Impaired glycosylation and cutis laxa caused by mutations in the vesicular 
H+-ATPase subunit ATP6V0A2

Kornak, Uwe; Reynders, Ellen; Dimopoulou, Aikaterini; van Reeuwijk, Jeroen; Fischer, Bjoern; Rajab, Anna; Budde, Birgit; Nürnberg, Peter; Foulquier, Francois; Lefeber, Dirk; Urban, Zsolt; Gruenewald, Stephanie; Annaert, Wim; Brunner, Han G; van Bokhoven, Hans; Wevers, Ron; Morava, Eva; Matthijs, Gert; Van Maldergem, Lionel; Mundlos, Stefan; The ARCL Debré-type Study Group

doi:10.1038/ng.2007.45

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Impaired glycosylation and cutis laxa caused by mutations in the vesicular H+-ATPase subunit ATP6V0A2

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Kornak, Uwe
Research Group Development & Disease (Head: Stefan Mundlos), Max Planck Institute for Molecular Genetics, Max Planck Society;

Dimopoulou, Aikaterini
Max Planck Society;

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Mundlos, Stefan
Research Group Development & Disease (Head: Stefan Mundlos), Max Planck Institute for Molecular Genetics, Max Planck Society;

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Citation

Kornak, U., Reynders, E., Dimopoulou, A., van Reeuwijk, J., Fischer, B., Rajab, A., et al. (2008). Impaired glycosylation and cutis laxa caused by mutations in the vesicular H+-ATPase subunit ATP6V0A2. Nature Genetics, 40(1), 32-34. doi:10.1038/ng.2007.45.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0010-80BD-3

Abstract

We identified loss-of-function mutations in ATP6V0A2, encoding the a2 subunit of the V-type H+ ATPase, in several families with autosomal recessive cutis laxa type II or wrinkly skin syndrome. The mutations result in abnormal glycosylation of serum proteins (CDG-II) and cause an impairment of Golgi trafficking in fibroblasts from affected individuals. These results indicate that the a2 subunit of the proton pump has an important role in Golgi function.