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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Mahogunin, ring finger 1

Mgrn1, mahogunin ring finger-1
Mahogunin (MGRN1) is a C3HC4 RING-containing protein with E3 ubiquitin ligase activity in vitro.[supplied by OMIM, Apr 2004] (from NCBI)
Top mentioned proteins: Ubiquitin, FINGER1, V1a, attractin, MC1R
Papers on Mgrn1
Mahogunin ring finger 1 confers cytoprotection against mutant SOD1 aggresomes and is defective in an ALS mouse model.
New
Mishra et al., Jodhpur, India. In Neurobiol Dis, Feb 2016
Here, we found that the Mahogunin ring finger-1 (MGRN1) E3 ubiquitin ligase, which catalyzes mono-ubiquitination to the substrate, was dysregulated in the cellular and mouse models of ALS and that it preferentially interacted with various mutant forms of SOD1.
Ubiquitin mediated regulation of the E3 ligase GP78 by Mahogunin in trans affects mitochondrial homeostasis.
New
Chakrabarti et al., Calcutta, India. In J Cell Sci, Feb 2016
This study elucidates a novel interaction of the cytosolic E3 ligase, MGRN1 with the ER ubiquitin E3 ligase, GP78.
Mahogunin Ring Finger-1 (MGRN1), a Multifaceted Ubiquitin Ligase: Recent Unraveling of Neurobiological Mechanisms.
New
Mishra et al., Jodhpur, India. In Mol Neurobiol, Sep 2015
Mahogunin Ring Finger-1 (MGRN1), an E3 ubiquitin ligase of the Really Interesting New Gene (RING) finger family, plays a pivotal role in many biological and cellular mechanisms.
Ubiquitin in regulation of spindle apparatus and its positioning: implications in development and disease.
Review
New
Chakrabarti et al., Calcutta, India. In Biochem Cell Biol, Aug 2015
Some of the ubiquitin ligases regulating these proteins include PARK2, BRCA1/BARD1, MGRN1, SMURF2, and SIAH1; these play a pivotal role in the correct positioning of the spindle apparatus.
Regulation of neuronal survival and morphology by the E3 ubiquitin ligase RNF157.
New
Stegmüller et al., Göttingen, Germany. In Cell Death Differ, Apr 2015
RNF157 is a homolog of the E3 ligase mahogunin ring finger-1, which has been previously implicated in spongiform neurodegeneration.
Mahogunin regulates fusion between amphisomes/MVBs and lysosomes via ubiquitination of TSG101.
Chakrabarti et al., Calcutta, India. In Cell Death Dis, 2014
Aberrant metabolic forms of the prion protein (PrP), membrane-associated (Ctm)PrP and cytosolic (cyPrP) interact with the cytosolic ubiquitin E3 ligase, Mahogunin Ring Finger-1 (MGRN1) and affect lysosomes.
Mahogunin ring finger 1 suppresses misfolded polyglutamine aggregation and cytotoxicity.
Mishra et al., Jodhpur, India. In Biochim Biophys Acta, 2014
MGRN1 co-immunoprecipitates with expanded-polyglutamine huntingtin and ataxin-3 proteins.
Mahogunin-mediated α-tubulin ubiquitination via noncanonical K6 linkage regulates microtubule stability and mitotic spindle orientation.
Chakrabarti et al., Calcutta, India. In Cell Death Dis, 2013
Mahogunin ring finger-1 (MGRN1) is a cytosolic ubiquitin ligase whose disruption or interaction with some isoforms of cytosolically exposed prion protein leads to spongiform neurodegeneration and also lack of which results in reduced embryonic viability due to mispatterning of the left-right (LR) axis during development.
Functional conservation between mammalian MGRN1 and plant LOG2 ubiquitin ligases.
Pilot et al., Davis, United States. In Febs Lett, 2013
Plant LOSS OF GDU 2 (LOG2) and Mammalian Mahogunin Ring Finger 1 (MGRN1) proteins are RING-type E3 ligases sharing similarity N-terminal to the RING domain.
RML prions act through Mahogunin and Attractin-independent pathways.
Carlson et al., Great Falls, United States. In Prion, 2013
Mahogunin ring finger-1 (Mgrn1) and Attractin (Atrn) null mutant mice accumulate vacuoles throughout the brain that appear very similar to those associated with prion disease, but they do not accumulate the protease-resistant scrapie form of the prion protein or become sick.
Mahogunin ring finger-1 (MGRN1) suppresses chaperone-associated misfolded protein aggregation and toxicity.
Mishra et al., Jodhpur, India. In Sci Rep, 2012
Lack of the mahogunin ring finger-1 (MGRN1) E3 ubiquitin ligase in mice causes the development of age-dependent spongiform neurodegeneration.
Levels of the Mahogunin Ring Finger 1 E3 ubiquitin ligase do not influence prion disease.
Gunn et al., Great Falls, United States. In Plos One, 2012
Mice lacking the Mahogunin Ring Finger 1 (MGRN1) E3 ubiquitin ligase develop spongiform encephalopathy by 9 months of age but do not become ill.
The E3 ubiquitin ligase Mahogunin ubiquitinates the melanocortin 2 receptor.
GeneRIF
Clark et al., London, United Kingdom. In Endocrinology, 2011
It therefore seems probable that the role of MGRN1 in the adrenal relates to the trafficking and/or degradation of the melanocortin 2 receptor.
Mahoganoid and mahogany mutations rectify the obesity of the yellow mouse by effects on endosomal traffic of MC4R protein.
GeneRIF
Leibel et al., New York City, United States. In J Biol Chem, 2011
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.
Agouti protein, mahogunin, and attractin in pheomelanogenesis and melanoblast-like alteration of melanocytes: a cAMP-independent pathway.
GeneRIF
Bennett et al., London, United Kingdom. In Pigment Cell Melanoma Res, 2009
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
Transgenic analysis of the physiological functions of Mahogunin Ring Finger-1 isoforms.
GeneRIF
Gunn et al., Ithaca, United States. In Genesis, 2009
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
Functional depletion of mahogunin by cytosolically exposed prion protein contributes to neurodegeneration.
Impact
GeneRIF
Hegde et al., Bethesda, United States. In Cell, 2009
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.
The ubiquitin-proteasome system in spongiform degenerative disorders.
Review
Chin et al., Atlanta, United States. In Biochim Biophys Acta, 2008
The link between aberrant ubiquitination and spongiform neurodegeneration has been strengthened by the discovery that a null mutation in the E3 ubiquitin-protein ligase mahogunin ring finger-1 (Mgrn1) causes an autosomal recessively inherited form of spongiform neurodegeneration in animals.
Biology of epidermal and hair pigmentation in cattle: a mini-review.
Review
Hwang et al., Ch'ŏnan, South Korea. In Vet Dermatol, 2007
The switching between the syntheses of melanin components depends on several genes like melanocortin-1receptor gene (MC1r) - also known as melanocyte-stimulating hormone receptor gene (MSHr)-, agouti (A), attractin (Atrn) and mahogunin (Mgrn1).
Accessory proteins for melanocortin signaling: attractin and mahogunin.
Review
Barsh et al., Stanford, United States. In Ann N Y Acad Sci, 2003
We have recently determined that the gene mutated in mahoganoid, which is also known as Mahogunin (Mgrn1), encodes an E3 ubiquitin ligase.
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