Foulquier, François Legrand, Dominique
Published in
Biochimica et biophysica acta. General subjects
About half of the eukaryotic proteins bind biometals that participate in their structure and functions in virtually all physiological processes, including glycosylation. After reviewing the biological roles and transport mechanisms of calcium, magnesium, manganese, zinc and cobalt acting as cofactors of the metalloproteins involved in sugar metabol...
Murali, Pavitra Johnson, Blake P. Lu, Zhongpeng Climer, Leslie Scott, Danielle A. Foulquier, Francois Oprea-Ilies, Gabriela Lupashin, Vladimir Drake, Richard R. Abbott, Karen L.
...
Published in
Oncotarget
The TMEM165 gene encodes for a multiple pass membrane protein localized in the Golgi that has been linked to congenital disorders of glycosylation. The TMEM165 protein is a putative ion transporter that regulates H+/Ca++/Mn++ homeostasis and pH in the Golgi. Previously, we identified TMEM165 as a potential biomarker for breast carcinoma in a glycop...
Thines, Louise Stribny, Jiri Morsomme, Pierre
Published in
Microbial cell (Graz, Austria)
The Uncharacterized Protein Family 0016 (UPF0016) gathers poorly studied membrane proteins well conserved through evolution that possess one or two copies of the consensus motif Glu-x-Gly-Asp-(Arg/Lys)-(Ser/Thr). Members are found in many eukaryotes, bacteria and archaea. The interest for this protein family arose in 2012 when its human member TMEM...
Lebredonchel, Elodie Houdou, Marine Hoffmann, Hans-Heinrich Kondratska, Kateryna Krzewinski, Marie-Ange Vicogne, Dorothée Rice, Charles M Klein, André Foulquier, François
Published in
The Biochemical journal
TMEM165 was highlighted in 2012 as the first member of the Uncharacterized Protein Family 0016 (UPF0016) related to human glycosylation diseases. Defects in TMEM165 are associated with strong Golgi glycosylation abnormalities. Our previous work has shown that TMEM165 rapidly degrades with supraphysiological manganese supplementation. In this paper,...
Vicogne, Dorothée Houdou, Marine Garat, Anne Climer, Leslie Lupashin, Vladimir Morelle, Willy Foulquier, François
Published in
Journal of inherited metabolic disease
TMEM165 is involved in a rare genetic human disease named TMEM165-CDG (congenital disorders of glycosylation). It is Golgi localized, highly conserved through evolution and belongs to the uncharacterized protein family 0016 (UPF0016). The use of isogenic TMEM165 KO HEK cells was crucial in deciphering the function of TMEM165 in Golgi manganese home...
Lebredonchel, Elodie Houdou, Marine Potelle, Sven de Bettignies, Geoffroy Schulz, Céline Krzewinski Recchi, Marie-Ange Lupashin, Vladimir Legrand, Dominique Klein, André Foulquier, François
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Published in
Biochimie
Since 2012, the interest for TMEM165 increased due to its implication in a rare genetic human disease named TMEM165-CDG (Congenital Disorder(s) of Glycosylation). TMEM165 is a Golgi localized protein, highly conserved through evolution and belonging to the uncharacterized protein family 0016 (UPF0016). Although the precise function of TMEM165 in gl...
Hoecker, Natalie Leister, Dario Schneider, Anja
Published in
Plant signaling & behavior
PHOTOSYNTHESIS AFFECTED MUTANT71 (PAM71) is an integral thylakoid membrane protein that functions in manganese uptake into the lumen. Manganese is needed in the thylakoid lumen to build up the inorganic Mn4CaO5 cluster, the catalytic center for water oxidation, and is hence indispensable for oxygen evolution. A recent study revealed that PAM71 is w...
Schulte Althoff, S Grüneberg, M Reunert, J Park, J H Rust, S Mühlhausen, C Wada, Y Santer, R Marquardt, T
Published in
JIMD reports
Congenital disorders of glycosylation form a rapidly growing group of inherited metabolic diseases. As glycosylation affects proteins all over the organism, a mutation in a single gene leads to a multisystemic disorder. We describe a patient with TMEM165-CDG with facial dysmorphism, nephrotic syndrome, cardiac defects, enlarged cerebral ventricles,...
Reinhardt, Timothy A. Lippolis, John D. Sacco, Randy E.
Published in
Biochemical and Biophysical Research Communications
Plasma membrane Ca2+-ATPase 2 (PMCA2) knockout mice showed that ∼60% of calcium in milk is transported across the mammary cells apical membrane by PMCA2. The remaining milk calcium is thought to arrive via the secretory pathway through the actions of secretory pathway Ca2+-ATPase’s 1 and/or 2 (SPCA1 and 2). However, another secretory pathway calciu...
