI:
0021-9525(20010305)152:5<923:TGHPIA>2.0.ZU;2-5
Fonte:
ISI
Lingua:
ENG
Soggetto:
MANNOSE 6-PHOSPHATE RECEPTORS; ADP-RIBOSYLATION FACTOR; MULTIVESICULAR ENDOSOMES; ENDOPLASMIC-RETICULUM; CYTOPLASMIC DYNEIN; BREFELDIN-A; FORMIMINOTRANSFERASE CYCLODEAMINASE; INTERMEDIATE COMPARTMENT; ENDOCYTIC TRAFFICKING; MEMBRANE-TRANSPORT;
Keywords:
membrane trafficking; Hook protein; endosomes; brefeldin A; Golgi complex;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
63
Recensione:
Indirizzi per estratti:
Indirizzo: Kramer, H Univ Texas, SW Med Ctr, Ctr Basic Neurosci, 5323 Harry Hines Blvd, Dallas,TX 75235 USA Univ Texas 5323 Harry Hines Blvd Dallas TX USA 75235X 75235 USA
Citazione:
J.H. Walenta et al., "The Golgi-associated Hook3 protein is a member of a novel family of microtubule-binding proteins", J CELL BIOL, 152(5), 2001, pp. 923-934

Abstract

Microtubules are central to the spatial organization of diverse membrane-trafficking systems. Here, we report that Hook proteins constitute a novel family of cytosolic coiled coil proteins that bind to organelles and to microtubules. The conserved NH2-terminal domains of Hook proteins mediate attachment to microtubules, whereas the more divergent COOH-terminal domains mediate the binding to organelles. Human Hook3 bound to Golgi membranes in vitro and was enriched in the cis-Golgi in vivo. Unlike other cis-Golgi-associated proteins, however. a large fraction of Hook3 maintained its juxtanuclear localization after Brefeldin A treatment, indicating a Golgi-independentmechanism for Hook3 localization. Because overexpression of Hook3 caused fragmentation of the Golgi complex, we propose that Hook3 participates in defining the architecture and localization of the mammalian Golgi complex.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 14/07/20 alle ore 10:06:18