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Titolo:
The Golgi-associated COPI-coated buds and vesicles contain beta/gamma-actin
Autore:
Valderrama, F; Luna, A; Babia, I; Martinez-Menaruguez, JA; Ballesta, J; Barth, H; Chaponnier, C; Renau-Piqueras, J; Egea, G;
Indirizzi:
Univ Barcelona, IDIBAPS, Fac Med, Dept Cellular Biol, E-08036 Barcelona, Spain Univ Barcelona Barcelona Spain E-08036 ar Biol, E-08036 Barcelona, Spain Univ Murcia, Fac Med, Dept Biol Celular, E-30071 Murcia, Spain Univ Murcia Murcia Spain E-30071 ept Biol Celular, E-30071 Murcia, Spain Univ Freiburg, Inst Pharmakol & Toxikol, D-79104 Freiburg, Germany Univ Freiburg Freiburg Germany D-79104 oxikol, D-79104 Freiburg, Germany Univ Geneva, Dept Pathol, CH-1211 Geneva 4, Switzerland Univ Geneva Geneva Switzerland 4 t Pathol, CH-1211 Geneva 4, Switzerland Hosp La Fe, Ctr Invest, E-46009 Valencia, Spain Hosp La Fe Valencia Spain E-46009 e, Ctr Invest, E-46009 Valencia, Spain
Titolo Testata:
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
fascicolo: 4, volume: 97, anno: 2000,
pagine: 1560 - 1565
SICI:
0027-8424(20000215)97:4<1560:TGCBAV>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
GTP-BINDING-PROTEIN; ADP-RIBOSYLATION; BETA-COP; TRANSPORT VESICLES; GENE-PRODUCT; MYOSIN-II; CELLS; SPECTRIN; IDENTIFICATION; COMPLEX;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
39
Recensione:
Indirizzi per estratti:
Indirizzo: Egea, G Univ Barcelona, Fac Med, Dept Biol Cellular & Anat Patol, C Casanova 143, Barcelona 08036, Spain Univ Barcelona C Casanova 143 Barcelona Spain 08036 08036, Spain
Citazione:
F. Valderrama et al., "The Golgi-associated COPI-coated buds and vesicles contain beta/gamma-actin", P NAS US, 97(4), 2000, pp. 1560-1565

Abstract

It has been shown previously that the morphology and subcellular positioning of the Golgi complex is controlled by actin microfilaments. To further characterize the association between actin microfilaments and the Golgi complex, we have used the Clostridium botolinum toxins C2 and C3, which specifically inhibit actin polymerization and cause depolymerization of F-actin inintact cells by the ADP ribosylation of G-actin monomers and the Rho smallCTP-binding protein, respectively. Normal rat kidney cells treated with C2showed that disruption of the actin and the collapse of the Golgi complex occurred concomitantly, However, when cells were treated with C3, the actindisassembly was observed without any change in the organization of the Golgi complex. The absence of the involvement of Rho was further confirmed by the treatment with lysophosphatidic acid or microinjection with the constitutively activated form of RhoA, both of which induced the stress fiber formation without affecting the Golgi complex. Immunogold electron microscopy in normal rat kidney cells revealed that beta- and gamma-actin isoforms werefound in Golgi-associated COPI-coated buds and vesicles. Taken together, the results suggest that the Rho signaling pathway does not directly regulate Golgi-associated actin microfilaments, and that beta- and gamma-actins might be involved in the formation and/or transport of Golgi-derived vesicular or tubular intermediates.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/07/20 alle ore 09:39:45