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The protein encoded by ENSA belongs to a highly conserved cAMP-regulated phosphoprotein (ARPP) family.
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The extended S phase in Ensa-depleted cells is completely rescued by the overexpression of Treslin.
Taken together our results suggest a hierarchy of phosphatases coordinating Greatwall (Montrer MASTL Kits ELISA), Ensa/ARPP19 and Cdk (Montrer CDK4 Kits ELISA) substrate dephosphorylation during mitotic exit.
Overexpressed ENSA suppresses tumor growth in an established hepatic cell line whereas hypermethylated ENSA might help maintain liver cancer initiating cells.
The considerably decreased alpha-endosulfine could result in the continuous opening of K(ATP) channels and the subsequent decrease of neurotransmitters release associated with cognition in Down Syndrome.
We mapped ENSA in silico to chromosome 1q21 near a confirmed type 2 diabetes susceptibility locus, and derived the genomic structure of four exons and three introns.
The ENSA gene on 1q21 produces several alternatively spliced transcripts, and is located within a region linked with T2DM in diverse populations including the Pima Indians
description of how Gwl activation results in PP2A inhibition; Arpp19 and alpha-Endosulfine when phosphorylated by Gwl associate with and inhibit PP2A promoting mitotic entry; endogenous Arpp19 responsible for PP2A inhibition at mitotic entry in egg extracts
inhibition of PP2A-B55delta results from Ensa, that is phosphorylated in mitosis by the protein kinase Greatwall; this converts Ensa into specific inhibitor of PP2A-B55delta; this pathway represents a previously unknown element in mitosis control
The protein encoded by this gene belongs to a highly conserved cAMP-regulated phosphoprotein (ARPP) family. This protein was identified as an endogenous ligand for the sulfonylurea receptor, ABCC8/SUR1. ABCC8 is the regulatory subunit of the ATP-sensitive potassium (KATP) channel, which is located on the plasma membrane of pancreatic beta cells and plays a key role in the control of insulin release from pancreatic beta cells. This protein is thought to be an endogenous regulator of KATP channels. In vitro studies have demonstrated that this protein modulates insulin secretion through the interaction with KATP channel, and this gene has been proposed as a candidate gene for type 2 diabetes. At least eight alternatively spliced transcript variants encoding distinct isoforms have been observed.