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Titolo:
THE RELATIVE ROLES OF SPECIFIC N-TERMINAL AND C-TERMINAL PHOSPHORYLATION SITES IN THE DISASSEMBLY OF INTERMEDIATE FILAMENT IN MITOTIC BHK-21-CELLS
Autore:
CHOU YH; OPAL P; QUINLAN RA; GOLDMAN RD;
Indirizzi:
NORTHWESTERN UNIV,SCH MED,DEPT CELL & MOLEC BIOL CHICAGO IL 60611 NORTHWESTERN UNIV,SCH MED,DEPT CELL & MOLEC BIOL CHICAGO IL 60611 UNIV DUNDEE,DEPT BIOCHEM DUNDEE DD1 4HN SCOTLAND
Titolo Testata:
Journal of Cell Science
, volume: 109, anno: 1996,
parte:, 4
pagine: 817 - 826
SICI:
0021-9533(1996)109:<817:TRROSN>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
HAMSTER-KIDNEY CELLS; PROTEIN-KINASE; VIMENTIN FILAMENTS; ASSEMBLY PROPERTIES; NUCLEAR LAMINA; GROWTH-FACTOR; TAIL DOMAIN; HEAD DOMAIN; CDC2 KINASE; MITOSIS;
Keywords:
VIMENTIN; MITOSIS; PROTEIN PHOSPHORYLATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
67
Recensione:
Indirizzi per estratti:
Citazione:
Y.H. Chou et al., "THE RELATIVE ROLES OF SPECIFIC N-TERMINAL AND C-TERMINAL PHOSPHORYLATION SITES IN THE DISASSEMBLY OF INTERMEDIATE FILAMENT IN MITOTIC BHK-21-CELLS", Journal of Cell Science, 109, 1996, pp. 817-826

Abstract

Previously we identified p34(cdc2) as one of two protein kinases mediating the hyperphosphorylation and disassembly of vimentin in mitotic BHK-21 cells. In this paper, we identify the second kinase as a 37 kDaprotein. This p37 protein kinase phosphorylates vimentin on two adjacent residues (thr-457 and ser-458) which are located in the C-terminalnon-alpha-helical domain. Contrary to the p34(cdc2) mediated N-terminal phosphorylation (at ser-55) which can disassemble vimentin intermediate filaments (IF) in vitro, p37 protein kinase phosphorylates vimentin-IF without obviously affecting its structure in vitro. We have further examined the in vivo role(s) of vimentin phosphorylation in the disassembly of the IF network in mitotic BHK cells by transient transfection assays. In untransfected BHK cells, the interphase vimentin IF networks are disassembled into non-filamentous aggregates when cells enter mitosis. Transfection of cells with vimentin cDNA lacking the p34(cdc2) phosphorylation site (ser55:ala) effectively prevents mitotic cells from disassembling their IF. In contrast, apparently normal disassembly takes place in cells transfected with cDNA containing mutated p37kinase phosphorylation sites (thr457:ala/ser458:ala). Transfection ofcells with vimentin cDNAs lacking both the N- and C-terminal phosphorylation sites yields a phenotype indistinguishable from that obtained with the single N-terminal mutant. Taken together, our results demonstrate that the site-specific phosphorylation of the N-terminal domain, but not the C-terminal domain of vimentin plays an important role in determining the state of IF polymerization and supramolecular organization in mitotic cells.

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Documento generato il 22/01/20 alle ore 12:47:23