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Titolo:
Phosphorylation of a conserved integrin alpha 3 QPSXXE motif regulates signaling, motility, and cytoskeletal engagement
Autore:
Zhang, XA; Bontrager, AL; Stipp, CS; Kraeft, SK; Bazzoni, G; Chen, LB; Hemler, ME;
Indirizzi:
Harvard Univ, Sch Med, Dana Farber Canc Inst, Boston, MA 02115 USA HarvardUniv Boston MA USA 02115 a Farber Canc Inst, Boston, MA 02115 USA Harvard Univ, Sch Med, Dept Pathol, Boston, MA 02115 USA Harvard Univ Boston MA USA 02115 h Med, Dept Pathol, Boston, MA 02115 USA
Titolo Testata:
MOLECULAR BIOLOGY OF THE CELL
fascicolo: 2, volume: 12, anno: 2001,
pagine: 351 - 365
SICI:
1059-1524(200102)12:2<351:POACIA>2.0.ZU;2-8
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN-KINASE-C; ACTIVATION-DEPENDENT ADHESION; CYTOPLASMIC DOMAIN; CELL-MIGRATION; EXTRACELLULAR-MATRIX; TYROSINE PHOSPHORYLATION; LAMININ RECEPTOR; FIBRONECTIN RECEPTOR; TISSUE DISTRIBUTION; LEUKOCYTE ADHESION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
81
Recensione:
Indirizzi per estratti:
Indirizzo: Hemler, ME Harvard Univ, Sch Med, Dana Farber Canc Inst, Boston, MA 02115 USA Harvard Univ Boston MA USA 02115 nc Inst, Boston, MA 02115 USA
Citazione:
X.A. Zhang et al., "Phosphorylation of a conserved integrin alpha 3 QPSXXE motif regulates signaling, motility, and cytoskeletal engagement", MOL BIOL CE, 12(2), 2001, pp. 351-365

Abstract

Integrin alpha 3A cytoplasmic tail phosphorylation was mapped to amino acid S1042, as determined by mass spectrometry, and confirmed by mutagenesis. This residue occurs within a "QPSXXE" motif conserved in multiple alpha chains (alpha 3A, alpha 6A, alpha 7A), from multiple species. Phosphorylation of a3A and a6A did not appear to be directly mediated by protein kinase C (PKC) alpha, beta, gamma, delta, epsilon, zeta or mu, or by any of several other known serine kinases, although PKC has an indirect role in promoting phosphorylation. A S1042A mutation did not affect alpha3-Chinese hamster ovary (CHO) cell adhesion to laminin-5, but did alter 1) alpha3-dependent tyrosine phosphorylation of focal adhesion kinase and paxillin (in the presenceor absence of phorbol 12-myristate 13 acetate stimulation), and p130(CAS) (in the absence of phorbol 12-myristate 13 acetate stimulation), 2) the shape of cells spread on laminin-5, and 3) alpha3-dependent random CHO cell migration on laminin-5. In addition, S1042A mutation altered the PKC-dependent, ligand-dependent subcellular distribution of alpha3 and F-actin in CHO cells. Together, the results demonstrate clearly that alpha 3A phosphorylation is functionally relevant. In addition, the results strongly suggest thatalpha3 phosphorylation may regulate alpha3 integrin interaction with the cytoskeleton.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/04/20 alle ore 08:46:34