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Protein phosphatase 1 regulatory subunit 7 (PPP1R7) is a regulatory protein that binds to the catalytic subunit of protein phosphatase 1 (PP1), a serine/threonine phosphatase essential for many cellular dephosphorylation events[1][5]. PPP1R7 is required for the completion of mitosis and proper targeting of PP1 to mitotic kinetochores, and plays a pivotal role in regulating PP1 substrate specificity by acting as part of the PP1 interactome[1][2]. In the heart, PPP1R7 is one of the strongest PP1 interactors and is essential for normal cardiac function; its altered binding to PP1 during heart failure progression suggests an adaptive or compensatory mechanism[2]. PPP1R7 belongs to ciliary and flagellar integrity-associated protein families and features leucine-rich repeat domains[3][5]. Diseases associated with PPP1R7 dysfunction include chromosomal deletion syndromes and rare skeletal diseases, with broader potential involvements in cancer, cardiovascular, and metabolic disease as part of PP1-regulated pathways[1][4]. Its central regulatory role and adaptation in disease highlight its interest as a therapeutic target, but no directly interacting drugs are currently described, and therapeutic interference may pose significant safety challenges[2][4].
Modulation of dephosphorylation in PP1 holoenzyme complexes. Alters substrate specificity and localization of PP1. Acts as a "competitive molecular sponge" for PP1 catalytic subunit, sequestering PP1 and affecting phosphorylation of downstream targets.
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