Amino acids and KLHL22 do not activate mTORC1 via DEPDC5 degradation
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F25%3A00605347" target="_blank" >RIV/61388963:_____/25:00605347 - isvavai.cz</a>
Result on the web
<a href="https://doi.org/10.1038/s41586-024-07974-0" target="_blank" >https://doi.org/10.1038/s41586-024-07974-0</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1038/s41586-024-07974-0" target="_blank" >10.1038/s41586-024-07974-0</a>
Alternative languages
Result language
angličtina
Original language name
Amino acids and KLHL22 do not activate mTORC1 via DEPDC5 degradation
Original language description
Activation of the mechanistic target of rapamycin complex 1 (mTORC1) requires its nutrient-dependent recruitment to the surface of the lysosome, a process that is controlled by several multiprotein complexes, including GATOR1, a negative regulator of mTORC1 signalling. Recently, Chen et al. suggested that KLHL22-dependent ubiquitylation and proteasomal degradation of the GATOR1 component DEPDC5 mediates mTORC1 activation by amino acids. Here we report that the antibody central to the conclusions of Chen et al. neither sensitively nor specifically detects endogenous DEPDC5, and we determine, using validated antibodies and endogenously tagged cell lines, that the stability of DEPDC5 is insensitive to amino acid availability, proteasome activity and KLHL22 loss of function. These results call into question the conclusions of Chen et al. and indicate that alternative mechanisms convey nutrient availability to mTORC1.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology
Result continuities
Project
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Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2025
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Nature
ISSN
0028-0836
e-ISSN
1476-4687
Volume of the periodical
637
Issue of the periodical within the volume
8045
Country of publishing house
GB - UNITED KINGDOM
Number of pages
4
Pages from-to
"E11"-"E14"
UT code for WoS article
001410545800001
EID of the result in the Scopus database
2-s2.0-85215071300