Trafficking of human ADAM 12-L: retention in the trans-Golgi network

Biochem Biophys Res Commun. 2000 Aug 28;275(2):261-7. doi: 10.1006/bbrc.2000.3295.


We have investigated the trafficking of the membrane-anchored form of human ADAM 12 (ADAM 12-L) fused to a green fluorescence protein tag. Subcellular localization of the protein in transiently transfected cells was determined by fluorescence microscopy and trypsin sensitivity. Full-length ADAM 12-L was retained in a perinuclear compartment, which was shown to be the trans-Golgi network. In contrast, ADAM 12-L lacking the cytoplasmic domain reached the cell surface. Based on analysis of deletions and mutations of the cytoplasmic tail of ADAM 12-L, the retention signal is comprised of both the cytoplasmic and transmembrane domains, but not the Src homology 3 domain (SH3) binding sites. These results raise the possibility that a trafficking checkpoint in the trans-Golgi network is one of the cellular mechanisms for regulation of ADAM 12-L function, by allowing a rapid release of ADAM 12-L to the cell surface under specific stimuli.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • ADAM Proteins
  • ADAM12 Protein
  • Animals
  • Biological Transport
  • CHO Cells
  • COS Cells
  • Cell Compartmentation
  • Cell Membrane / metabolism
  • Cricetinae
  • Cytoplasm / metabolism
  • Golgi Apparatus / metabolism*
  • HeLa Cells
  • Humans
  • Immunohistochemistry
  • Membrane Proteins / biosynthesis
  • Membrane Proteins / metabolism*
  • Metalloendopeptidases / biosynthesis
  • Metalloendopeptidases / metabolism*
  • Microscopy, Fluorescence
  • Octoxynol


  • Membrane Proteins
  • Octoxynol
  • ADAM Proteins
  • ADAM12 Protein
  • ADAM12 protein, human
  • Metalloendopeptidases