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anti-Human Mahogunin RING Finger Protein 1 Antikörper:
anti-Mouse (Murine) Mahogunin RING Finger Protein 1 Antikörper:
anti-Rat (Rattus) Mahogunin RING Finger Protein 1 Antikörper:
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epletion of MGRN1 activity may hamper physiologically important processes like mitochondrial movement in neuronal processes and intracellular transport of ligands through the endosomal pathway thereby contributing to the pathogenesis of neurodegeneration in certain types of prion diseases
In a heterologous expression system, MC1R-dependent Arrestins B ubiquitination was enhanced by overexpression of MGRN1 and was impaired by siRNA-mediated MGRN1 knockdown thus pointing to MGRN1 as the responsible E3-ligase.
Hypomethylation of CpG sites in RPTOR, MGRN1 and RAPSN in blood is associated with breast cancer.
Regulation of Mfn1 by MGRN1 and the proteasome modulates mitochondrial fusion.
With aging, the neuroprotective e3 ligase MGRN1 relocates from the cytosol to the nucleus of neurons, where it associates with chromatin and potentiates the cellular response to proteotoxic stress. This nuclear shift is due to a proteasome impairment dependent increase of a monoubiquitinated form of MGRN1.
Catalytic inactivation of MGRN1 results in elevated levels of GP78 and a consequential increase in the initiation of mitophagy.
Mahogunin-mediated alpha-tubulin ubiquitination via noncanonical K6 linkage regulates microtubule stability and mitotic spindle orientation.
data suggest that MGRN1 selectively targets misfolded proteins for degradation and may exhibit viable therapeutic potential for the treatment of spongiform neurodegeneration
It therefore seems probable that the role of MGRN1 in the adrenal relates to the trafficking and/or degradation of the melanocortin 2 receptor.
a role for Mahogunin in a proteasome-independent ubiquitylation pathway: TSG101 is a specific Mahogunin substrate
Study shows that both (Ctm)PrP and cyPrP can interact with and disrupt the function of Mahogunin (Mgrn), a cytosolic ubiquitin ligase whose loss causes spongiform neurodegeneration.
Mgrn1 can negatively regulate signaling through the Hedgehog pathway by reducing cell-surface and ciliary levels of Smoothened, an oncoprotein that transmits the Hedgehog signal across the membrane.
Findings suggest that mahogunin ring finger-1 contributes to the clearance of toxic mutant copper-zinc superoxide dismutase inclusions likely through autophagic pathway.
This study indicates the mahogunin deficiency results in the infertility of male mice, disruption of hormones secretion and impaired active progressive motility.
ATRN also has no effect on prion disease onset or progression and discuss possible mechanisms that could cause vacuolation of the central nervous system in Mgrn1 and Atrn null mutant mice
pigment-type switching likely requires MGRN1's ubiquitin ligase activity but not its ability to bind TSG101 or NEDD4.
Levels of the Mahogunin Ring Finger 1 E3 ubiquitin ligase do not influence prion disease.
the md and mg mutations rescue the A(y) phenotypes by a primarily cAMP-independent mechanism promoting trafficking of MC4R and likely MC1R away from the lysosome toward the cell surface.
positional cloning of mahoganoid, encoding a novel 494-amino acid protein containing a C3HC4 RING (really interesting new gene) domain that may function as an E3 ubiquitin ligase
a null mutation for mahoganoid causes a similar age-dependent neuropathology that includes many features of prion diseases but without accumulation of protease-resistant prion protein
Mahoganoid mutation (Mgrn1md) on insulin sensitivity suggests that Mgrn1md may be increasing insulin sensitivity via the hypothalamic melanocortin-3 receptor pathway.
Mgrn1 mutant embryos show abnormal expression of asymmetrically expressed genes involved in LR patterning.
Our results indicate that reduced levels of MGRN1 cause the pigmentation phenotypes of Mgrn1 mutant mice and that there are no significant differences in the function of the four MGRN1 isoforms in pigment-type switching.
Loss of E3 ubiquitin ligase MGRN1 in mutant mice causes neurodegeneration via accumulation of its substrates.
data show that different Mgrn1 isoforms are not functionally equivalent in vivo and that the presence of only isoform I or III is sufficient for normal development, pigmentation, and neuronal integrity
study shows ASIP-MC1R signaling includes a cAMP-independent pathway through attractin and mahogunin, while the known cAMP-dependent component requires neither attractin nor mahogunin
Mahogunin (MGRN1) is a C3HC4 RING-containing protein with E3 ubiquitin ligase activity in vitro.
E3 ubiquitin-protein ligase MGRN1
, RING finger protein 156
, mahogunin RING finger protein 1
, mahogunin, ring finger 1
, probable E3 ubiquitin-protein ligase MGRN1
, mahogunin ring finger protein 1