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Titolo:
NuMA: A nuclear protein involved in mitotic centrosome function
Autore:
Zeng, CQ;
Indirizzi:
Baylor Coll Med, Verna & Marrs Mclean Dept Biochem, Houston, TX 77030 USA Baylor Coll Med Houston TX USA 77030 Dept Biochem, Houston, TX 77030 USA
Titolo Testata:
MICROSCOPY RESEARCH AND TECHNIQUE
fascicolo: 5, volume: 49, anno: 2000,
pagine: 467 - 477
SICI:
1059-910X(20000601)49:5<467:NANPII>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
MICROTUBULE-ASSOCIATED PROTEIN; KINESIN-RELATED PROTEIN; ACUTE PROMYELOCYTIC LEUKEMIA; BIPOLAR SPINDLE FORMATION; HEAT-INDUCED APOPTOSIS; XENOPUS EGG EXTRACTS; APPARATUS PROTEIN; CYTOPLASMIC DYNEIN; MAMMALIAN-CELLS; COILED-COIL;
Keywords:
spindle poles; PCM; microtubules; cytoplasmic dynein; MTOCs; MT motors;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
112
Recensione:
Indirizzi per estratti:
Indirizzo: Zeng, CQ Baylor Coll Med, Verna & Marrs Mclean Dept Biochem, 1 Baylor Plaza, Houston, TX 77030 USA Baylor Coll Med 1 Baylor Plaza Houston TX USA 77030 TX 77030 USA
Citazione:
C.Q. Zeng, "NuMA: A nuclear protein involved in mitotic centrosome function", MICROSC RES, 49(5), 2000, pp. 467-477

Abstract

Nuclear mitotic apparatus protein, NuMA, is an abundant 240 kDa protein with microtubule (MT) binding capacity via its carboxyl terminal region. Structurally, it has been shown to be a double-strand coiled-coil that has a high potential to form filamentous polymers. During interphase, NuMA locates within the nucleus but rapidly redistributes to the separating centrosomes during early mitosis. Xenopus NuMA associates with MT minus end-directed motor cytoplasmic dynein and its motility-activating complex dynactin at mitotic centrosomal regions. This NuMA-motor complex binds the free ends of MTs, converging and tethering spindle MT ends to the poles. A similar scenarioappears to be true in higher vertebrates as well. As a mitotic centrosomalcomponent, NuMA is essential for the organization and stabilization of spindle poles from early mitosis until at least the onset of anaphase. The cell cycle-dependent distribution and function of NuMA is regulated by phosphorylation and dephosphorylation, and p34/CDC2 activity is important to the mitotic role of NuMA. This review summarizes data about the structural features and mitotic function of NuMA with particular emphasis on the newly discovered NuMA-motor complex in spindle organization. Furthermore, NuMA may represent a large group of proteins whose mitotic function is sequestered in the nucleus during interphase. (C) 2000 Wiley-Liss.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/11/20 alle ore 11:06:45