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@ARTICLE{Pal:298906,
author = {J. Pal and M. Riester and A. Ganner and A. Ghosh$^*$ and S.
Dhamija$^*$ and D. Mookherjee and C. Voss and I. J. Frew and
F. Kotsis and E. Neumann-Haefelin and A. Spang and S.
Diederichs$^*$},
title = {{N}onstop mutations cause loss of renal tumor suppressor
proteins {VHL} and {BAP}1 and affect multiple stages of
protein translation.},
journal = {Science advances},
volume = {11},
number = {7},
issn = {2375-2548},
address = {Washington, DC [u.a.]},
publisher = {Assoc.},
reportid = {DKFZ-2025-00345},
pages = {eadr6375},
year = {2025},
abstract = {Nonstop extension or stop-loss mutations lead to the
extension of a protein at its carboxyl terminus. Recently,
nonstop mutations in the tumor suppressor SMAD Family Member
4 (SMAD4) have been discovered to lead to proteasomal SMAD4
degradation. However, this mutation type has not been
studied in other cancer genes. Here, we explore somatic
nonstop mutations in the tumor suppressor genes BRCA1
Associated Protein 1 (BAP1) and Von Hippel-Lindau (VHL)
enriched in renal cell carcinoma. For BAP1, nonstop
mutations generate an extremely long extension. Instead of
proteasomal degradation, the extension decreases translation
and depletes BAP1 messenger RNA from heavy polysomes. For
VHL, the short extension leads to proteasomal degradation.
Unexpectedly, the mutation alters the selection of the
translational start site shifting VHL isoforms. We identify
germline VHL nonstop mutations in patients leading to the
early onset of severe disease manifestations. In summary,
nonstop extension mutations inhibit the expression of renal
tumor suppressor genes with pleiotropic effects on
translation and protein stability.},
keywords = {Von Hippel-Lindau Tumor Suppressor Protein: genetics / Von
Hippel-Lindau Tumor Suppressor Protein: metabolism / Tumor
Suppressor Proteins: genetics / Tumor Suppressor Proteins:
metabolism / Humans / Ubiquitin Thiolesterase: genetics /
Ubiquitin Thiolesterase: metabolism / Protein Biosynthesis /
Kidney Neoplasms: genetics / Kidney Neoplasms: metabolism /
Kidney Neoplasms: pathology / Mutation / Carcinoma, Renal
Cell: genetics / Carcinoma, Renal Cell: metabolism /
Carcinoma, Renal Cell: pathology / Proteasome Endopeptidase
Complex: metabolism / Proteasome Endopeptidase Complex:
genetics / Proteolysis / BAP1 protein, human (NLM Chemicals)
/ Von Hippel-Lindau Tumor Suppressor Protein (NLM Chemicals)
/ Tumor Suppressor Proteins (NLM Chemicals) / Ubiquitin
Thiolesterase (NLM Chemicals) / VHL protein, human (NLM
Chemicals) / Proteasome Endopeptidase Complex (NLM
Chemicals)},
cin = {FR01},
ddc = {500},
cid = {I:(DE-He78)FR01-20160331},
pnm = {899 - ohne Topic (POF4-899)},
pid = {G:(DE-HGF)POF4-899},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:39937911},
doi = {10.1126/sciadv.adr6375},
url = {https://inrepo02.dkfz.de/record/298906},
}