Article
Mutations in the X-linked ATP6AP2 cause a glycosylation disorder with autophagic defects.
The Journal of experimental medicine - 4 Dec 2017
Rujano Maria A, Cannata Serio Magda, Panasyuk Ganna, Péanne Romain, Reunert Janine, Rymen Daisy, Hauser Virginie, Park Julien H, Freisinger Peter, Souche Erika, Guida Maria Clara, Maier Esther M, Wada Yoshinao, Jäger Stefanie, Krogan Nevan J, Kretz Oliver, Nobre Susana, Garcia Paula, Quelhas Dulce, Bird Thomas D, Raskind Wendy H, Schwake Michael, Duvet Sandrine, Foulquier Francois, Matthijs Gert, Marquardt Thorsten, Simons Matias
Abstract excerpt
The biogenesis of the multi-subunit vacuolar-type H+-ATPase (V-ATPase) is initiated in the endoplasmic reticulum with the assembly of the proton pore V0, which is controlled by a group of assembly factors. Here, we identify two hemizygous missense mutations in the extracellular domain of the accessory V-ATPase subunit ATP6AP2 (also known as the [pro]renin receptor) responsible for a glycosylation disorder with...
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