N-Myristoyltransferase 2 Is Regulated by Polyphosphate-Driven Lysine Interactions.

Isabella Martins, Kaia Bailey, Anni Ge, Ethan Belrose, Xiaolong Yang, Zongchao Jia

Abstract read

In one paragraph

Article in Biomolecules, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed

–field-weighted citation impact

1 · What the graph read from it

What it found

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

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3 · Its place in the literature

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0 citing papers in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

6 authors.

Isabella MartinsDepartment of Biomedical and Molecular Sciences, Queen's University, Kingston, ON K7L 3N6, Canada.

Kaia BaileyDepartment of Biomedical and Molecular Sciences, Queen's University, Kingston, ON K7L 3N6, Canada.

Anni GeDepartment of Pathology and Molecular Medicine, Queen's University, Kingston, ON K7L 3N6, Canada.ORCID 0000-0003-2751-9745

Ethan BelroseDepartment of Biomedical and Molecular Sciences, Queen's University, Kingston, ON K7L 3N6, Canada.ORCID 0009-0008-0814-9172

Xiaolong YangDepartment of Pathology and Molecular Medicine, Queen's University, Kingston, ON K7L 3N6, Canada.ORCID 0000-0002-8073-8675

Zongchao JiaDepartment of Biomedical and Molecular Sciences, Queen's University, Kingston, ON K7L 3N6, Canada.ORCID 0000-0002-9322-9394

Funding

Natural Sciences and Engineering Research Council of Canada RGPIN-2024-05181

6 · The paper itself

Abstract

Inorganic polyphosphate (polyP) is a ubiquitous polymer increasingly recognized as a regulator of protein function through lysine polyphosphate modification (KPM), a reversible interaction with lysine-rich protein regions. Although numerous KPM targets have been identified, the functional consequences of polyP binding remain poorly understood. N-myristoyltransferase 2 (NMT2), an essential enzyme that catalyzes protein N-myristoylation and regulates membrane-associated signaling pathways, was previously identified as a candidate KPM target. Here, we investigated the molecular and functional relationship between polyP and NMT2. Using a fluorescence-based coenzyme A release assay, we found that polyP directly down-regulated NMT2 enzymatic activity in a dose-dependent manner, with long-chain polyP (polyP

Indexed as

AcyltransferasesLysinePolyphosphatesHeLa CellsHumansPhosphorylationSignal TransductionAcyltransferasesglycylpeptide N-tetradecanoyltransferaseLysinePolyphosphatesKPMlysine polyphosphate modificationlysine repeatsmyristoylationNMT2phosphorylated Srcpolyphosphate

Identifiers

PMID42650764

DOI10.3390/biom16081096

PMCPMC13510580

What Socratic holds

Textmetadata

Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.