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

Melanin-concentrating hormone receptor 1

dynamin 2, MCHR1, melanin-concentrating hormone receptor 1, MCH receptor
The protein encoded by this gene, a member of the G protein-coupled receptor family 1, is an integral plasma membrane protein which binds melanin-concentrating hormone. The encoded protein can inhibit cAMP accumulation and stimulate intracellular calcium flux, and is probably involved in the neuronal regulation of food consumption. Although structurally similar to somatostatin receptors, this protein does not seem to bind somatostatin. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Dynamin I, V1a, CAN, Neuropeptide, HAD
Papers on dynamin 2
Possible regulation of caveolar endocytosis and flattening by phosphorylation of F-BAR domain protein PACSIN2/Syndapin II.
Suetsugu et al., Helsinki, Finland. In Bioarchitecture, Feb 2016
PACSIN2 is thought to function in the scission and stabilization of caveolae, through binding to dynamin-2 and EHD2, respectively.
Discovery of (3-(4-(2-oxa-6-azaspiro[3.3]heptan-6-ylmethyl)phenoxy)azetidin-1-yl)(5-(4-methoxyphenyl)-1,3,4-oxadiazol-2-yl)methanone (AZD1979), a melanin concentrating hormone receptor 1 (MCHr1) antagonist with favourable physicochemical properties.
Hogner et al., In J Med Chem, Feb 2016
UNASSIGNED: A novel series of melanin concentrating hormone receptor 1 (MCHr1) antagonists were the starting point for a drug discovery program that culminated in the discovery of 103 (AZD1979).
Melanin-concentrating Hormone Receptor 1 Antagonists lacking an aliphatic amine: Synthesis and Structure-Activity Relationships of Novel 1-(Imidazo[1,2-a]pyridin-6-yl)pyridin-2(1H)-one Derivatives.
Maekawa et al., In J Med Chem, Feb 2016
UNASSIGNED: Aiming to discover melanin-concentrating hormone receptor 1 (MCHR1) antagonists with improved safety profiles, we hypothesized that the aliphatic amine employed in most antagonists reported to date could be removed if the bicyclic motif of the compound scaffold interacted with Asp123 and/or Tyr272 of MCHR1.
Impaired dynamin 2 function leads to increased AP-1 transcriptional activity through the JNK/c-Jun pathway.
Miaczynska et al., Warsaw, Poland. In Cell Signal, Jan 2016
Here we show that inhibition of dynamin 2 (Dyn2), a major regulator of endocytic internalization, strongly stimulates the AP-1 pathway.
MCH levels in the CSF, brain preproMCH and MCHR1 gene expression during paradoxical sleep deprivation, sleep rebound and chronic sleep restriction.
D'Almeida et al., São Paulo, Brazil. In Peptides, Dec 2015
With the hypothesis that the MCHergic system function would be modified by the time of the day as well as by disruptions of the sleep-wake cycle, we quantified in rats the concentration of MCH in the cerebrospinal fluid (CSF), the expression of the MCH precursor (Pmch) gene in the hypothalamus, and the expression of the MCH receptor 1 (Mchr1) gene in the frontal cortex and hippocampus.
Mitochondrial dynamics and inherited peripheral nerve diseases.
Piscosquito et al., Milano, Italy. In Neurosci Lett, Jul 2015
Indeed, mitochondrial transport involves directly or indirectly components of the kinesin superfamily (KIF5A, KIF1A, KIF1B), responsible of anterograde transport, and of the dynein complex and related proteins (DYNC1H1, dynactin, dynamin-2), implicated in retrograde flow.
Novel MCH1 receptor antagonists: a patent review.
Löfberg et al., Mölndal, Sweden. In Expert Opin Ther Pat, Feb 2015
Large efforts have been invested in discovery programs to identify novel MCH1 receptor (MCHR1) antagonists.
Melanin-Concentrating Hormone (MCH): Role in REM Sleep and Depression.
Monti et al., Montevideo, Uruguay. In Front Neurosci, 2014
In the DR, this effect is prevented by the systemic administration of antidepressant drugs (either fluoxetine or nortriptyline) and blocked by the intra-DR microinjection of a specific MCH receptor antagonist.
Adult-onset autosomal dominant spastic paraplegia linked to a GTPase-effector domain mutation of dynamin 2.
Toro et al., Bethesda, United States. In Bmc Neurol, 2014
Molecular analyses uncovered a missense c.2155C > T, p.R719W mutation in the highly conserved GTP-effector domain of dynamin 2. The mutant DNM2 co-segregated with HSP and affected endocytosis when expressed in HeLa cells.
Pathogenic mechanisms in centronuclear myopathies.
Gautel et al., London, United Kingdom. In Front Aging Neurosci, 2013
The most common forms of congenital myopathies with central nuclei have been attributed to X-linked recessive mutations in the MTM1 gene encoding myotubularin ("X-linked myotubular myopathy"), autosomal-dominant mutations in the DNM2 gene encoding dynamin-2 and the BIN1 gene encoding amphiphysin-2 (also named bridging integrator-1, BIN1, or SH3P9), and autosomal-recessive mutations in BIN1, the RYR1 gene encoding the skeletal muscle ryanodine receptor, and the TTN gene encoding titin.
Clinicopathological features of centronuclear myopathy in Japanese populations harboring mutations in dynamin 2.
Nishino et al., Kodaira, Japan. In Clin Neurol Neurosurg, 2012
clinicopathological features of DNM2 centronuclear myopathy are rather homogeneous and can be distinguished from the features of non-DNM2 centronuclear myopathy
Caveolin-1 and dynamin-2 are essential for removal of the complement C5b-9 complex via endocytosis.
Fishelson et al., Tel Aviv-Yafo, Israel. In J Biol Chem, 2012
Caveolin-1 and dynamin-2 are essential for removal of the complement C5b-9 complex via endocytosis.
Mutation spectrum in the large GTPase dynamin 2, and genotype-phenotype correlation in autosomal dominant centronuclear myopathy.
Laporte et al., Illkirch-Graffenstaden, France. In Hum Mutat, 2012
Defects in membrane trafficking due to DNM2 mutations potentially represent a common pathological mechanism in CNM and CMT.
Structure of a yeast Dyn2-Nup159 complex and molecular basis for dynein light chain-nuclear pore interaction.
Slep et al., Chapel Hill, United States. In J Biol Chem, 2012
Data indicate that the comparative binding of Dyn2 to two Nup159 target sites shows similar affinities (18 and 13 muM), but divergent thermal binding modes.
Dynamin 2 mutations in Charcot-Marie-Tooth neuropathy highlight the importance of clathrin-mediated endocytosis in myelination.
Suter et al., Zürich, Switzerland. In Brain, 2012
This study suggested that myelination is strictly dependent on Dnm2 and clathrin-mediated endocytosis function.
The blood-testis barrier and its implications for male contraception.
Mruk et al., New York City, United States. In Pharmacol Rev, 2012
Studies have demonstrated that some unlikely partners, namely adhesion protein complexes (e.g., occludin-ZO-1, N-cadherin-β-catenin, claudin-5-ZO-1), steroids (e.g., testosterone, estradiol-17β), nonreceptor protein kinases (e.g., focal adhesion kinase, c-Src, c-Yes), polarity proteins (e.g., PAR6, Cdc42, 14-3-3), endocytic vesicle proteins (e.g., clathrin, caveolin, dynamin 2), and actin regulatory proteins (e.g., Eps8, Arp2/3 complex), are working together, apparently under the overall influence of cytokines (e.g., transforming growth factor-β3, tumor necrosis factor-α, interleukin-1α).
Crystal structure of nucleotide-free dynamin.
Daumke et al., Berlin, Germany. In Nature, 2011
This intricate domain interaction rationalizes a number of disease-related mutations in dynamin 2 and suggests a structural model for the mechanochemical coupling that reconciles previous models of dynamin function.
Rapid and efficient clathrin-mediated endocytosis revealed in genome-edited mammalian cells.
Drubin et al., Berkeley, United States. In Nat Cell Biol, 2011
To analyse endocytic dynamics in mammalian cells in which endogenous protein stoichiometry is preserved, we targeted zinc finger nucleases (ZFNs) to the clathrin light chain A and dynamin-2 genomic loci and generated cell lines expressing fluorescent protein fusions from each locus.
Mutations in amphiphysin 2 (BIN1) disrupt interaction with dynamin 2 and cause autosomal recessive centronuclear myopathy.
Laporte et al., Illkirch-Graffenstaden, France. In Nat Genet, 2007
The severe neonatal X-linked form (myotubular myopathy) is due to mutations in the phosphoinositide phosphatase myotubularin (MTM1), whereas mutations in dynamin 2 (DNM2) have been found in some autosomal dominant cases.
Mutations in dynamin 2 cause dominant centronuclear myopathy.
Guicheney et al., Paris, France. In Nat Genet, 2005
Missense mutations in dynamin 2 is associated with dominant centronuclear myopathy
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