A tale of short tails, through thick and thin: investigating the sorting mechanisms of Golgi enzymes

FEBS Letters

article

Lawrence G. Welch¹  Sean Munro¹ 

[1] MRC Laboratory of Molecular Biology

关键词: cisternal maturation;    COPI;    glycosylation;    glycosyltransferase;    golgi;    golgi enzyme;    membrane thickness;    sorting motifs;   

DOI  :  10.1002/1873-3468.13553

来源: John Wiley & Sons Ltd.

【 摘 要 】

The Golgi apparatus is an important site for the modification of most secreted and membrane proteins. Glycan processing is the major class of modification and is mediated by a large number of Golgi-resident glycosyltransferases and glycosidases. These Golgi enzymes are largely type II transmembrane domain (TMD) proteins consisting of a short N-terminal cytosolic tail, a relatively short TMD and a lumenal ‘stem/stalk’ region which acts as a spacer between the catalytic domain and the lipid bilayer. The cytosolic tail, TMD, and stem together make what is termed the CTS domain which is responsible for the specific localisation of these enzymes within sub-Golgi compartments via multiple mechanisms. In addition, the catalytic domains of some Golgi enzymes are secreted as a consequence of proteolytic cleavage within their TMDs or stem regions. Finally, there is evidence to suggest that when the retention of Golgi enzymes is perturbed they are targeted for lysosomal degradation.

【 授权许可】

Unknown