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Comparative analyses of the Conserved Oligomeric Golgi (COG) complex in vertebrates.

Quental R, Azevedo L, Matthiesen R, Amorim A - BMC Evol. Biol. (2010)

Bottom Line: The results showed that all COG subunits are evolving under strong purifying selection, although COG1 seems to evolve faster than the remaining proteins.COG 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.

View Article: PubMed Central - HTML - PubMed

Affiliation: Institute of Molecular Pathology and Immunology of the University of Porto, Portugal. aquental@ipatimup.pt

ABSTRACT

Background: The 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.

Results: We 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.

Conclusions: COG 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.

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Schematic architectural representation of mammalian COG complex. COG is organized in two heterotrimeric subcomplexes (Cog2 to Cog4 and Cog5 to Cog7), which are connected by a heterodimer (Cog1 and Cog8). Numbers represent COG subunits. Adapted from [29].
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Figure 1: Schematic architectural representation of mammalian COG complex. COG is organized in two heterotrimeric subcomplexes (Cog2 to Cog4 and Cog5 to Cog7), which are connected by a heterodimer (Cog1 and Cog8). Numbers represent COG subunits. Adapted from [29].

Mentions: COG complex is composed by eight distinct subunits [10,12,13,24-26], Cog1 to Cog8, arranged in two lobes consisting of Cog1 to Cog4 (lobe A) and Cog5 to Cog8 (lobe B) [10]. Although several models have been advanced refining the architecture of COG [22,27-29], the most recent studies converge in suggesting that mammalian COG members are organized in two heterotrimeric groups, Cog2-Cog3-Cog4 and Cog5-Cog6-Cog7, which are linked by the dimeric group formed by Cog1 and Cog8. In particular, Cog1 associates with Cog2-Cog3-Cog4, whereas Cog8 interacts with Cog5-Cog6-Cog7 (Figure 1) [22,29].


Comparative analyses of the Conserved Oligomeric Golgi (COG) complex in vertebrates.

Quental R, Azevedo L, Matthiesen R, Amorim A - BMC Evol. Biol. (2010)

Schematic architectural representation of mammalian COG complex. COG is organized in two heterotrimeric subcomplexes (Cog2 to Cog4 and Cog5 to Cog7), which are connected by a heterodimer (Cog1 and Cog8). Numbers represent COG subunits. Adapted from [29].
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC2927914&req=5

Figure 1: Schematic architectural representation of mammalian COG complex. COG is organized in two heterotrimeric subcomplexes (Cog2 to Cog4 and Cog5 to Cog7), which are connected by a heterodimer (Cog1 and Cog8). Numbers represent COG subunits. Adapted from [29].
Mentions: COG complex is composed by eight distinct subunits [10,12,13,24-26], Cog1 to Cog8, arranged in two lobes consisting of Cog1 to Cog4 (lobe A) and Cog5 to Cog8 (lobe B) [10]. Although several models have been advanced refining the architecture of COG [22,27-29], the most recent studies converge in suggesting that mammalian COG members are organized in two heterotrimeric groups, Cog2-Cog3-Cog4 and Cog5-Cog6-Cog7, which are linked by the dimeric group formed by Cog1 and Cog8. In particular, Cog1 associates with Cog2-Cog3-Cog4, whereas Cog8 interacts with Cog5-Cog6-Cog7 (Figure 1) [22,29].

Bottom Line: The results showed that all COG subunits are evolving under strong purifying selection, although COG1 seems to evolve faster than the remaining proteins.COG 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.

View Article: PubMed Central - HTML - PubMed

Affiliation: Institute of Molecular Pathology and Immunology of the University of Porto, Portugal. aquental@ipatimup.pt

ABSTRACT

Background: The 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.

Results: We 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.

Conclusions: COG 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.

Show MeSH
Related in: MedlinePlus