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

Mucolipin 3

TRPML3, MCOLN3, V a, mucolipin-3
This gene encodes one of members of the mucolipin cation channel proteins. Mutation studies of the highly similar protein in mice have shown that the protein is found in cochlea hair cells, and mutant mice show early-onset hearing loss and balance problems. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Nov 2011] (from NCBI)
Top mentioned proteins: TRPML2, HAIR, MG2, CAN, TRPV4
Papers on TRPML3
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.
A TRP Channel Senses Lysosome Neutralization by Pathogens to Trigger Their Expulsion.
Abraham et al., Durham, United States. In Cell, Jul 2015
This change is detected by mucolipin TRP channel 3 (TRPML3), a transient receptor potential cation channel localized to lysosomes.
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.
Mucolipin co-deficiency causes accelerated endolysosomal vacuolation of enterocytes and failure-to-thrive from birth to weaning.
García-Añoveros et al., Chicago, United States. In Plos Genet, 2014
We found that mouse enterocytes before weaning express high levels of two endolysosomal cation channels, mucolipins 3 and 1 -products of Trpml3 and Trpml1 genes; moreover neonatal enterocytes of mice lacking both mucolipins (Trpml3-/-;Trpml1-/-) vacuolated pathologically within hours of birth and remained so until weaning.
Differential mechanisms of action of the mucolipin synthetic agonist, ML-SA1, on insect TRPML and mammalian TRPML1.
Zhu et al., Guangzhou, China. In Cell Calcium, 2014
On the other hand, constitutive activation of TRPML by a mutation that mimics the varitint-waddler (Va) mutation of mouse TRPML3 rendered the insect channel sensitive to activation by ML-SA1 alone.
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
Using TRPML A487P, which mimics the varitint-waddler (Va) mutant of mouse TRPML3 with constitutive whole-cell currents, we show that TRPML is biphasically regulated by extracytosolic pH, with an optimal pH about 0.6 pH unit higher than that of human TRPML1.
The Ca2+ channel TRPML3 specifically interacts with the mammalian ATG8 homologue GATE16 to regulate autophagy.
Kim et al., Suwŏn, South Korea. In Biochem Biophys Res Commun, 2014
TRPML3 is a Ca(2+) permeable cation channel expressed in multiple intracellular compartments.
TRPs in hearing.
Göpfert et al., Göttingen, Germany. In Handb Exp Pharmacol, 2013
In vertebrates, TRPs are unlikely to form auditory transduction channels, yet most TRPs are expressed in inner ear tissues, and mutations in TRPN1, TRPVA1, TRPML3, TRPV4, and TRPC3/TRPC6 have been implicated in inner ear function.
Wahl-Schott et al., München, Germany. In Handb Exp Pharmacol, 2013
TRPML3 belongs to the MCOLN (TRPML) subfamily of transient receptor potential (TRP) channels comprising three genes in mammals.
TRPML2 and mucolipin evolution.
Wiwatpanit et al., Chicago, United States. In Handb Exp Pharmacol, 2013
This contrasts with the ubiquitous expression of TRPML1 and the limited but diverse expression of TRPML3 and clearly suggests a specialized role for TRPML2 in immunity.
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).
A novel ion channel formed by interaction of TRPML3 with TRPV5.
Heller et al., Palo Alto, United States. In Plos One, 2012
TRPML3 and TRPV5 are members of the mucolipin (TRPML) and TRPV subfamilies of transient receptor potential (TRP) cation channels.
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
Negatively charged amino acids in the extracellular loops of TRPML3 may interfere with the observed sodium inhibition.
Identification of Selective Agonists of the Transient Receptor Potential Channels 3 (TRPML3)
Hodder et al., Bethesda, United States. In Unknown Journal, 2012
When mutated, the Transient Receptor Potential Channels 3 (TRPML3) ion channel causes deafness and pigmentation defects.
Expression and vesicular localization of mouse Trpml3 in stria vascularis, hair cells, and vomeronasal and olfactory receptor neurons.
García-Añoveros et al., Chicago, United States. In J Comp Neurol, 2011
Results describe the expression and subcellular distribution of TRPML3 in the inner ear as well as in other sensory organs.
Mucolipin-3 regulates luminal calcium, acidification, and membrane fusion in the endosomal pathway.
Puertollano et al., Bethesda, United States. In J Biol Chem, 2011
prominent role for MCOLN3 in regulating Ca(2+) homeostasis at the endosomal pathway
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.
Genetic inactivation of Trpml3 does not lead to hearing and vestibular impairment in mice.
Heller et al., Stanford, United States. In Plos One, 2009
Trpml3 inactivation does not lead to hearing and vestibular impairment in mice
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