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Titolo:
BINDING OF E-MAP-115 TO MICROTUBULES IS REGULATED BY CELL CYCLE-DEPENDENT PHOSPHORYLATION
Autore:
MASSON D; KREIS TE;
Indirizzi:
UNIV GENEVA,MED CTR,1 RUE MICHEL SERVET CH-1211 GENEVA SWITZERLAND UNIV GENEVA,DEPT BIOL CELLULAIRE CH-1211 GENEVA SWITZERLAND
Titolo Testata:
The Journal of cell biology
fascicolo: 4, volume: 131, anno: 1995,
pagine: 1015 - 1024
SICI:
0021-9525(1995)131:4<1015:BOETMI>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
MITOTIC SPINDLES; MAP KINASE; STABLE MICROTUBULES; MAMMALIAN-CELLS; CULTURED-CELLS; PROTEIN; DYNAMICS; MITOSIS; IDENTIFICATION; INVITRO;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
43
Recensione:
Indirizzi per estratti:
Citazione:
D. Masson e T.E. Kreis, "BINDING OF E-MAP-115 TO MICROTUBULES IS REGULATED BY CELL CYCLE-DEPENDENT PHOSPHORYLATION", The Journal of cell biology, 131(4), 1995, pp. 1015-1024

Abstract

Expression levels of E-MAP-115, a microtubule-associated protein thatstabilizes microtubules, increase with epithelial cell polarization and differentiation (Masson and Kreis, 1993). Although polarizing cellscontain significant amounts of this protein, they can still divide and thus all stabilized microtubules must disassemble at the onset of mitosis to allow formation of the dynamic mitotic spindle, We show here that binding of E-MAP-115 to microtubules is regulated by phosphorylation during the cell cycle, Immunolabeling of HeLa cells for E-MAP-115 indicates that the protein is absent from microtubules during early prophase and progressively reassociates with microtubules after late prophase, A fraction of E-MAP-115 from HeLa cells released from a block at the G1/S boundary runs with higher apparent molecular weight on SDS-PAGE, with a peak correlating with the maximal number of cells in early stages of mitosis, E-MAP-115 from nocodazole-arrested mitotic cells,which can be obtained in larger amounts, displays identical modifications and was used for further biochemical characterization. The level of incorporation of P-32 into mitotic E-MAP-115 is about 15-fold higher than into the interphase protein. Specific threonine phosphorylationoccurs in mitosis, and the amount of phosphate associated with serinealso increases. Hyperphosphorylated E-MAP-115 from mitotic cells cannot bind stably to microtubules in vitro. These results suggest that phosphorylation of E-MAP-115 is a prerequisite for increasing the dynamic properties of the interphase microtubules which leads to the assembly of the mitotic spindle at the onset of mitosis. Microtubule-associated proteins are thus most likely key targets for kinases which controlchanges in microtubule dynamic properties at the G2- to M-phase transition.

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Documento generato il 27/09/20 alle ore 22:55:07