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Titolo:
Store-operated Ca2+ entry: Evidence for a secretion-like coupling model
Autore:
Patterson, RL; van Rossum, DB; Gill, DL;
Indirizzi:
Univ Maryland, Sch Med, Dept Biochem & Mol Biol, Baltimore, MD 21201 USA Univ Maryland Baltimore MD USA 21201 & Mol Biol, Baltimore, MD 21201 USA
Titolo Testata:
CELL
fascicolo: 4, volume: 98, anno: 1999,
pagine: 487 - 499
SICI:
0092-8674(19990820)98:4<487:SCEEFA>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
CAPACITATIVE CALCIUM-ENTRY; OKADAIC ACID; CALYCULIN-A; PROTEIN PHOSPHATASE-1; ENDOTHELIAL-CELLS; ERM PROTEINS; F-ACTIN; RELEASE; POOLS; INHIBITION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
52
Recensione:
Indirizzi per estratti:
Indirizzo: Gill, DL Univ Maryland, Sch Med, Dept Biochem & Mol Biol, Baltimore, MD 21201 USA Univ Maryland Baltimore MD USA 21201 ol, Baltimore, MD 21201 USA
Citazione:
R.L. Patterson et al., "Store-operated Ca2+ entry: Evidence for a secretion-like coupling model", CELL, 98(4), 1999, pp. 487-499

Abstract

elusive coupling between endoplasmic reticulum (ER) Ca2+ stores and plasmamembrane (PM) "store-operated" Ca2+ entry channels was probed through a novel combination of cytoskeletal modifications. Whereas coupling was unaffected by disassembly of the actin cytoskeleton, in situ redistribution of F-actin into a tight cortical layer subjacent to the PM displaced cortical ER and prevented coupling between ER and PM Ca2+ entry channels, while not affecting inositol 1,4,5-trisphosphate-mediated store release, Importantly, disassembly of the induced cortical actin layer allowed ER to regain access to the PM and reestablish coupling of Ca2+ entry channels to Ca2+ store depletion. Coupling is concluded to be mediated by a physical "secretion-like" mechanism involving close but reversible interactions between the ER and the PM.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 08/04/20 alle ore 12:14:15