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Titolo:
INHIBITORS OF ACTIN POLYMERIZATION AND CALMODULIN-BINDING ENHANCE PROTEIN-KINASE C-INDUCED TRANSLOCATION OF MARCKS IN C6 GLIOMA-CELLS
Autore:
DOUGLAS DN; FINK HS; ROSE SD; RIDGWAY ND; COOK HW; BYERS DM;
Indirizzi:
DALHOUSIE UNIV,DEPT PEDIAT,ATLANTIC RES CTR,CLIN RES CTR,ROOM C-205,5849 UNIV AVE HALIFAX NS CANADA DALHOUSIE UNIV,DEPT PEDIAT,ATLANTIC RES CTR,CLIN RES CTR HALIFAX NS CANADA DALHOUSIE UNIV,DEPT BIOCHEM,ATLANTIC RES CTR,CLIN RES CTR HALIFAX NS CANADA
Titolo Testata:
Biochimica et biophysica acta. Molecular cell research
fascicolo: 2, volume: 1356, anno: 1997,
pagine: 121 - 130
SICI:
0167-4889(1997)1356:2<121:IOAPAC>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
SUBSTRATE MARCKS; MEMBRANE ASSOCIATION; DIFFERENTIAL EXPRESSION; PLASMA-MEMBRANE; PKC ISOFORMS; PHOSPHORYLATION; STAUROSPORINE; BRAIN; NEUROBLASTOMA; CYTOSKELETON;
Keywords:
MYRISTOYLATED ALANINE-RICH C KINASE SUBSTRATE; PROTEIN KINASE C; CALMODULIN; ACTIN; CYTOCHALASIN; TRANSLOCATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
44
Recensione:
Indirizzi per estratti:
Citazione:
D.N. Douglas et al., "INHIBITORS OF ACTIN POLYMERIZATION AND CALMODULIN-BINDING ENHANCE PROTEIN-KINASE C-INDUCED TRANSLOCATION OF MARCKS IN C6 GLIOMA-CELLS", Biochimica et biophysica acta. Molecular cell research, 1356(2), 1997, pp. 121-130

Abstract

MARCKS (myristoylated alanine-rich C-kinase substrate) is known to interact with calmodulin, actin filaments, and anionic phospholipids at a central basic domain which is also the site of phosphorylation by protein kinase C (PKC). In the present study, cytochalasin D (CD) and calmodulin antagonists were used to examine the influence of F-actin andcalmodulin on membrane interaction of MARCKS in C6 glioma cells. CD treatment for 1 h disrupted F-actin filaments, increased membrane boundimmunoreactive MARCKS (from 51% to 62% of total), yet markedly enhanced the amount of MARCKS translocated to the cytosolic fraction in response to the phorbol ester 4 beta-12-O-tetradecanoylphorbol 13-acetate. In contrast, CD treatment had no effect on phorbol ester-stimulated phosphorylation of MARCKS or on translocation of PKC ct to the membranefraction. Staurosporine also increased membrane association of MARCKSin a PKC-independent manner, as no change in MARCKS phosphorylation was noted and bis-indolylmaleimide (a more specific PKC inhibitor) did not alter MARCKS distribution. Staurosporine inhibited the phorbol ester-induced translocation of MARCKS but not of PKC alpha in both CD pretreated and untreated cells. Calmodulin antagonists (trifluoperazine, calmidazolium) had little effect on the cellular distribution or phosphorylation of MARCKS, but were synergistic with phorbol ester in translocating MARCKS from the membrane without a further increase in its phosphorylation. We conclude that cytoskeletal integrity is not requiredfor phosphorylation and translocation of MARCKS in response to activated PKC, but that interaction with both F-actin and calmodulin might serve to independently modulate PKC-regulated localization and functionof MARCKS at cellular membranes.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/04/20 alle ore 19:23:31