Conserved oligomeric Golgi complex subunit 1 deficiency reveals a previously uncharacterized congenital disorder of glycosylation type II

Foulquier, François; Vasile, Eliza; Schollen, E; Callewaert, Nico; Raemaekers, Tim; Quelhas, Dulce; Jaeken, Jacques; Mills, Philippa B.; Winchester, Bryan; Krieger, Monty; Annaert, Wim; Matthijs, Gert

doi:10.1073/pnas.0507685103

Cited by 165 publications

(157 citation statements)

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“…In deed, Loss of the Cog7 subunit was seen to disrupt Lobe B, alter both N-and O-Linked glycosylation and alter retrograde Golgi trafficking. Recently mutations in Cog1 subunit have yielded similar biochemical results, but the patient had a much milder phenotype [4].…”

Section: Discussionmentioning

confidence: 83%

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Molecular and clinical characterization of a Moroccan Cog7 deficient patient

Kranz

Hagebeuk

et al. 2007

Molecular Genetics and Metabolism

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Mutations in the N-linked glycosylation pathway cause rare autosomal recessive defects known as Congenital Disorders of Glycosylation (CDG). A previously reported mutation in the Conserved Oligomeric Golgi complex gene, COG7, defined a new subtype of CDG in a Tunisian family. The mutation disrupted the hetero-octomeric COG complex and altered both N-and O-linked glycosylation. Here we present clinical and biochemical data from a second family with the same mutation.

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Section: Discussionmentioning

confidence: 83%

“…CDG-II patients have been reported with mutations in glycosyltransferases (MGAT2 and B4GALT1), Golgi based sugar transporters (SLC35A1 and FUCT1) and in a processing glucosidase [2]. More recently, a new family of CDG defects was identified with mutations in Conserved Oligomeric Golgi complex genes, COG7 and COG1 [3,4].…”

Section: Introductionmentioning

confidence: 99%

Molecular and clinical characterization of a Moroccan Cog7 deficient patient

Kranz

Hagebeuk

et al. 2007

Molecular Genetics and Metabolism

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“…In yeast, subunits of Lobe A are essential components of the complex (VanRheenen et al, 1998;Whyte and Munro, 2001;Wuestehube et al, 1996), whereas Lobe B subunits are not substantially required for cell growth or internal membrane organisation (Ram et al, 2002;Whyte and Munro, 2001). Mutations in the genes encoding human COG1, COG4-COG8 have been associated with congenital disorders of glycosylation (CDG) (Foulquier et al, 2006Foulquier et al, 2007Kranz et al, 2007;Lübbehusen et al, 2010;Ng et al, 2007;Paesold-Burda et al, 2009;Reynders et al, 2009;Spaapen et al, 2005;Steet and Kornfeld, 2006;Wu et al, 2004) indicating a role for COG in the transport and/or stability of Golgi glycosylation enzymes. Indeed studies in both yeast and mammalian cells have suggested that COG complex might function as a vesicle-tethering factor in intra-Golgi retrograde COPI transport (Ungar et al, 2002), thus regulating the distribution and the stability of Golgi resident proteins (Oka et al, 2004;Shestakova et al, 2006;Suvorova et al, 2001;Suvorova et al, 2002;Walter et al, 1998).…”

Section: Introductionmentioning

confidence: 99%

Mutations inCog7affect Golgi structure, meiotic cytokinesis and sperm development duringDrosophilaspermatogenesis

Belloni

Sechi

Riparbelli

et al. 2012

Journal of Cell Science

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SummaryThe conserved oligomeric Golgi (COG) complex plays essential roles in Golgi function, vesicle trafficking and glycosylation. Deletions in the human COG7 gene are associated with a rare multisystemic congenital disorder of glycosylation that causes mortality within the first year of life. In this paper, we characterise the Drosophila orthologue of COG7 (Cog7). Loss-of-function Cog7 mutants are viable but male sterile. The Cog7 gene product is enriched in the Golgi stacks and in Golgi-derived structures throughout spermatogenesis. Mutations in the Cog7 gene disrupt Golgi architecture and reduce the number of Golgi stacks in primary spermatocytes. During spermiogenesis, loss of the Cog7 protein impairs the assembly of the Golgi-derived acroblast in spermatids and affects axoneme architecture. Similar to the Cog5 homologue, four way stop (Fws), Cog7 enables furrow ingression during cytokinesis. We show that the recruitment of the small GTPase Rab11 and the phosphatidylinositol transfer protein Giotto (Gio) to the cleavage site requires a functioning wild-type Cog7 gene. In addition, Gio coimmunoprecipitates with Cog7 and with Rab11 in the testes. Our results altogether implicate Cog7 as an upstream component in a gio-Rab11 pathway controlling membrane addition during cytokinesis.

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“…The identification of milder cases of COG6 and COG7 deficiency harboring different mutations [56,57] however shows that the severity of the disease does not simply relate to the subunit affected but rather to the capability of forming a fully functional COG complex. Besides the severe diseases observed for COG6 and COG7 defects, moderate clinical manifestations have been associated with mutations in COG1 [58,59] COG subunits build a complex of two lobes, including COG1 to COG4 in lobe A and COG5 to COG8 in lobe B (Figure 4). In general, defects in lobe A lead to milder disease than defects in lobe B. Lobe A appears to be important for overall Golgi architecture, playing a role in Golgi organization and cisGolgi sorting [66].…”

Section: Localization Of Glycosyltransferasesmentioning

confidence: 99%

Section: Localization Of Glycosyltransferasesmentioning

confidence: 99%

Congenital disorders of glycosylation: a concise chart of glycocalyx dysfunction

Hennet

Cabalzar

2015

Trends in Biochemical Sciences

112

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Glycosylation is a ubiquitous modification of lipids and proteins. Despite the essential contribution of glycoconjugates to the viability of all living organisms, diseases of glycosylation in humans have only been identified over the past few decades. The recent development of next-generation DNA sequencing techniques has accelerated the pace of discovery of novel glycosylation defects. The description of multiple mutations across glycosylation pathways not only revealed tremendous diversity in functional impairments, but also pointed to phenotypic similarities, emphasizing the interconnected flow of substrates underlying glycan assembly. The current list of 100 known glycosylation disorders provides an overview of the significance of glycosylation in human development and physiology. Congenital disorders of glycosylation -a consice chart of glycocalyx dysfunctionThierry Hennet, Jürg Cabalzar Institute of Physiology, University of Zurich, CH-8057 Zurich, Switzerland AbstractGlycosylation is a ubiquitous modification of lipids and proteins. Despite the essential contribution of glycoconjugates to the viability of all living organisms, diseases of glycosylation in humans have only been identified over the past few decades. The recent development of next-generation DNA sequencing techniques has accelerated the pace of discovery of novel glycosylation defects. The description of multiple mutations across glycosylation pathways has revealed a tremendous diversity of functional impairments bus also pointed to phenotypic similarities emphasizing the interconnected flow of substrates underlying glycan assembly. The current list of 100 known glycosylation disorders provides an overview on the significance of glycosylation in human development and physiology. Highlights Congenital disorders underline the role of glycosylation in human development.  Next-gen sequencing techniques expanded the discovery of glycosylation gene defects.  The clinical variability of glycosylation disorders implies they are underdiagnosed. Glycosylation disordersGlycosylation is by far the most complex form of protein [1,2] and lipid modification [3,4] in all domains of life. The tremendous diversity of glycoconjugate structures resulting from intricate biosynthetic pathways is a major factor hampering the assignment of functions to glycans chains. Much has been learnt from the study of disrupted glycosylation genes in model organisms, thereby establishing numerous essential contributions of glycans in regulating cell and organ functions [5]. The study of human diseases of glycosylation brings additional insights by providing a more differentiated view on glycan functions. Indeed, most human mutations are hypomorphic, thus causing partial loss of glycosylation reactions that lead to variable clinical manifestations.Diseases of glycosylation are also referred to as congenital disorders of glycosylation (CDG). Given the heterogeneity of glycans, the clinical scope of CDG is considerable, ranging from nearly normal phenotypes to sever...

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Conserved oligomeric Golgi complex subunit 1 deficiency reveals a previously uncharacterized congenital disorder of glycosylation type II

Abstract: The conserved oligomeric Golgi (COG) complex is a heterooctameric complex that regulates intraGolgi trafficking and the integrity of the Golgi compartment in eukaryotic cells. Here, we describe a patient with a mild form of congenital disorder of glycosylation type II (

Cited by 165 publications

References 36 publications

Molecular and clinical characterization of a Moroccan Cog7 deficient patient

Molecular and clinical characterization of a Moroccan Cog7 deficient patient

Mutations inCog7affect Golgi structure, meiotic cytokinesis and sperm development duringDrosophilaspermatogenesis

Congenital disorders of glycosylation: a concise chart of glycocalyx dysfunction

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