It depends on whether you are referring to glycosylation site occupation dependent oligomerization (presence/absence of the glycan at a specific Asn), or glycan structure dependent oligomerization (eg. branched structures/sialylation/fucosylation of a glycan on the Asn). For the latter, I have not come across any examples. Note that it is not to be confused with oligomerization dependent glycosylation, of which there are examples where monomeric proteins are glycosylated differently from their oligomeric counterparts, eg. HIV GP120. For the former, one example is IgM, where there is evidence that the absence of glycans at Asn563 of the heavy chain results in the formation of more hexameric IgM, rather than the pentameric IgM. However, this is a chicken-and-egg mystery between the Asn563 glycosylation and J-chain incorporation. Have a browse of these early publications on IgM, along with some of the references if you're interested.
http://www.ncbi.nlm.nih.gov/pubmed/9839552
http://www.ncbi.nlm.nih.gov/pubmed/807966
http://www.ncbi.nlm.nih.gov/pubmed/2665773
Dear Edward Moh,
Thank you for the response. What I specifically mean is presence of glycan results in oligomer formation and removal results in monomers. (So Oligomerization which is solely mediated by the presence of glycans at a particular site).
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