HID-1 is a peripheral membrane protein primarily associated with the medial- and trans- Golgi apparatus

Protein Cell. 2011 Jan;2(1):74-85. doi: 10.1007/s13238-011-1008-3. Epub 2011 Feb 20.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Brefeldin A / pharmacology
  • Cell Line, Tumor
  • Cytosol / drug effects
  • Cytosol / metabolism
  • Humans
  • Intracellular Space / drug effects
  • Intracellular Space / metabolism
  • Membrane Proteins / metabolism*
  • Protein Transport / drug effects
  • Rats
  • Vesicular Transport Proteins / metabolism*
  • trans-Golgi Network / drug effects
  • trans-Golgi Network / metabolism*


  • Membrane Proteins
  • Vesicular Transport Proteins
  • Brefeldin A