Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Thrombopoietin stimulates cortactin translocation to the cytoskeleton independently of tyrosine phosphorylation
Autore:
Lopez, I; Duprez, V; Melle, J; Dreyfus, F; Levy-Toledano, S; Fontenay-Roupie, M;
Indirizzi:
Hop Cochin, Dept Hematol, AP HP, F-75679 Paris 14, France Hop Cochin Paris France 14 Dept Hematol, AP HP, F-75679 Paris 14, France Univ Paris 05, Hop Cochin, INSERM U363, ICGM, F-75014 Paris, France Univ Paris 05 Paris France F-75014 ERM U363, ICGM, F-75014 Paris, France Hop Lariboisiere, INSERM U348, Inst Federatif Rech Circulat, F-75010 Paris, France Hop Lariboisiere Paris France F-75010 ch Circulat, F-75010 Paris, France
Titolo Testata:
BIOCHEMICAL JOURNAL
, volume: 356, anno: 2001,
parte:, 3
pagine: 875 - 881
SICI:
0264-6021(20010615)356:<875:TSCTTT>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
PLATELET ACTIVATION; INTEGRIN ALPHA(IIB)BETA(3); 11Q13 AMPLIFICATION; KINASE PP72(SYK); P80/85 CORTACTIN; CONTACT SITES; SRC FAMILY; V-SRC; C-SRC; PROTEIN;
Keywords:
blood platelets; cortical actin-binding protein; tyrosine kinases;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
37
Recensione:
Indirizzi per estratti:
Indirizzo: Fontenay-Roupie, M Hop Cochin, Dept Hematol, AP HP, 27 Rue Faubourg St Jacques, F-75679 Paris14, France Hop Cochin 27 Rue Faubourg St Jacques Paris France 14
Citazione:
I. Lopez et al., "Thrombopoietin stimulates cortactin translocation to the cytoskeleton independently of tyrosine phosphorylation", BIOCHEM J, 356, 2001, pp. 875-881

Abstract

Cortactin is an F-actin-binding protein expressed in platelets. During aggregation by thrombin, cortactin associates with Src, is tyrosine phosphorylated, and then translocates to the cytoskeleton. It is also found to associate with Syk during platelet shape change. Since cortactin undergoes tyrosine phosphorylation in platelets activated by thrombopoietin (TPO) that exhibit neither shape change nor aggregation, we investigated whether it could also relocalize to the detergent-insoluble fraction. We demonstrate that cortactin was present as a tyrosine-phosphorylated protein and co-localized with Syk in the Triton X-100-insoluble fraction of TPO-activated platelets. TPO stimulated Syk activation and association with cortactin. Conversely, cortactin associated with the kinases, Syk and Src, Cortactin tyrosine phosphorylation was blocked by Syk kinase inhibitor, piceatannol or Src family kinase inhibitor, PP2, suggesting that it depends on these two kinases. However, piceatannol or PP2 did not prevent cortactin translocation to the detergent-insoluble fraction. These data suggest that tyrosine phosphorylation is not required for cortactin translocation to the detergent-insoluble compartment. Furthermore, TPO activates, through its receptor c-Mp1, a signalling pathway to the cytoskeleton.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 18/01/20 alle ore 21:34:07