ReviewBiology2026
Methyl-Lysine-Dependent Control of Protein Lifetime Through Lysine-Node Crosstalk and Reader-Coupled Degradation.
Review in Biology, 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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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.
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1 author.
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Abstract
The half-life of proteins is determined by the "information" carried within specific regions of the protein. Lysine methylation is an emerging post-translational modification that can act at the decision node. In contrast to the charge-neutralizing effects of lysine acylation, methylation maintains the positive charge of the lysine residue, allowing for the presence of multiple methylation states (Kme1/2/3). This property enables the "reading" of the methylation state by "methyl lysine readers." Although the methyl group is chemically stable, the methylation is enzymatically reversible by lysine demethylases. In this review, we conceptualize the "methyl lysine" as an "information"-containing "signal" at the decision node. The "information" is composed of the interplay between the "competition" among the same site modifications, the "methylation-dependent degron" or "methyl degrons," the "steric blockade" or "methyl shields," and the "changes in spatial routing" or "methyl routing cues." In this review, we discuss the emerging evidence within these three types of functional methyl lysine.
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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 OpenQuestion graph.