期刊
PROTEIN & CELL
卷 2, 期 1, 页码 74-85出版社
SPRINGEROPEN
DOI: 10.1007/s13238-011-1008-3
关键词
HID-1; Golgi; peripheral membrane protein; fluorescent recovery after photobleaching; N-myristoylation
类别
资金
- National Science Foundation of China [30870564, 30900268]
- The Beijing Natural Science Foundation [5092017]
- Major State Basic Research Program of China [2010CB833701]
- CAS [KSCX2-SW-224]
- CAS (Novo Nordisk-CAS)
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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