The localisation of glycosylation enzymes within the Golgi apparatus is fun
damental to the regulation of glycoprotein and glycolipid biosynthesis. Reg
ions responsible for specifying Golgi localisation have been identified in
numerous Golgi resident enzymes. The transmembrane domain of Golgi glycosyl
transferases provides a dominant localisation signal and in many cases ther
e are also major contributions from the lumenal domain. The mechanism by wh
ich these targeting domains function in maintaining an asymmetric distribut
ion of Golgi resident glycosylation enzymes has been intensely debated in r
ecent years. It is now clear that the targeting of Golgi resident enzymes i
s intimately associated with the organisation of Golgi membranes and the co
ntrol of protein and lipid traffic in both anterograde and retrograde direc
tions. Here we discuss the recent advances into how Golgi targeting signals
of glycosylation enzymes function, and propose a model for maintaining the
steady-state localisation of Golgi glycosyltransferases. (C) 2001 Societe
francaise de biochimie et biologic moleculaire/Editions scientifiques et me
dicales Elsevier SAS. All rights reserved.