PPP1R10

Last update 08 May 2025

Basic Info

Synonyms

CAT53, FB19, MHC class I region proline-rich protein CAT53

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Introduction

Scaffold protein which mediates the formation of the PTW/PP1 phosphatase complex by providing a binding platform to each component of the complex. The PTW/PP1 phosphatase complex plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. Mediates interaction of WDR82 and PPP1CA. Inhibitor of PPP1CA and PPP1CC phosphatase activities. Has inhibitory activity on PPP1CA only when phosphorylated. Binds to mRNA, single-stranded DNA (ssDNA), poly(A) and poly(G) homopolymers (By similarity).

100 Clinical Results associated with PPP1R10

100 Translational Medicine associated with PPP1R10

0 Patents (Medical) associated with PPP1R10

243

Literatures (Medical) associated with PPP1R10

01 May 2025·International Journal of Biological Macromolecules

A functional role for myostatin in muscle hyperplasia and hypertrophy revealed by comparative transcriptomics in Yesso scallop Patinopecten yessoensis

Article

Author: Zhou, Liqing ; Zheng, Yanxin ; Wu, Biao ; Yang, Hongsu ; Sun, Xiujun ; Liu, Zhihong ; Yu, Tao ; Liu, Shufang

Elucidating the molecular regulatory mechanisms underlying muscle growth and development is of profound significance in aquaculture. Yesso scallop is a cold-water bivalve of considerable economic importance, having its primary edible component of adductor muscle. In this study, comparative transcriptomics and histological analysis at different sampling times after Myostatin (MSTN) interference were performed to identify the potential candidate genes potentially involved in muscle growth and development. The comparative transcriptomics revealed that growth factors and cytokines, extracellular matrix proteins and ubiquitin-proteasome system are potentially involved in muscle hypertrophy and hyperplasia. After MSTN interference, striated adductor muscle displays significant muscle hypertrophy (51.77 % increase on day 7 and 59.83 % increase on day 21) and muscle hyperplasia (59.36 % increase on day 7 and 61.83 % increase on day 21). WGCNA identifies the key darkolivegreen module, which may play crucial roles in muscle hyperplasia and hypertrophy within the striated muscle of the scallop. Five key transcription factors (zf-CCCH, zf-C2H2, PPP1R10, LRRFIP2, and Gon4) are identified by analyzing the co-expression patterns of core genes within the module. These findings will aid in understanding the regulatory mechanisms of muscle growth in scallops and provide a basis for genetic improvement in shellfish aquaculture.

01 May 2025·Cell Reports

PP1/PNUTS phosphatase binds the restrictor complex and stimulates RNA Pol II transcription termination

Article

Author: Mouilleron, Stephane ; Fong, Nova ; Fedoryshchak, Roman ; Saviola, Anthony J ; Bentley, David L ; Larson, Keira Y ; Treisman, Richard ; Hansen, Kirk C ; Erickson, Benjamin ; Sheridan, Ryan

The restrictor ZC3H4/WDR82 terminates antisense transcription from bidirectional promoters, but its mechanism is poorly understood. We report that ZC3H4/WDR82 immunoprecipitates with PP1 phosphatase and its nuclear targeting subunit, PP1 phosphatase nuclear targeting subunit (PNUTS), which binds to WDR82. AlphaFold predicts a complex of PP1/PNUTS with the restrictor where both PNUTS and ZC3H4 contact WDR82. A substrate trap, PP1^H66K-PNUTS, comprising inactive PP1 fused to the PNUTS C terminus, antagonizes restrictor-mediated termination, whereas PP1^WT-PNUTS has less of an effect, suggesting that phosphatase activity is required for termination. One PP1/PNUTS substrate implicated in termination by the restrictor is RNA polymerase II (RNA Pol II) CTD Ser5-P. PP1^H66K-PNUTS induces Ser5-P hyperphosphorylation at 5' ends, presumably by inhibiting dephosphorylation. NET-seq analysis suggests that CTD Ser5 dephosphorylation would promote termination by increasing RNA Pol II pausing. Both inhibition of termination and CTD hyperphosphorylation require the WDR82 binding domain of PP1^H66K-PNUTS, which mediates restrictor binding. In summary, the PP1/PNUTS phosphatase associated with the restrictor via WDR82 promotes efficient transcription termination.

01 Mar 2025·Molecular Cell

Pcf11/Spt5 condensates stall RNA polymerase II to facilitate termination and piRNA-guided heterochromatin formation

Article

Author: Wang, Yuan ; Wang, Sheng ; Luo, Xiu ; Wang, Zhenning ; Xv, Xiangjin ; Deng, Lijun ; Liu, Chao ; Li, Pilong ; Chen, Fei Xavier ; Li, Yu ; Zhang, Tianyu ; Li, Wei ; Liu, Weiwei ; Gao, Pu ; Lu, Xiaohua ; Lin, Chengqi ; Zhang, Yadi ; Ji, Jinyao ; Goh, Wee Siong Sho ; Li, Dong ; Chen, Chunlai ; Miao, Na ; Dang, Yunkun ; Luo, Zhuojuan ; Guan, Li ; Yu, Yang ; Liu, Xiaojun ; Wang, Ming ; Wu, Xueming ; Zhou, Wenhao ; Qiao, Zhenghao ; Ouyang, Xuan

The PIWI-interacting RNA (piRNA) pathway plays a crucial role in protecting animal germ cells by repressing transposons. However, the mechanism of piRNA-guided heterochromatin formation and its relationship to transcriptional termination remains elusive. Through RNA interference screening, we discovered Pcf11 and PNUTS as essential for piRNA-guided silencing in Drosophila germ line. Enforced tethering of Pcf11 leads to co-transcriptional repression and RNA polymerase II (RNA Pol II) stalling, and both are dependent on an α-helical region of Pcf11 capable of forming condensates. An intrinsically disordered region can substitute for the α-helical region of Pcf11 in its silencing capacity and support animal development, arguing for a causal relationship between phase separation and Pcf11's function. Pcf11 stalls RNA Pol II by preferentially forming condensates with the unphosphorylated Spt5, promoted by the PP1/PNUTS phosphatase during termination. We propose that Pcf11/Spt5 condensates control termination by decelerating polymerase elongation, a property exploited by piRNAs to silence transposons and initiate RNA-mediated heterochromatin formation.

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PPP1R10

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