期刊
AMERICAN JOURNAL OF HUMAN GENETICS
卷 91, 期 1, 页码 15-26出版社
CELL PRESS
DOI: 10.1016/j.ajhg.2012.05.002
关键词
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资金
- FWO (Fonds voor Wetenschappelijk Onderzoek, Vlaanderen, Belgium) [G.0553.08]
- AFM (Association Francaise contre les Myopathies, France) [12540]
- PEPS-CNRS (Projets Exploratoires/Premier Soutien du Centre National de la Recherche Scientifique, France)
- Marie Curie Reintegration Grant (VTG-CDG)
- Agence Nationale Recherche Jeune Chercheur
- F.R.S.-FNRS (Fonds de la Recherche Scientifique, Wallonie)
- la Communaute Francaise de Wallonie-Bruxelles
- la Loterie Nationale (Belgium)
- Interuniversity Attraction Poles Program of the Belgian Science Policy (Belgium) [6/05]
- Rocket Fund
- European Commission [LSHM-CT.2005-512131]
- Korber Stiftung
- [R01DK55615]
Protein glycosylation is a complex process that depends not only on the activities of several enzymes and transporters but also on a subtle balance between vesicular Golgi trafficking, compartmental pH, and ion homeostasis. Through a combination of autozygosity mapping and expression analysis in two siblings with an abnormal serum-transferrin isoelectric focusing test (type 2) and a peculiar skeletal phenotype with epiphyseal, metaphyseal, and diaphyseal dysplasia, we identified TMEM165 (also named TPARL) as a gene involved in congenital disorders of glycosylation (CDG). The affected individuals are homozygous for a deep. intronic splice mutation in TMEM165. In our cohort of unsolved CDG-II cases, we found another individual with the same mutation and two unrelated individuals with missense mutations in TMEM165. TMEM165 encodes a putative transmembrane 324 amino acid protein whose cellular functions are unknown. Using a siRNA strategy, we showed that TMEM165 deficiency causes Golgi glycosylation defects in HEK cells.
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