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Titolo:
MECHANICS OF MOTILITY - DISTINCT DYNEIN BINDING DOMAINS ON ALPHA-TUBULIN AND BETA-TUBULIN
Autore:
GOLDSMITH M; YARBROUGH L; VANDERKOOY D;
Indirizzi:
UNIV TORONTO,DEPT ANAT & CELL BIOL TORONTO ON M5S 1A8 CANADA UNIV TORONTO,DEPT ANAT & CELL BIOL TORONTO ON M5S 1A8 CANADA UNIV KANSAS,MED CTR,SCH MED,DEPT BIOCHEM KANSAS CITY KS 66103
Titolo Testata:
Biochemistry and cell biology
fascicolo: 9-10, volume: 73, anno: 1995,
pagine: 665 - 671
SICI:
0829-8211(1995)73:9-10<665:MOM-DD>2.0.ZU;2-0
Fonte:
ISI
Lingua:
ENG
Soggetto:
MICROTUBULES INVITRO; CYTOPLASMIC DYNEIN; AXONAL-TRANSPORT; MITOTIC SPINDLES; MOTORS; KINETOCHORES; MOVEMENT; ANTIBODY; SURFACE;
Keywords:
MICROTUBULE; MICROTUBULE-BASED MOTILITY; DYNEIN; SPERM MOTILITY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
25
Recensione:
Indirizzi per estratti:
Citazione:
M. Goldsmith et al., "MECHANICS OF MOTILITY - DISTINCT DYNEIN BINDING DOMAINS ON ALPHA-TUBULIN AND BETA-TUBULIN", Biochemistry and cell biology, 73(9-10), 1995, pp. 665-671

Abstract

Microtubules (MTs) interact with force-generating proteins to generate a variety of intracellular movements, including intracellular particle transport, ciliary-flagellar beating, and chromosome-spindle movements during mitosis-meiosis. Relatively little is known about the mechanics of these motor-MT interactions, in part because the motor bindingdomains of the MT and the corresponding MT binding domains of the motor have not been well characterized. Using a flagellar motility assay,we report that the MT subunits, alpha- and beta-tubulin, each containa dynein binding domain located near the C-termini of their respective tubulin subunits. Blocking either alpha- or beta-tubulin binding domains of dynein attenuates motility in demembranated sea urchin sperm up to 50%. Interestingly, blocking both alpha- and beta-tubulin bindingdomains on dynein produces much greater decreases in motility. These data suggest that flagellar dynein binds to both subunits of the MT polymer, alpha- and beta-tubulin. In addition, the two subunits appear to contribute equivalent, but functionally separate, roles to flagellarmotility.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/09/20 alle ore 22:39:25