Oligomerization of a membrane protein correlates with its retention in the Golgi complex

It is not clear how the transmembrane domain of Gml molecules might interact to form a large oligomer. The large lumenal domain of Gml may sterically prevent direct interaction between many transmembrane domains to form an oligomer. Furthermore, the polar face of the ml domain itself could be expected to interact with at most one or two similar domains. The transmembrane domains of these proteins might interact to form small clusters (dimers or trimers) of Gml, mutant Gml proteins, and ~mlG. These clusters could be organized into large arrays by interactions between the heads and/or tails of proteins in different clusters. These structures might contain lipids and other endogenous Golgi-resident proteins. Association into such an array could prevent Golgi-resident proteins from entering transport vesicles and thereby function as a mechanism for their retention.