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Mucolipin 2

TRPML2, MCOLN2, mucolipin-2
Mucolipins constitute a family of cation channel proteins with homology to the transient receptor potential superfamily. In mammals, the mucolipin family includes 3 members, MCOLN1 (MIM 605248), MCOLN2, and MCOLN3 (MIM 607400), that exhibit a common 6-membrane-spanning topology. Homologs of mammalian mucolipins exist in Drosophila and C. elegans. Mutations in the human MCOLN1 gene cause mucolipodosis IV (MIM 262650) (Karacsonyi et al., 2007 [PubMed 17662026]).[supplied by OMIM, Sep 2009] (from NCBI)
Top mentioned proteins: TRPML3, MG2, CAN, HAIR, OUT
Papers on TRPML2
The mucolipin-2 (TRPML2) ion channel: a tissue-specific protein crucial to normal cell function.
Valadez et al., Fullerton, United States. In Pflugers Arch, Feb 2016
The TRPML protein subfamily consists of three members, TRPML1, TRPML2, and TRPML3, which are encoded by MCOLN1, MCOLN2, and MCOLN3 genes, respectively.
Novel Role of TRPML2 in the Regulation of the Innate Immune Response.
Puertollano et al., Bethesda, United States. In J Immunol, Dec 2015
Although TRPML1 and TRPML3 have been well characterized, the cellular function of TRPML2 has remained elusive.
The role of TRPMLs in endolysosomal trafficking and function.
Zhu et al., Houston, United States. In Cell Calcium, Jul 2015
Whereas loss-of-function mutations in human TRPML1 were first identified as being causative for the lysosomal storage disease, Mucolipidosis type IV, most mammals also express two other TRPML isoforms called TRPML2 and TRPML3.
Role of the transient receptor potential (TRP) channel gene expressions and TRP melastatin (TRPM) channel gene polymorphisms in obesity-related metabolic syndrome.
Demiryürek et al., Gaziantep, Turkey. In Eur Rev Med Pharmacol Sci, Apr 2015
Although there were marked decreases in TRPC1, TRPC3, TRPM2, TRPM5, TRPV4, TRPV5, TRPV6, MCOLN2 (TRPML2), and MCOLN3 (TRPML3) gene expressions, an augmentation was noted in TRPC6 gene expression.
PAX5 is the transcriptional activator of mucolipin-2 (MCOLN2) gene.
Cuajungco et al., Fullerton, United States. In Gene, Feb 2015
Specifically, heterologous expression of PAX5 in HEK-293 cells significantly increased endogenous MCOLN2 transcript and TRPML2 protein levels, while RNA interference targeting endogenous PAX5 reduced its effect.
Integrated methylome and transcriptome analysis reveals novel regulatory elements in pediatric acute lymphoblastic leukemia.
Taylor et al., Columbia, United States. In Epigenetics, 2014
These genes include potential epi-driver genes, such as SYNE1, PTPRS, PAWR, HDAC9, RGCC, MCOLN2, LYN, TRAF3, FLT1, and MELK, which may provide a selective advantage to leukemic cells.
Drosophila TRPML forms PI(3,5)P2-activated cation channels in both endolysosomes and plasma membrane.
Zhu et al., Guangzhou, China. In J Biol Chem, 2014
These features resemble more closely to mammalian TRPML1 than TRPML2 and TRPML3, but with some obvious differences.
TRPML2 and mucolipin evolution.
Wiwatpanit et al., Chicago, United States. In Handb Exp Pharmacol, 2013
The TRPML2 protein, encoded by the Mcoln2 gene, is one of the three mucolipins (TRPML1-3), a subset of the TRP superfamily of ion channels.
Characterization and expression analysis of mcoln1.1 and mcoln1.2, the putative zebrafish co-orthologs of the gene responsible for human mucolipidosis type IV.
Borsani et al., Brescia, Italy. In Int J Dev Biol, 2012
TRPML1 belongs to a transient receptor potential channels (TRP) subfamily, which in mammals includes two other members: mucolipin-2 (TRPML2) and mucolipin-3 (TRPML3).
Concurrent gene signatures for han chinese breast cancers.
Chuang et al., Taipei, Taiwan. In Plos One, 2012
A breast cancer risk predictive model was built based on the first supervised principal component from 16 genes (RCAN3, MCOLN2, DENND2D, RWDD3, ZMYM6, CAPZA1, GPR18, WARS2, TRIM45, SCRN1, CSNK1E, HBXIP, CSDE1, MRPL20, IKZF1, and COL20A1), and distinct survival patterns were observed between the high- and low-risk groups from the combined dataset of 408 microarrays.
Constitutive activity of TRPML2 and TRPML3 channels versus activation by low extracellular sodium and small molecules.
Heller et al., München, Germany. In J Biol Chem, 2012
TRPML2 is activated by lowering the extracellular sodium concentration as well as by a subset of small chemical compounds that were previously identified as activators of TRPML3.
TRPML: transporters of metals in lysosomes essential for cell survival?
Muallem et al., Pittsburgh, United States. In Cell Calcium, 2011
Recent evidence suggests that TRPML1 is involved in Fe(2+), Ca(2+) and Zn(2+) transport across the lysosomal membrane, ascribing novel physiological roles to this ion channel, and perhaps to its relatives TRPML2 and TRPML3 and illuminating poorly understood aspects of lysosomal function.
A diverse range of gene products are effectors of the type I interferon antiviral response.
Rice et al., New York City, United States. In Nature, 2011
Several ISGs, including ADAR, FAM46C, LY6E and MCOLN2, enhanced the replication of certain viruses, highlighting another layer of complexity in the highly pleiotropic type I interferon system.
TRPML2 and the evolution of mucolipins.
García-Añoveros et al., Chicago, United States. In Adv Exp Med Biol, 2010
TRPML2, the polypeptide product of the gene Trpml2 (aka Mcoln2), is a member of the TRPML or mucolipin branch of the TRP super family of ion channels.
Heteromultimeric TRPML channel assemblies play a crucial role in the regulation of cell viability models and starvation-induced autophagy.
Bach et al., Jerusalem, Israel. In J Cell Sci, 2010
TRPML 1, 2 and 3 assemblies regulated cell viability and starvation-induced autophagy.
Functional multimerization of mucolipin channel proteins.
Slaugenhaupt et al., Boston, United States. In J Cell Physiol, 2010
Data show that TRPMLs form distinct functional channel complexes.
Constitutive activity of the human TRPML2 channel induces cell degeneration.
Minke et al., Jerusalem, Israel. In J Biol Chem, 2010
constitutively active h-TRPML2 leads to cell death by causing Ca(2+) overload
Campaign to Identify Agonists of Transient Receptor Potential Channels 3 and 2 (TRPML3 & TRPML2)
Hodder et al., Bethesda, United States. In Unknown Journal, 2009
The two probes reported here [SID24801657 (ML123) and SID24787221ML122)] exhibit potent EC50 values against TRPML3 (EC50 values of 0.873 μM and 1.43 μM), and activate TRPML2 (54.5%ACT and 23.5% ACT).
The tissue-specific expression of TRPML2 (MCOLN-2) gene is influenced by the presence of TRPML1.
Cuajungco et al., Fullerton, United States. In Pflugers Arch, 2009
TRPML1 appears to play a novel role in the tissue-specific transcriptional regulation of TRPML2.
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