Deubiquitination, a new player in Golgi to endoplasmic reticulum retrograde transport
Deubiquitination, a new player in Golgi to endoplasmic reticulum retrograde transport
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DOI：
10.1074/jbc.c300451200
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发表时间：
2003-12-26
影响因子：
4.8
通讯作者：
Dargemont, C
中科院分区：
文献类型：
--
作者：
Cohen, M;Stutz, F;Dargemont, C
泛素的修饰在广泛的细胞功能中起着重要作用。虽然这个过程的逆转，去泛素化，可能代表了一个重要的调节步骤，有助于细胞内稳态，去泛素化酶的功能仍然很差的特点。我们以前已经表明，泛素蛋白酶Ubp 3 p需要一个辅因子，Bre 5 p，专门deubiquitinate的外壳蛋白复合物II（COPII）亚基Sec 23 p，这是参与内质网和高尔基体之间的顺行运输。在本报告中，我们表明，BRE 5基因的破坏也导致了从高尔基体到内质网的逆行运输的缺陷。进一步的分析表明，COPI亚基β '-COP代表Ubp 3 p的另一种底物。Bre 5 p复合物。总之，我们的结果表明，Ubp 3 p. Bre 5 p去泛素化复合物协同调节内质网和高尔基体间的顺行和逆行转运。
Modification by ubiquitin plays a major role in a broad array of cellular functions. Although reversal of this process, deubiquitination, likely represents an important regulatory step contributing to cellular homeostasis, functions of deubiquitination enzymes still remain poorly characterized. We have previously shown that the ubiquitin protease Ubp3p requires a co-factor, Bre5p, to specifically deubiquitinate the coat protein complex II ( COPII) subunit Sec23p, which is involved in anterograde transport between endoplasmic reticulum and Golgi compartiments. In the present report, we show that disruption of BRE5 gene also led to a defect in the retrograde transport from the Golgi to the endoplasmic reticulum. Further analysis indicate that the COPI subunit beta'-COP represents another substrate of the Ubp3p . Bre5p complex. All together, our results indicate that the Ubp3p . Bre5p deubiquitination complex co-regulates anterograde and retrograde transports between endoplasmic reticulum and Golgi compartments.