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Titolo:
The secretory pathway mediates localization of the cell polarity regulatorAip3p/Bud6p
Autore:
Jin, H; Amberg, DC;
Indirizzi:
SUNY Upstate Med Univ, Dept Biochem & Mol Biol, Syracuse, NY 13210 USA SUNY Upstate Med Univ Syracuse NY USA 13210 Biol, Syracuse, NY 13210 USA
Titolo Testata:
MOLECULAR BIOLOGY OF THE CELL
fascicolo: 2, volume: 11, anno: 2000,
pagine: 647 - 661
SICI:
1059-1524(200002)11:2<647:TSPMLO>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
YEAST ACTIN CYTOSKELETON; BUD-SITE SELECTION; SACCHAROMYCES-CEREVISIAE; PLASMA-MEMBRANE; UNCONVENTIONAL MYOSIN; VESICULAR TRANSPORT; BUDDING YEAST; SEC4 FUNCTION; GENE ENCODES; PEP4 GENE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
42
Recensione:
Indirizzi per estratti:
Indirizzo: Amberg, DC SUNY Upstate Med Univ, Dept Biochem & Mol Biol, Syracuse, NY 13210 USA SUNY Upstate Med Univ Syracuse NY USA 13210 cuse, NY 13210 USA
Citazione:
H. Jin e D.C. Amberg, "The secretory pathway mediates localization of the cell polarity regulatorAip3p/Bud6p", MOL BIOL CE, 11(2), 2000, pp. 647-661

Abstract

Ai3p/Bud6p is a regulator of cell and cytoskeletal polarity in Saccharomyces cerevisiae that was previously identified as an actin-interacting protein. Actin-interacting protein 3 (Aip3p) localizes at the cell cortex where cytoskeleton assembly must be achieved to execute polarized cell growth, anddeletion of AIP3 causes gross defects in cell and cytoskeletal polarity. We have discovered that Aip3p localization is mediated by the secretory pathway. Mutations in early- or late-acting components of the secretory apparatus lead to Aip3p mislocalization. Biochemical data show that a pool of Aip3p is associated with post-Golgi secretory vesicles. An investigation of thesequences within Aip3p necessary for Aip3p localization has identified a sequence within the N terminus of Aip3p that is sufficient for directing Aip3p localization. Replacement of the N terminus of Aip3p with a homologous region from a Schizosaccharomyces pombe protein allows for normal Aip3p localization, indicating that the secretory pathway-mediated Aip3p localizationpathway is conserved. Delivery of Aip3p also requires the type V myosin motor Myo2p and its regulatory light-chain calmodulin. These data suggest that one function of calmodulin is to activate Myo2p's activity in the secretory pathway; this function is likely the polarized movement of late secretory vesicles and associated Aip3p on actin cables.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 23/01/21 alle ore 09:43:17