The N-terminal domains determine cellular localization and functions of the Doa4 and Ubp5 deubiquitinating enzymes
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- 作者：Nazia Woltersa ; Alexander Amerika ; b ; amerik.alexander@gmail.com" class="auth_mail" title="E-mail the corresponding author ; amerik@sky.chph.ras.ru" class="auth_mail" title="E-mail the corresponding author
- 关键词：Ubiquitin ; Deubiquitinating enzymes ; ESCRT-III ; Vacuolar protein sorting ; Cytokinesis
- 刊名：Biochemical and Biophysical Research Communications
- 出版年：2015
- 出版时间：20 November 2015
- 年：2015
- 卷：467
- 期：3
- 页码：570-576
- 全文大小：944 K
文摘
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The VPS protein Snf7 physically interacts with Doa4.
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Doa4 preferentially cleaves Lys63-linked ubiquitin oligomers involved in endocytosis and membrane protein trafficking.
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Unstable regulator of cytokynesis Hof1 is critical for the bud neck localization of Ubp5.