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Titolo:
Proteomic analysis of a developmentally regulated secretory vesicle
Autore:
Srinivasan, S; Traini, M; Herbert, B; Sexton, D; Harry, J; Alexander, H; Williams, KL; Alexander, S;
Indirizzi:
Univ Missouri, Div Biol Sci, Columbia, MO 65211 USA Univ Missouri Columbia MO USA 65211 Div Biol Sci, Columbia, MO 65211 USA Proteome Syst N Ryde, Sydney, NSW, Australia Proteome Syst N Ryde Sydney NSW Australia N Ryde, Sydney, NSW, Australia
Titolo Testata:
PROTEOMICS
fascicolo: 9, volume: 1, anno: 2001,
pagine: 1119 - 1127
SICI:
1615-9853(200109)1:9<1119:PAOADR>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
DICTYOSTELIUM-DISCOIDEUM CELLS; SPORE COAT PROTEINS; 2-DIMENSIONAL ELECTROPHORESIS; GLYCOPROTEIN COMPLEX; PRESPORE VESICLES; GENE; IDENTIFICATION; ORGANIZATION; AGGREGATION; ACTIVATION;
Keywords:
organelle; prespore vesicle; dictyostelium; Rab GTPase; NDP kinase; protein secretion; actin binding protein; calcium binding protein;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
48
Recensione:
Indirizzi per estratti:
Indirizzo: Alexander, S Univ Missouri, Div Biol Sci, 303 Tucker Hall, Columbia, MO 65211 USA Univ Missouri 303 Tucker Hall Columbia MO USA 65211 65211 USA
Citazione:
S. Srinivasan et al., "Proteomic analysis of a developmentally regulated secretory vesicle", PROTEOMICS, 1(9), 2001, pp. 1119-1127

Abstract

Secretion of spore coat proteins from the prespore secretory vesicles (PSVs) in Dictyostelium discoideum is a signal mediated event that underlies terminal cell differentiation, and represents an important case of developmentally regulated secretion. In order to study the biochemical mechanisms that govern the regulated fusion of the PSVs with the plasma membrane and the subsequent secretion of their cargo, we purified this organelle from prespore cells. Analysis of protein extracts of highly purified PSVs indicated that, in addition to the cargo of structural spore coat proteins, many more proteins are associated with the PSVs. Their identification is paramount to the understanding of the mechanism of regulated secretion in this system. In this study we have taken the first comprehensive proteomic approach to the analysis of an entire, previously uncharacterized, organelle, with the goal of identifying the major proteins associated with the PSVs. We show thatin addition to the structural spore coat proteins, the PSVs contain the enzymes needed for proper spore coat assembly (thioredoxin 2 and 3), regulatory proteins which we predict receive and transduce the developmental signalfor secretion (rab7 GTPase, PI-3 kinase, NDP kinase and the calcium binding proteins calfumirin-1 and calreticulin) as well as proteins that interactwith the cytoskeleton to mediate movement of the PSVs to the plasma membrane (actin binding proteins coactosin and profilin 1). In addition, the results suggest that proteins can play multiple roles in the cell, and that protein function can be dictated in part by subcellular localization. The identification of the PSV proteins is allowing us to develop testable hypotheses about the roles of these proteins within the functional context of developmentally regulated secretion.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 12/07/20 alle ore 04:10:28