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Titolo:
The yeast kinesin-related protein Smy1p exerts its effects on the class V myosin Myo2p via a physical interaction
Autore:
Beningo, KA; Lillie, SH; Brown, SS;
Indirizzi:
Univ Michigan, Sch Med, Dept Anat & Cell Biol, Ann Arbor, MI 48109 USA Univ Michigan Ann Arbor MI USA 48109 & Cell Biol, Ann Arbor, MI 48109 USA
Titolo Testata:
MOLECULAR BIOLOGY OF THE CELL
fascicolo: 2, volume: 11, anno: 2000,
pagine: 691 - 702
SICI:
1059-1524(200002)11:2<691:TYKPSE>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
SACCHAROMYCES-CEREVISIAE; UNCONVENTIONAL MYOSIN; VESICULAR TRANSPORT; POLARIZED GROWTH; ACTIN; GENE; MOVEMENT; SITES; MOTOR;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
30
Recensione:
Indirizzi per estratti:
Indirizzo: Beningo, KA Univ Massachusetts, Sch Med, Dept Physiol, 377 Plantat St,Room327, Worcester, MA 01605 USA Univ Massachusetts 377 Plantat St,Room 327 Worcester MA USA 01605
Citazione:
K.A. Beningo et al., "The yeast kinesin-related protein Smy1p exerts its effects on the class V myosin Myo2p via a physical interaction", MOL BIOL CE, 11(2), 2000, pp. 691-702

Abstract

We have discovered evidence for a physical interaction between a class V myosin, Myo2p, and a kinesin-related protein, Smy1p, in budding yeast. Theseproteins had previously been linked by genetic and colocalization studies,but we had been unable to determine the nature of their association. We now show by two-hybrid analysis that a 69-amino acid region of the Smy1p tailinteracts with the globular portion of the Myo2p tail. Deletion of this myosin-binding region of Smy1p eliminates its ability to colocalize with Myo2p and to overcome the myo2-66 mutant defects, suggesting that the interaction is necessary for these functions. Further insights about the Smy1p-Myo2pinteraction have come from studies of a new mutant allele, myo2-2, which causes a loss of Myo2p localization. We report that Smy1p localization is also lost in the myo2-2 mutant, demonstrating that Smy1p localization is dependent on Myo2p. We also found that overexpression of Smy1p partially restores myo2-2p localization in a myosin-binding region-dependent manner. Thus, overexpression of Smy1p can overcome defects in both the head and tail domains of Myo2p (caused by the myo2-66 and myo2-2 alleles, respectively). We propose that Smy1p enhances some aspect of Myo2p function, perhaps delivery or docking of vesicles at the bud tip.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 23/01/21 alle ore 08:55:11