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@ARTICLE{Kopp:295902,
author = {J. Kopp and D. Jahn and G. Vogt and A. Psoma and E.
Ratto$^*$ and W. Morelle and N. Stelzer and I. Hausser and
A. Hoffmann and M. R. de Los Santos and L. A. Koch and B.
Fischer-Zirnsak and C. Thiel and W. Palm$^*$ and D.
Meierhofer and G. van den Bogaart and F. Foulquier and A.
Meinhardt and U. Kornak},
title = {{G}olgi p{H} elevation due to loss of {V}-{ATP}ase subunit
{V}0a2 function correlates with tissue-specific
glycosylation changes and globozoospermia.},
journal = {Cellular and molecular life sciences},
volume = {82},
number = {1},
issn = {1420-682X},
address = {Cham (ZG)},
publisher = {Springer International Publishing AG},
reportid = {DKFZ-2024-02716},
pages = {4},
year = {2025},
abstract = {Loss-of-function variants in ATP6V0A2, encoding the trans
Golgi V-ATPase subunit V0a2, cause wrinkly skin syndrome
(WSS), a connective tissue disorder with glycosylation
defects and aberrant cortical neuron migration. We used
knock-out (Atp6v0a2-/-) and knock-in (Atp6v0a2RQ/RQ) mice
harboring the R755Q missense mutation selectively abolishing
V0a2-mediated proton transport to investigate the WSS
pathomechanism. Homozygous mutants from both strains
displayed a reduction of growth, dermis thickness, and
elastic fiber formation compatible with WSS. A hitherto
unrecognized male infertility due to globozoospermia was
evident in both mouse lines with impaired Golgi-derived
acrosome formation and abolished mucin-type O-glycosylation
in spermatids. Atp6v0a2-/- mutants showed enhanced
fucosylation and glycosaminoglycan modification, but reduced
levels of glycanated decorin and sialylation in skin and/or
fibroblasts, which were absent or milder in Atp6v0a2RQ/RQ.
Atp6v0a2RQ/RQ mutants displayed more abnormal migration of
cortical neurons, correlating with seizures and a reduced
O-mannosylation of α-dystroglycan. While anterograde
transport within the secretory pathway was similarly delayed
in both mutants the brefeldin A-induced retrograde fusion of
Golgi membranes with the endoplasmic reticulum was less
impaired in Atp6v0a2RQ/RQ. Measurement of the pH in the
trans Golgi compartment revealed a shift from 5.80 in
wildtype to 6.52 in Atp6v0a2-/- and 6.25 in Atp6v0a2RQ/RQ.
Our findings suggest that altered O-glycosylation is more
relevant for the WSS pathomechanism than N-glycosylation and
leads to a secondary dystroglycanopathy. Most phenotypic and
cellular properties correlate with the different degrees of
trans Golgi pH elevation in both mutants underlining the
fundamental relevance of pH regulation in the secretory
pathway.},
keywords = {Animals / Male / Glycosylation / Golgi Apparatus:
metabolism / Mice / Vacuolar Proton-Translocating ATPases:
metabolism / Vacuolar Proton-Translocating ATPases: genetics
/ Hydrogen-Ion Concentration / Mice, Knockout /
Teratozoospermia: metabolism / Teratozoospermia: genetics /
Teratozoospermia: pathology / Mice, Inbred C57BL / Humans /
Fibroblasts: metabolism / Cutis laxa (Other) /
Globozoospermia (Other) / Glycosylation (Other) / Golgi
(Other) / Neuronal migration (Other) / Spermiogenesis
(Other) / V-ATPase (Other) / Vesicular trafficking (Other) /
pH-regulation (Other) / Vacuolar Proton-Translocating
ATPases (NLM Chemicals)},
cin = {A330},
ddc = {610},
cid = {I:(DE-He78)A330-20160331},
pnm = {311 - Zellbiologie und Tumorbiologie (POF4-311)},
pid = {G:(DE-HGF)POF4-311},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:39680136},
doi = {10.1007/s00018-024-05506-7},
url = {https://inrepo02.dkfz.de/record/295902},
}