SYMPK

更新于：2025-05-07

基本信息

别名

Pta1、SPK、SYM

+ [3]

简介

Scaffold protein that functions as a component of a multimolecular complex involved in histone mRNA 3'-end processing. Specific component of the tight junction (TJ) plaque, but might not be an exclusively junctional component. May have a house-keeping rule. Is involved in pre-mRNA polyadenylation. Enhances SSU72 phosphatase activity.

关联

100 项与 SYMPK 相关的临床结果

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100 项与 SYMPK 相关的转化医学

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0 项与 SYMPK 相关的专利（医药）

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213

项与 SYMPK 相关的文献（医药）

2025-02-01·American Journal of Physiology-Heart and Circulatory Physiology

Prenatal dexamethasone programs autonomic dysregulation in female rats

Article

作者: Martinez, Monique ; Hale, Taben M ; Sharma, Arpan ; Madhavpeddi, Lakshmi ; Alvarez, Jared ; Tobet, Stuart A ; Hu, Chengcheng

Pharmacological antagonists are used to characterize the nature of the autonomic dysregulation induced in female offspring exposed to dexamethasone, in utero. The female offspring of dams injected with dexamethasone in late gestation show a reduction in vulnerability to parasympathetic blockade and an increase in responses to acute restraint stress even in the presence of sympathetic blockade. This suggests that late gestation dexamethasone disrupts the normal development of the autonomic function in females, shifting sympathovagal balance.

2023-11-01·Open Biology

Molecular details of the CPSF73-CPSF100 C-terminal heterodimer and interaction with Symplekin

Article

作者: Fribourg, Sébastien ; Talenton, Vincent ; Thore, Stéphane ; Mackereth, Cameron D ; Raoelijaona, Finaritra

Eukaryotic pre-mRNA is processed by a large multiprotein complex to accurately cleave the 3′ end, and to catalyse the addition of the poly(A) tail. Within this cleavage and polyadenylation specificity factor (CPSF) machinery, the CPSF73/CPSF3 endonuclease subunit directly contacts both CPSF100/CPSF2 and the scaffold protein Symplekin to form a subcomplex known as the core cleavage complex or mammalian cleavage factor. Here we have taken advantage of a stable CPSF73-CPSF100 minimal heterodimer from Encephalitozoon cuniculi to determine the solution structure formed by the first and second C-terminal domain (CTD1 and CTD2) of both proteins. We find a large number of contacts between both proteins in the complex, and notably in the region between CTD1 and CTD2. A similarity is also observed between CTD2 and the TATA-box binding protein (TBP) domains. Separately, we have determined the structure of the terminal CTD3 domain of CPSF73, which also belongs to the TBP domain family and is connected by a flexible linker to the rest of CPSF73. Biochemical assays demonstrate a key role for the CTD3 of CPSF73 in binding Symplekin, and structural models of the trimeric complex from other species allow for comparative analysis and support an overall conserved architecture.

2023-11-01·Genes & Development

Restrictor synergizes with Symplekin and PNUTS to terminate extragenic transcription

Article

作者: Polletti, Sara ; Natoli, Gioacchino ; Marenda, Mattia ; Russo, Marta ; Mandana, Gaurav Madappa ; Borriero, Carolina ; Cuomo, Alessandro ; Rodighiero, Simona ; Piccolo, Viviana ; Bedin, Fabio ; Michieletto, Davide ; Polizzese, Danilo ; Prosperini, Elena

Transcription termination pathways mitigate the detrimental consequences of unscheduled promiscuous initiation occurring at hundreds of thousands of genomiccis-regulatory elements. The Restrictor complex, composed of the Pol II-interacting protein WDR82 and the RNA-binding protein ZC3H4, suppresses processive transcription at thousands of extragenic sites in mammalian genomes. Restrictor-driven termination does not involve nascent RNA cleavage, and its interplay with other termination machineries is unclear. Here we show that efficient termination at Restrictor-controlled extragenic transcription units involves the recruitment of the protein phosphatase 1 (PP1) regulatory subunit PNUTS, a negative regulator of the SPT5 elongation factor, and Symplekin, a protein associated with RNA cleavage complexes but also involved in cleavage-independent and phosphatase-dependent termination of noncoding RNAs in yeast. PNUTS and Symplekin act synergistically with, but independently from, Restrictor to dampen processive extragenic transcription. Moreover, the presence of limiting nuclear levels of Symplekin imposes a competition for its recruitment among multiple transcription termination machineries, resulting in mutual regulatory interactions. Hence, by synergizing with Restrictor, Symplekin and PNUTS enable efficient termination of processive, long-range extragenic transcription.

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