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Titolo:
Vrp1p functions in both actomyosin ring-dependent and Hof1p-dependent pathways of cytokinesis
Autore:
Naqvi, SN; Feng, G; Boulton, VJ; Zahn, R; Munn, AL;
Indirizzi:
Natl Univ Singapore, Inst Mol Agrobiol, Lab Yeast Cell Biol, Singapore 117604, Singapore Natl Univ Singapore Singapore Singapore 117604 ngapore 117604, Singapore
Titolo Testata:
TRAFFIC
fascicolo: 3, volume: 2, anno: 2001,
pagine: 189 - 201
SICI:
1398-9219(200103)2:3<189:VFIBAR>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
ALDRICH-SYNDROME PROTEIN; SACCHAROMYCES-CEREVISIAE; BUDDING YEAST; TYROSINE PHOSPHATASE; ACTIN CYTOSKELETON; ESCHERICHIA-COLI; ARP2/3 COMPLEX; CELL-CYCLE; MORPHOGENESIS; VERPROLIN;
Keywords:
Bee1p; budding; cell cycle; cell division; cell polarity; cell wall; cleavage furrow; cytoskeleton; Las17p; mitosis; WASP; WIP; PSTPIP;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
40
Recensione:
Indirizzi per estratti:
Indirizzo: Munn, AL Natl Univ Singapore, Inst Mol Agrobiol, Lab Yeast Cell Biol, 1 Res Link, Singapore 117604, Singapore Natl Univ Singapore 1 Res Link Singapore Singapore 117604 gapore
Citazione:
S.N. Naqvi et al., "Vrp1p functions in both actomyosin ring-dependent and Hof1p-dependent pathways of cytokinesis", TRAFFIC, 2(3), 2001, pp. 189-201

Abstract

Vrp1p/verprolin/End5p is a Saccharomyces cerevisiae proline-rich protein, structurally and functionally related to human Wiskott-Aldrich syndrome protein-interacting protein. Vrp1p is required for viability at 37 degreesC, but not 24 degreesC. Here, we show that loss of Vrp1p (vrp1 Delta) leads to a 3-4-fold delay in cytokinesis, wide bud necks, abnormal actomyosin rings,and aberrant septa even at 24 degreesC. Like other mutations affecting theactomyosin ring, vrp1 Delta is synthetic lethal with deletion of HOF1 (or CYK2), which encodes a protein related to mammalian proline serine threonine phosphatase-interacting protein and Schizosaccharomyces pombe Cdc15p required for an actomyosin ring-independent pathway of cytokinesis in S. cerevisiae. At 37 degreesC, vrp1 Delta cells rapidly cease dividing and exhibit anovel terminal phenotype: a single large bud, two well-separated nuclei, and an interphase microtubule array. The arrested cells have a persistent ring containing both actin and myosin at the bud neck. Many also exhibit somepolarisation of cortical actin patches to the bud neck. Vrp1p binds an SH3-domain-containing fragment of Hof1p in vitro. Vrp1p is required in vivo for Hof1p relocalisation to a single ring at the bud neck prior to cytokinesis at 37 degreesC, but not at 24 degreesC. Vrp1p thus acts in both actomyosin ring formation and function, as well as in Hof1p localisation during cytokinesis.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/05/20 alle ore 23:31:24