Oligomerization of a trans-Golgi/trans-Golgi network retained protein occurs in the Golgi complex and may be part of its retention.

The mouse hepatitis virus M protein is a triple spanning membrane glycoprotein that, when expressed independently, localizes to trans-Golgi as well as to the trans-Golgi network (TGN). Passage of this protein from the endoplasmic reticulum through the intermediate compartment to the late Golgi and TGN can be conveniently followed by analyzing its O-linked sugars. Using pulse-chase analyses we studied the oligomerization of the M protein in sucrose gradients. The Golgi and TGN forms migrated as large heterogeneous complexes, whereas the endoplasmic reticulum and intermediate compartment forms of the protein appeared to migrate as monomer. Moreover, a mutant of the M protein lacking the 22 COOH-terminal amino acids, that is transported to the plasma membrane, gave rise to similar complexes, albeit smaller in size, that persisted at the plasma membrane. We propose that the trans-Golgi/TGN retention of the MHV-M protein is governed by two mechanisms: oligomerization possibly mediated by the transmembrane domains and binding of its cytoplasmic tail to cellular factors in trans Golgi/TGN.