Key result
PP1cβ T197Q mutation alters PP1 holoenzyme composition and increases Plk1 phosphorylation, revealing isoform-specific preferences.
Why the study?
To systematically characterize PP1c isoform-specific interactions and define the determinants of MYPT1-PP1cβ specificity.
Population
Cells expressing PP1c isoforms (PP1cα, PP1cβ, and PP1cγ) and genome-edited cells
Comparison
PP1cβ-PP1cγ chimeras, PP1cβ point mutations, and PP1cβ T197Q mutation vs wild-type
Design
Preclinical mass spectrometry and genome-editing study
Authors
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Isoform-specific PP1 interactomes mapped; extends molecular catalog but leaves open cardiovascular functional roles.
A single amino acid change (T197Q) in PP1cβ alters holoenzyme composition and phosphorylation signaling, providing insight into how clinical variants impact PP1 biology.
Poimenidou et al. (2026) studied this question. PP1cβ T197Q mutation vs. Wild-type PP1cβ was evaluated on PP1 holoenzyme composition and phosphorylation signaling. A single amino acid change (PP1cβ T197Q) altered PP1 holoenzyme composition and increased phosphorylation of the Plk1 activation loop, demonstrating determinants of PP1c isoform-specific preference.
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