Author
Listed:
- Danming Tang
(Cellular and Developmental Biology, University of Michigan, 830 North University Avenue, Ann Arbor, Michigan 48109-1048, USA.)
- Yi Xiang
(Cellular and Developmental Biology, University of Michigan, 830 North University Avenue, Ann Arbor, Michigan 48109-1048, USA.)
- Stefano De Renzis
(European Molecular Biology Unit, Meyerhofstrasse 1, 69117 Heidelberg, Germany.)
- Jochen Rink
(Max Planck Institute of Molecular Cell Biology and Genetics, Pfotenhauerstrasse 108, 01307 Dresden, Germany.)
- Gen Zheng
(Cellular and Developmental Biology, University of Michigan, 830 North University Avenue, Ann Arbor, Michigan 48109-1048, USA.)
- Marino Zerial
(Max Planck Institute of Molecular Cell Biology and Genetics, Pfotenhauerstrasse 108, 01307 Dresden, Germany.)
- Yanzhuang Wang
(Cellular and Developmental Biology, University of Michigan, 830 North University Avenue, Ann Arbor, Michigan 48109-1048, USA.)
Abstract
Partitioning of the Golgi membrane into daughter cells during mammalian cell division occurs through a unique disassembly and reassembly process that is regulated by ubiquitination. However, the identity of the ubiquitin ligase is unknown. Here we show that the Homologous to the E6-AP Carboxyl Terminus (HECT) domain containing ubiquitin ligase HACE1 is targeted to the Golgi membrane through interactions with Rab proteins. The ubiquitin ligase activity of HACE1 in mitotic Golgi disassembly is required for subsequent postmitotic Golgi membrane fusion. Depletion of HACE1 using small interfering RNAs or expression of an inactive HACE1 mutant protein in cells impaired postmitotic Golgi membrane fusion. The identification of HACE1 as a Golgi-localized ubiquitin ligase provides evidence that ubiquitin has a critical role in Golgi biogenesis during the cell cycle.
Suggested Citation
Danming Tang & Yi Xiang & Stefano De Renzis & Jochen Rink & Gen Zheng & Marino Zerial & Yanzhuang Wang, 2011.
"The ubiquitin ligase HACE1 regulates Golgi membrane dynamics during the cell cycle,"
Nature Communications, Nature, vol. 2(1), pages 1-11, September.
Handle:
RePEc:nat:natcom:v:2:y:2011:i:1:d:10.1038_ncomms1509
DOI: 10.1038/ncomms1509
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