Lifen Wang, Yi Zhan, Eli Song, Yong Yu, Yaming Jiu, Wen Du, Jingze Lu, Pingsheng Liu, Pingyong Xu, Tao Xu. HID-1 is a peripheral membrane protein primarily associated with the medial- and trans-Golgi apparatus[J]. Protein&Cell, 2011, 2(1): 74-85. doi: 10.1007/s13238-011-1008-3
Citation:
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Lifen Wang, Yi Zhan, Eli Song, Yong Yu, Yaming Jiu, Wen Du, Jingze Lu, Pingsheng Liu, Pingyong Xu, Tao Xu. HID-1 is a peripheral membrane protein primarily associated with the medial- and trans-Golgi apparatus[J]. Protein&Cell, 2011, 2(1): 74-85. doi: 10.1007/s13238-011-1008-3
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Lifen Wang, Yi Zhan, Eli Song, Yong Yu, Yaming Jiu, Wen Du, Jingze Lu, Pingsheng Liu, Pingyong Xu, Tao Xu. HID-1 is a peripheral membrane protein primarily associated with the medial- and trans-Golgi apparatus[J]. Protein&Cell, 2011, 2(1): 74-85. doi: 10.1007/s13238-011-1008-3
Citation:
|
Lifen Wang, Yi Zhan, Eli Song, Yong Yu, Yaming Jiu, Wen Du, Jingze Lu, Pingsheng Liu, Pingyong Xu, Tao Xu. HID-1 is a peripheral membrane protein primarily associated with the medial- and trans-Golgi apparatus[J]. Protein&Cell, 2011, 2(1): 74-85. doi: 10.1007/s13238-011-1008-3
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HID-1 is a peripheral membrane protein primarily associated with the medial- and trans-Golgi apparatus
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Lifen Wang1,2
,
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Yi Zhan3
,
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Eli Song1
,
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Yong Yu1,2
,
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Yaming Jiu3
,
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Wen Du1
,
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Jingze Lu1
,
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Pingsheng Liu1
,
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Pingyong Xu1
,
,
,
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Tao Xu1,3
,
,
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1 National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China;
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2 Graduate School of the Chinese Academy of Sciences, Beijing 100864, China;
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3 College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan 430074, China
- Received Date: 2011-01-11
- Rev Recd Date:
2011-01-18
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Abstract
Caenorhabditis elegans hid-1 gene was first identified in a screen for mutants with a high-temperature-induced dauer formation (Hid) phenotype. Despite the fact that the hid-1 gene encodes a novel protein (HID-1) which is highly conserved from Caenorhabditis elegans to mammals, the domain structure, subcellular localization, and exact function of HID-1 remain unknown. Previous studies and various bioinformatic softwares predicted that HID-1 contained many transmembrane domains but no known functional domain. In this study, we revealed that mammalian HID-1 localized to the medial- and trans-Golgi apparatus as well as the cytosol, and the localization was sensitive to brefeldin A treatment. Next, we demonstrated that HID-1 was a peripheral membrane protein and dynamically shuttled between the Golgi apparatus and the cytosol. Finally, we verified that a conserved N-terminal myristoylation site was required for HID-1 binding to the Golgi apparatus. We propose that HID-1 is probably involved in the intracellular trafficking within the Golgi region.
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References
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Proportional views
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