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dc.contributor.authorWalvekar, Adhish S-
dc.contributor.authorKadamur, Ganesh-
dc.contributor.authorSreedharan, Sreesa-
dc.date.accessioned2024-04-10T08:30:36Z-
dc.date.available2024-04-10T08:30:36Z-
dc.date.issued2020-
dc.identifier.otherOER000000692vi
dc.identifier.urihttp://dlib.hust.edu.vn/handle/HUST/24343-
dc.descriptionTài liệu này được phát hành theo giấy phép CC-BY-NC-ND 4.0vi
dc.description.abstractMethionine, through S-adenosylmethionine, activates multifaceted growth programs where ribosome biogenesis, carbon metabolism, amino acid and nucleotide biosynthesis are induced. This growth program requires activity of the Gcn4 transcription factor (called ATF4 in mammals), which enables metabolic precursor supply essential for anabolism. Here, we discover how the Gcn4 protein is induced by methionine, despite conditions of high translation and anabolism. This induction mechanism is independent of transcription, as well as the conventional Gcn2/eIF2α mediated increased translation of Gcn4. Instead, when methionine is abundant, Gcn4 ubiqitination and therefore degradation is reduced, due to the decreased phosphorylation of this protein. This Gcn4 stabilization is mediated by the activity of the conserved methyltransferase, Ppm1, which specifically methylates the catalytic subunit of protein phosphatase PP2A when methionine is abundant. This methylation of PP2A shifts the balance of Gcn4 to a dephosphorylated state, which stabilizes the protein. The loss of Ppm1, or PP2A-methylation destabilizes Gcn4 when methionine is abundant, and the Gcn4-dependent anabolic program collapses. These findings reveal a novel signaling and regulatory axis, where methionine directs a conserved methyltransferase Ppm1, via its target phosphatase PP2A, to selectively stabilize Gcn4. Thereby, when methionine is abundant, cells conditionally modify a major phosphatase in order to stabilize a metabolic master-regulator and drive anabolism.vi
dc.description.urihttps://www.biorxiv.org/content/10.1101/2020.05.05.079020v1vi
dc.formatPDFvi
dc.language.isoenvi
dc.publisherBiochemical Journalvi
dc.rightsAttribution-NonCommercial-NoDerivs 3.0 Vietnam*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/vn/*
dc.subjectS-adenosylmethioninevi
dc.subjectThe Gcn4 proteinvi
dc.subject.lccQD405vi
dc.titleMethylated PP2A stabilizes Gcn4 to enable a methionine-induced anabolic programvi
dc.typeJournal articlevi
Appears in Collections:OER - Kỹ thuật hóa học; Công nghệ sinh học - Thực phẩm; Công nghệ môi trường

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