Abstract
BackgroundThe Conserved Oligomeric Golgi (COG) complex is an eight-subunit assembly that localizes peripherally to Golgi membranes and is involved in retrograde vesicular trafficking. COG subunits are organized in two heterotrimeric groups, Cog2, -3, -4 and Cog5, -6, -7, linked by a dimeric group formed by Cog1 and Cog8. Dysfunction of COG complex in humans has been associated with new forms of Congenital Disorders of Glycosylation (CDG), therefore highlighting its essential role. In the present study, we intended to gain further insights into the evolution of COG subunits in vertebrates, using comparative analyses of all eight COG proteins.ResultsWe used protein distances and dN/dS ratios as a measure of the rate of proteins evolution. The results showed that all COG subunits are evolving under strong purifying selection, although COG1 seems to evolve faster than the remaining proteins. In addition, we also tested the expression of COG genes in 20 human tissues, and demonstrate their ubiquitous nature.ConclusionsCOG complex has a critical role in Golgi structure and function, which, in turn, is involved in protein sorting and glycosylation. The results of this study suggest that COG subunits are evolutionary constrained to maintain the interactions between each other, as well with other partners involved in vesicular trafficking, in order to preserve both the integrity and function of the complex.
Highlights
The Conserved Oligomeric Golgi (COG) complex is an eight-subunit assembly that localizes peripherally to Golgi membranes and is involved in retrograde vesicular trafficking
This is well illustrated by mutations in COG-specific subunits, which give rise to different human diseases belonging to the Congenital Disorders of Glycosylation (CDG)
In turn, we have investigated the evolution of different subunits belonging to the same protein complex in vertebrates
Summary
The Conserved Oligomeric Golgi (COG) complex is an eight-subunit assembly that localizes peripherally to Golgi membranes and is involved in retrograde vesicular trafficking. Dysfunction of COG complex in humans has been associated with new forms of Congenital Disorders of Glycosylation (CDG), highlighting its essential role. Most cellular processes are carried out by multiprotein complexes that constitute important functional units in the cell [1]. This fact has motivated a number of studies aiming to investigate the structure, function and evolution of such multisubunit molecular machines [e.g., [14]]. A cellular process in which protein complexes are known to be involved is the transport of proteins between cellular compartments (vesicular trafficking) [5,6]. Several large protein complexes play an important role in the fidelity of vesicle
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