HID-1 is a peripheral membrane protein primarily associated with the medial- and trans- Golgi apparatus |
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Authors: | Lifen Wang Yi Zhan Eli Song Yong Yu Yaming Jiu Wen Du Jingze Lu Pingsheng Liu Pingyong Xu Tao Xu |
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Affiliation: | 1. National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China; 2. Graduate School of the Chinese Academy of Sciences, Beijing 100864, China; 3. College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan 430074, China |
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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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Keywords: | HID-1 Golgi peripheral membrane protein fluorescent recovery after photobleaching N-myristoylation |
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