Molecular and clinical characterization of a Moroccan Cog7 deficient patient

Ng, Bobby G.; Kranz, Christian; Hagebeuk, Eeo E. O.; Durán, Marinus; Abeling, Nggm G. G. M.; Wuyts, Birgitte; Ungár, Dániel; Lupashin, Vladimir; Hartdorff, Cm M.; Poll-Thé, Bwee Tien; Freeze, Hudson H.

doi:10.1016/j.ymgme.2007.02.011

Cited by 54 publications

(47 citation statements)

References 11 publications

(21 reference statements)

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“…Mutations in the genes encoding human COG1, COG4-COG8 have been associated with congenital disorders of glycosylation (CDG) (Foulquier et al, 2006;Foulquier et al, 2007;Kranz 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) suggesting a role for COG in the retention and/or retrieval of Golgi glycosylation enzymes. Indeed, loss of COG subunits impaired the localisation and the stability of Golgi resident proteins, which are known to recycle within the Golgi stacks (Oka et al, 2004;Zolov and Lupashin, 2005).…”

Section: Discussionmentioning

confidence: 99%

“…It was surprising that flies homozygous for null alleles of Cog7 were viable, although males were sterile and displayed various defects during spermatogenesis, as mutations in the gene encoding human Cog7 are associated with a lethal congenital disorder of glycosylation (CDG), causing multisystemic deficiencies including neurological, metabolic and anatomical abnormalities (Morava et al, 2007;Ng et al, 2007;Wu et al, 2004).…”

Section: Discussionmentioning

confidence: 99%

“…Loss of human COG7 is responsible for a rare, congenital disorder of glycosylation (CDG), namely CDG IIe (Morava et al, 2007;Ng et al, 2007;Wu et al, 2004). We show that mutants carrying null alleles of Drosophila Cog7 are viable but male sterile.…”

Section: Introductionmentioning

confidence: 93%

“…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%

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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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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 93%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Mutations inCog7affect Golgi structure, meiotic cytokinesis and sperm development duringDrosophilaspermatogenesis

Belloni

Sechi

Riparbelli

et al. 2012

Journal of Cell Science

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“…Among the known multisubunit tethering complexes, only COG (23)(24)(25)(26)(27)(28) and TRAPP (29) have been directly implicated in human genetic disease. Mutations in the Cog1 (24), Cog7 (26)(27)(28), and Cog8 (23,25) subunits cause type II congenital disorders of glycosylation (CDGs).…”

mentioning

confidence: 99%

Structural basis for a human glycosylation disorder caused by mutation of the COG4 gene

Richardson

Smith

Ungár

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

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The proper glycosylation of proteins trafficking through the Golgi apparatus depends upon the conserved oligomeric Golgi (COG) complex. Defects in COG can cause fatal congenital disorders of glycosylation (CDGs) in humans. The recent discovery of a form of CDG, caused in part by a COG4 missense mutation changing Arg 729 to Trp, prompted us to determine the 1.9 Å crystal structure of a Cog4 C-terminal fragment. Arg 729 is found to occupy a key position at the center of a salt bridge network, thereby stabilizing Cog4's small C-terminal domain. Studies in HeLa cells reveal that this C-terminal domain, while not needed for the incorporation of Cog4 into COG complexes, is essential for the proper glycosylation of cell surface proteins. We also find that Cog4 bears a strong structural resemblance to exocyst and Dsl1p complex subunits. These complexes and others have been proposed to function by mediating the initial tethering between transport vesicles and their membrane targets; the emerging structural similarities provide strong evidence of a common evolutionary origin and may reflect shared mechanisms of action.congenital disorder of glycosylation ͉ Golgi apparatus ͉ multi-subunit tethering complex ͉ vesicle trafficking ͉ X-ray crystallography M ultiple lines of evidence implicate the conserved oligomeric Golgi (COG) complex in retrograde transport within the Golgi apparatus (1, 2). For example, partial knockdown of mammalian COG3 permitted exocytosis, while simultaneously blocking the retrograde transport of Shiga toxin from endosomes to the ER (3). COG was initially isolated from bovine brain on the basis of its ability to stimulate an in vitro Golgi transport assay (4). Two of its 8 subunits, Cog1/ldlB and Cog2/ ldlC, had previously been identified in a genetic screen for compromised cell surface receptor stability (5, 6). In the yeast Saccharomyces cerevisiae, the COG complex was discovered through studies of one of its subunits, Cog8p/Dor1p. Implicated in vesicle targeting to the Golgi apparatus, Cog8p was found to co-immunoprecipitate with 7 other polypeptides (7). The 7 associated polypeptides included two (Cog2p/Sec35p and Cog3p/ Sec34p) that had earlier been identified in genetic screens for temperature-sensitive mutations causing secretion defects (8). In further support of a role in trafficking to and within the Golgi, COG interacts physically with a large number of Golgi-localized trafficking factors, including (in yeast) the Rab family G protein Ypt1p, the SNAREs Sed5p, Ykt6p, Gos1p, and Sec22p, and COPI vesicle coat proteins (9).COG is one of several large protein complexes proposed to function as multisubunit tethering factors, mediating the initial interaction between transport vesicles and their target membranes (2, 10-12). For many of these complexes, a dearth of structural information has slowed the development of mechanistic models and has made it difficult to know how-or whether-to apply lessons learned from studies of one complex to another. Subunits of the COG, exocyst, Dsl1p, and Golgiassoci...

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Maintaining order: COG complex controls Golgi trafficking, processing, and sorting

2019

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The conserved oligomeric Golgi (COG) complex, a multisubunit tethering complex of the CATCHR (complexes associated with tethering containing helical rods) family, controls membrane trafficking and ensures Golgi homeostasis by orchestrating retrograde vesicle targeting within the Golgi. In humans, COG defects lead to severe multisystemic diseases known as COG‐congenital disorders of glycosylation (COG‐CDG). The COG complex both physically and functionally interacts with all classes of molecules maintaining intra‐Golgi trafficking, namely SNAREs, SNARE‐interacting proteins, Rabs, coiled‐coil tethers, and vesicular coats. Here, we review our current knowledge of COG‐related trafficking and glycosylation defects in humans and model organisms, and analyze possible scenarios for the molecular mechanism of the COG orchestrated vesicle targeting.

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Molecular and clinical characterization of a Moroccan Cog7 deficient patient

Cited by 54 publications

References 11 publications

Mutations inCog7affect Golgi structure, meiotic cytokinesis and sperm development duringDrosophilaspermatogenesis

Mutations inCog7affect Golgi structure, meiotic cytokinesis and sperm development duringDrosophilaspermatogenesis

Structural basis for a human glycosylation disorder caused by mutation of the COG4 gene

Maintaining order: COG complex controls Golgi trafficking, processing, and sorting

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