α-Phenylalanyl tRNA synthetase competes with Notch signaling through its N-terminal domain.


Journal

PLoS genetics
ISSN: 1553-7404
Titre abrégé: PLoS Genet
Pays: United States
ID NLM: 101239074

Informations de publication

Date de publication:
04 2022
Historique:
received: 04 09 2021
accepted: 04 04 2022
revised: 11 05 2022
pubmed: 30 4 2022
medline: 18 5 2022
entrez: 29 4 2022
Statut: epublish

Résumé

The alpha subunit of the cytoplasmic Phenylalanyl tRNA synthetase (α-PheRS, FARSA in humans) displays cell growth and proliferation activities and its elevated levels can induce cell fate changes and tumor-like phenotypes that are neither dependent on the canonical function of charging tRNAPhe with phenylalanine nor on stimulating general translation. In intestinal stem cells of Drosophila midguts, α-PheRS levels are naturally slightly elevated and human FARSA mRNA levels are elevated in multiple cancers. In the Drosophila midgut model, elevated α-PheRS levels caused the accumulation of many additional proliferating cells resembling intestinal stem cells (ISCs) and enteroblasts (EBs). This phenotype partially resembles the tumor-like phenotype described as Notch RNAi phenotype for the same cells. Genetic interactions between α-PheRS and Notch suggest that their activities neutralize each other and that elevated α-PheRS levels attenuate Notch signaling when Notch induces differentiation into enterocytes, type II neuroblast stem cell proliferation, or transcription of a Notch reporter. These non-canonical functions all map to the N-terminal part of α-PheRS which accumulates naturally in the intestine. This truncated version of α-PheRS (α-S) also localizes to nuclei and displays weak sequence similarity to the Notch intracellular domain (NICD), suggesting that α-S might compete with the NICD for binding to a common target. Supporting this hypothesis, the tryptophan (W) residue reported to be key for the interaction between the NICD and the Su(H) BTD domain is not only conserved in α-PheRS and α-S, but also essential for attenuating Notch signaling.

Identifiants

pubmed: 35486661
doi: 10.1371/journal.pgen.1010185
pii: PGENETICS-D-21-01190
pmc: PMC9094542
doi:

Substances chimiques

RNA, Transfer, Phe 0
Phenylalanine 47E5O17Y3R
Phenylalanine-tRNA Ligase EC 6.1.1.20

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

e1010185

Déclaration de conflit d'intérêts

The authors have declared that no competing interests exist.

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Auteurs

Manh Tin Ho (MT)

Institute of Cell Biology, University of Bern, Bern, Switzerland.

Jiongming Lu (J)

Institute of Cell Biology, University of Bern, Bern, Switzerland.

Paula Vazquez-Pianzola (P)

Institute of Cell Biology, University of Bern, Bern, Switzerland.

Beat Suter (B)

Institute of Cell Biology, University of Bern, Bern, Switzerland.

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Classifications MeSH