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SYMPK encodes a nuclear protein that functions in the regulation of polyadenylation and promotes gene expression. Additionally we are shipping Symplekin Antibodies (47) and Symplekin Kits (2) and many more products for this protein.
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Authors propose a model in which the core cleavage complex formation is mediated by CPSF73 (show CPSF3 Proteins), CPSF100 (show CPSF2 Proteins), and Symplekin C-termini, and the N-terminal region of Symplekin facilitates cotranscriptional 3' end processing of histone mRNAs.
This localization depends on the RNA binding protein ypsilon schachtel. CPSF-73 (show CPSF3 Proteins) and a number of mRNAs are localized at this same site, suggesting that Symplekin participates in cytoplasmic polyadenylation at tricellular junctions.
Together, these data support the conclusion that the Symplekin HEAT domain serves as a scaffold for protein-protein interactions essential to the mRNA maturation process.
CPSF2 (show CPSF2 Proteins) and SYMPK, are RBFOX2 (show RBM9 Proteins) cofactors for both inclusion and exclusion of internal exons.
Symplekin interacts and co-localizes with both MOZ and MLL (show MLL Proteins) in immature hematopoietic cells. Its inhibition leads to a decrease of the HOXA9 (show HOXA9 Proteins) protein level but not of Hoxa9 (show HOXA9 Proteins) mRNA.
Symplekin expression regulates the assembly of tight junctions, thus helps to maintain the integrity of the epithelial monolayer and cellular polarity.
crystal structure at 2.4 A resolution of the amino-terminal domain (residues 30-340) of human symplekin in a ternary complex with the Pol II carboxy-terminal domain (CTD) Ser (show SIGLEC1 Proteins) 5 phosphatase Ssu72 (show SSU72 Proteins) and a CTD Ser (show SIGLEC1 Proteins) 5 phosphopeptide
Symplekin supports faithful mitosis by contributing to the formation of a bipolar spindle apparatus. Depletion of symplekin attenuates microtubule polymerization as well as expression of the critical microtubule polymerization protein CKAP5 (TOGp).
Data show that claudin-2 (show CLDN2 Proteins) expression was reduced following symplekin down-regulation, and siRNA-mediated claudin-2 (show CLDN2 Proteins) down-regulation increased the transepithelial resistance and decreased cyclin D1 (show CCND1 Proteins) expression and ZONAB (show CSDA Proteins) nuclear localization.
symplekin has a role in HSF1 (show HSF1 Proteins) modulation of Hsp70 (show HSP70 Proteins) mRNA polyadenylation
The decreased expression of symplekin may be an early step in the transformation of hepatocytes, whereas alteration of the expression of adherens junctions and desmosomes may indicate more serious changes.
The symplekin/ZONAB (show CSDA Proteins) complex inhibits intestinal cell differentiation by the repression of AML1/Runx1 (show RUNX1 Proteins).
In Xenopus, symplekin interacts with the CPSF complex and the regulatory protein CPEB, (show CPEB1 Proteins)and is re (show CPSF3 Proteins)quired for polyadenylation of CPE-containing RNA
Here, we identify a new factor essential for polyadenylation, namely, symplekin, a CPEB and CPSF (show CPSF2 Proteins) binding protein that serves as a scaffold upon which regulatory factors are assembled
This gene encodes a nuclear protein that functions in the regulation of polyadenylation and promotes gene expression. The protein forms a high-molecular weight complex with components of the polyadenylation machinery. It is thought to serve as a scaffold for recruiting regulatory factors to the polyadenylation complex. It also participates in 3'-end maturation of histone mRNAs, which do not undergo polyadenylation. The protein also localizes to the cytoplasmic plaques of tight junctions in some cell types.
, hepatocyte nuclear factor 3 gamma