HID-1 is a peripheral membrane protein primarily associated with the medial- and trans- Golgi apparatus.
10.1007/s13238-011-1008-3
- Author:
Lifen WANG
1
;
Yi ZHAN
;
Eli SONG
;
Yong YU
;
Yaming JIU
;
Wen DU
;
Jingze LU
;
Pingsheng LIU
;
Pingyong XU
;
Tao XU
Author Information
1. National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China.
- Publication Type:Journal Article
- MeSH:
Animals;
Brefeldin A;
pharmacology;
Cell Line, Tumor;
Cytosol;
drug effects;
metabolism;
Humans;
Intracellular Space;
drug effects;
metabolism;
Membrane Proteins;
metabolism;
Protein Transport;
drug effects;
Rats;
Vesicular Transport Proteins;
metabolism;
trans-Golgi Network;
drug effects;
metabolism
- From:
Protein & Cell
2011;2(1):74-85
- CountryChina
- Language:English
-
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.
