An evolutionary mechanism to assimilate new nutrient sensors into the mTORC1 pathway
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F24%3A00585114" target="_blank" >RIV/61388963:_____/24:00585114 - isvavai.cz</a>
Result on the web
<a href="https://doi.org/10.1038/s41467-024-46680-3" target="_blank" >https://doi.org/10.1038/s41467-024-46680-3</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1038/s41467-024-46680-3" target="_blank" >10.1038/s41467-024-46680-3</a>
Alternative languages
Result language
angličtina
Original language name
An evolutionary mechanism to assimilate new nutrient sensors into the mTORC1 pathway
Original language description
Animals sense and respond to nutrient availability in their environments, a task coordinated in part by the mTOR complex 1 (mTORC1) pathway. mTORC1 regulates growth in response to nutrients and, in mammals, senses specific amino acids through specialized sensors that bind the GATOR1/2 signaling hub. Given that animals can occupy diverse niches, we hypothesized that the pathway might evolve distinct sensors in different metazoan phyla. Whether such customization occurs, and how the mTORC1 pathway might capture new inputs, is unknown. Here, we identify the Drosophila melanogaster protein Unmet expectations (CG11596) as a species-restricted methionine sensor that directly binds the fly GATOR2 complex in a fashion antagonized by S-adenosylmethionine (SAM). We find that in Dipterans GATOR2 rapidly evolved the capacity to bind Unmet and to thereby repurpose a previously independent methyltransferase as a SAM sensor. Thus, the modular architecture of the mTORC1 pathway allows it to co-opt preexisting enzymes to expand its nutrient sensing capabilities, revealing a mechanism for conferring evolvability on an otherwise conserved system.
Czech name
—
Czech description
—
Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
—
OECD FORD branch
10608 - Biochemistry and molecular biology
Result continuities
Project
—
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2024
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Nature Communications
ISSN
2041-1723
e-ISSN
2041-1723
Volume of the periodical
15
Issue of the periodical within the volume
March
Country of publishing house
US - UNITED STATES
Number of pages
16
Pages from-to
2517
UT code for WoS article
001190797000001
EID of the result in the Scopus database
2-s2.0-85188350203