The E2-C vihar is required for the correct spatiotemporal proteolysis of cyclin B and itself undergoes cyclical degradation

Endre Máthé, Claudine Kraft, Régis Giet, P. Deák, Jan Michael Peters, David M. Glover

Research output: Contribution to journalArticle

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Abstract

Background: Proteolytic degradation of mitotic regulatory proteins first requires these targets to be ubiquitinated. This is regulated at the level of conjugation of ubiquitin to substrates by the anaphase-promoting complex/cyclosome (APC/C) ubiquitin-protein ligase. Substrate specificity and temporal activity of the APC/C has been thought to lie primarily with its two activators, Cdc20/Fizzy and Cdh1/Fizzy-related. Results: Here, we show that reduction in the E2 ubiquitin-conjugating enzyme (UBC) of the E2-C family that is encoded by the Drosophila gene vihar (vih), by either mutation or RNAi, leads to an accumulation of cells in a metaphase-like state. Cyclin B accumulates to high levels in all mitotic vih cells, particularly at the spindle poles. Vihar E2-C is present in the cytoplasm of mitotic cells but also associates with centrosomes, and its own degradation is initiated at the metaphase-anaphase transition. Expression of destruction D box mutants of vihar in the syncytial embryo results in mitotic arrest at late anaphase. In contrast to hypomorphic mutants, Cyclin B is degraded at the spindle poles and accumulates in the equatorial region of the spindle. Conclusions: In Drosophila, the Vihar E2 UBC contributes to the spatiotemporal control of Cyclin B degradation that first occurs at the spindle poles. APC/C-mediated proteolysis of Vihar E2-C autoinactivates the APC/C at the centrosome before a second wave of proteolysis to degrade Cyclin B on the rest of the spindle and elsewhere in the cell.

Original languageEnglish
Pages (from-to)1723-1733
Number of pages11
JournalCurrent Biology
Volume14
Issue number19
DOIs
Publication statusPublished - Oct 5 2004

Fingerprint

Anaphase-Promoting Complex-Cyclosome
Proteolysis
Cyclin B
cyclins
Spindle Poles
proteolysis
ubiquitin-protein ligase
Ubiquitin-Conjugating Enzymes
Degradation
centrosomes
Poles
Centrosome
Anaphase
degradation
anaphase
Metaphase
metaphase
Drosophila
cells
mutants

ASJC Scopus subject areas

  • Agricultural and Biological Sciences(all)

Cite this

The E2-C vihar is required for the correct spatiotemporal proteolysis of cyclin B and itself undergoes cyclical degradation. / Máthé, Endre; Kraft, Claudine; Giet, Régis; Deák, P.; Peters, Jan Michael; Glover, David M.

In: Current Biology, Vol. 14, No. 19, 05.10.2004, p. 1723-1733.

Research output: Contribution to journalArticle

Máthé, Endre ; Kraft, Claudine ; Giet, Régis ; Deák, P. ; Peters, Jan Michael ; Glover, David M. / The E2-C vihar is required for the correct spatiotemporal proteolysis of cyclin B and itself undergoes cyclical degradation. In: Current Biology. 2004 ; Vol. 14, No. 19. pp. 1723-1733.
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AU - Peters, Jan Michael

AU - Glover, David M.

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N2 - Background: Proteolytic degradation of mitotic regulatory proteins first requires these targets to be ubiquitinated. This is regulated at the level of conjugation of ubiquitin to substrates by the anaphase-promoting complex/cyclosome (APC/C) ubiquitin-protein ligase. Substrate specificity and temporal activity of the APC/C has been thought to lie primarily with its two activators, Cdc20/Fizzy and Cdh1/Fizzy-related. Results: Here, we show that reduction in the E2 ubiquitin-conjugating enzyme (UBC) of the E2-C family that is encoded by the Drosophila gene vihar (vih), by either mutation or RNAi, leads to an accumulation of cells in a metaphase-like state. Cyclin B accumulates to high levels in all mitotic vih cells, particularly at the spindle poles. Vihar E2-C is present in the cytoplasm of mitotic cells but also associates with centrosomes, and its own degradation is initiated at the metaphase-anaphase transition. Expression of destruction D box mutants of vihar in the syncytial embryo results in mitotic arrest at late anaphase. In contrast to hypomorphic mutants, Cyclin B is degraded at the spindle poles and accumulates in the equatorial region of the spindle. Conclusions: In Drosophila, the Vihar E2 UBC contributes to the spatiotemporal control of Cyclin B degradation that first occurs at the spindle poles. APC/C-mediated proteolysis of Vihar E2-C autoinactivates the APC/C at the centrosome before a second wave of proteolysis to degrade Cyclin B on the rest of the spindle and elsewhere in the cell.

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