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The protein encoded by PTPRN2 is a member of the protein tyrosine phosphatase (PTP) family. Zusätzlich bieten wir Ihnen Protein tyrosine Phosphatase, Receptor Type, N Polypeptide 2 Antikörper (67) und und viele weitere Produktgruppen zu diesem Protein an.
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Copy-number variations are enriched for PTPRN2 and other neurodevelopmental genes in children with developmental coordination disorder.
Haplotype-dependent allele-specific methylation of PTPRN2 gene is associated with neurological disorders.
Reduction in plasma membrane PI(4,5)P2 abundance by PTPRN2 and PLCbeta1 releases the PI(4,5)P2-binding protein cofilin from its inactive membrane-associated state into the cytoplasm where it mediates actin turnover dynamics.
Data indicate the X-ray structure of the mature ectodomain of mature ectodomain of phogrin/IA-2beta (PTPRN2) (ME phogrin) at pH 7.4 and 4.6.
ProPTPRN2 elicited these effects through direct interaction with TRAF2.
While PTPRN2 shares sequence similarity with protein tyrosine phosphatases, this study in rat suggests that this protein instead functions as a membrane bound phosphatidylinositol phosphatase.
The findings in this patient raise the possibility that PTPRN2 may be active during early development of the human brainstem and that its overexpression may cause bilateral Duane retraction syndrome as occurs in patients with homozygous HOXA1 mutations.
IA-2beta is involved in insulin secretion, but despite its importance as a major autoantigen in human type 1 diabetes, it is not required for the development of diabetes in NOD mice.
In mice IA-2beta expressed exclusively in dense core secretory vesicles (DCV) and with fractions rich in synaptic vesicles (SV) of neuroendocrine cells of brain and impairment of conditioned learning.
Relative to wildtype mice, IRS2 levels in phogrin-knockout mice islets decreased by 44%. When phogrin was silenced by shRNA in pancreatic beta-cell lines, glucose-induced insulin signaling led to proteasomal degradation of IRS2 via a negative feedback mechanism.
The deletion of IA-2 and IA-2beta results in multiple pathophysiologic changes and represents a unique in vivo model for studying the effect of hormone and neurotransmitter reduction on known and still unrecognized targets.
Data show that miRNAs are involved in regulating the expression of the major type 1 diabetes (T1D) autoantigens IA-2, IA-2beta, and GAD65 enzyme.
Membrane-proximal ectodomain of phogrin was produced as a recombinant protein and characterized' results showed that it is a properly folded monomeric domain.
phogrin is recycled in Min6 beta-cells
analysis of a tyrosine-targeting motif for endocytosis and recycling of the dense-core vesicle membrane protein phogrin
experiments show that the dense core vesicle proteins IA-2 and IA-2beta, alone or in combination, are involved in insulin secretion, but neither alone nor in combination are they required for the development of diabetes in NOD mice
IA-2beta, but not IA-2, is induced by ghrelin and inhibits glucose-stimulated insulin secretion
IA-2 and IA-2beta are dispensable for exocytosis of insulin granules, but are probably more important for cargo loading and/or stability of dense core vesicles
Phogrin and IA-2 function as essential regulators of autocrine insulin action in pancreatic beta-cells.
deletion of IA-2 and IA-2beta, structural proteins of secretory vesicles and modulators of neuroendocrine secretion, has a profound effect on the circadian system.
The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP possesses an extracellular region, a single transmembrane region, and a single intracellular catalytic domain, and thus represents a receptor-type PTP. The catalytic domain of this PTP is most closely related to PTPRN/IA-2beta. This PTP and PTPRN are both found to be major autoantigens associated with insulin-dependent diabetes mellitus. Three alternatively spliced transcript variants of this gene, which encode distinct proteins, have been reported.
IAR/receptor-like protein-tyrosine phosphatase
, islet cell autoantigen-related protein
, protein tyrosine phosphatase receptor pi
, receptor-type tyrosine-protein phosphatase N2
, tyrosine phosphatase IA-2 beta
, IA-2 beta
, PTP IA-2beta
, protein tyrosine phosphatase-NP
, PTP NE-6
, protein tyrosine phosphatase receptor-type N polypeptide 2
, protein tyrosine phosphatase, receptor-type, N polypeptide 2