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Polyclonal MCOLN1 Primary Antibody for WB - ABIN540401
Venkatachalam, Hofmann, Montell: Lysosomal localization of TRPML3 depends on TRPML2 and the mucolipidosis-associated protein TRPML1. in The Journal of biological chemistry 2006
study characterized mcoln1.1 and mcoln1.2, the putative co-orthologs of human MCOLN1 gene
the structures of human TRPML1 at pH 5.0 with PtdIns(3,5)P2, PtdIns(4,5)P2, or ML-SA1 and PtdIns(3,5)P2, revealing a unique lipid-binding site.
stimulation of TRPML1 elevates cytoplasmic calcium levels in retinal pigmented epithelial cells, but this response is reduced by lysosomal accumulation.
reactive oxygen species sensor localized on the lysosomal membrane that orchestrates autophagy-dependent negative-feedback program to mitigate oxidative stress in the cell
two electron cryo-microscopy structures of full-length human TRPML1: a 3.72-A apo structure at pH 7.0 in the closed state, and a 3.49-A agonist-bound structure at pH 6.0 in an open state
These results reveal that mTOR is a new type of calmodulin-dependent kinase, and TRPML1, lysosomal calcium and calmodulin play essential regulatory roles in the mTORC1 signaling pathway.
TRPML1 supports both Ca(2+) release and Ca(2+) entry.
These data suggest that lysosomal adenosine accumulation impairs lysosome function by inhibiting TRPML1 and subsequently leads to cell death in B-lymphocytes.
Here we identify the lipid kinase PIKfyve as a regulator of an alternative pathway that distributes engulfed contents in support of intracellular macromolecular synthesis during macropinocytosis, entosis, and phagocytosis. We find that PIKfyve regulates vacuole size in part through its downstream effector, the cationic transporter TRPML1
findings suggest that TRPML1 may function as a key lysosomal Ca(2+) channel controlling both lysosome biogenesis and reformat
This review summarizes the current understanding of TRPML1 activation and regulation
target of rapamycin (TOR), a nutrient-sensitive protein kinase that negatively regulates autophagy, directly targets and inactivates the TRPML1 channel and thereby functional autophagy, through phosphorylation
lysosomal adaptation to environmental cues such as nutrient levels requires mTOR/TFEB-dependent, lysosome-to-nucleus regulation of lysosomal ML1 channels and Ca(2+) signaling.
TRPML1 has a novel role in protecting against lysosomotropic amine toxicity.
Retinal pigmented epithelial cells develop a punctate phenotype within 48 hours of small interfering (si)RNA-induced TRPML1-knockdown.
report of the first Saudi patient with Mucolipidosis type IV from a consanguineous family with two branches having a total of five patients carrying a novel transition mutation, c.1307A>G (p.Y436C) in exon 11
Data identified proteins as candidate TRPML1 interactors, and some false-positive interactors.
Findings raise the possibility that the neurological dysfunction in patients with mucolipidosis type IV may arise from amino acid deprivation of TPRML in neurons.
TRPML1 works in concert with ZnT4 to regulate zinc translocation between the cytoplasm and lysosomes.
findings show that TRPML1-mediated lysosomal Ca(2 ) release is dramatically reduced in Niemann-Pick disease cells; propose that abnormal accumulation of luminal lipids causes secondary lysosome storage by blocking TRPML1- and Ca(2 )-dependent lysosomal trafficking
PI(4,5)P(2) may serve as a negative cofactor for intracellular channels such as TRPML1
an NAADP-sensitive Ca(2+) release channel is characteristic of TRP-ML1 channels
single-particle electron cryo-microscopy structure of the mouse TRPML1 channel embedded in nanodiscs; combined with mutagenesis analysis, the TRPML1 structure reveals that phosphatidylinositol-3,5-bisphosphate (PtdIns(3,5)P2) binds to the N terminus of the channel-distal from the pore-and the helix-turn-helix extension between segments S2 and S3 probably couples ligand binding to pore opening
TRPML1 overexpression or treatment with the mTOR activator propranolol also attenuated the amyloid beta-protein (1-42)-inhibited mTOR/S6K signalling pathway and theamyloid beta-protein(1-42)-induced autophagic lysosome reformation -related protein expression levels.
It has been proposed that TRPML1 is regulated by pH, Ca2+, and phosphoinositides in a combined manner in order to accommodate the dynamic endocytosis process.
Deletion of TRPML1 increases secretory organelle size by fusion with lysosomes. Enhanced exocytosis that was rescued by re-expression of TRPML1 in neurons.
Silencing of TRPML1 hindered phagosome fusion with lysosomes.
lack of both mucolipins 1 and 3 causes an accelerated mucolipidosis IV-type of vacuolation in enterocytes
In the title.
These results demonstrate that the PtdIns(3,5)P2-Mcoln1 axis has an important role in ssRNA transportation into lysosomes in DCs.
ML1-null mice develop a primary, early-onset muscular dystrophy independent of neural degeneration. Dystrophin-glycoprotein complex and known membrane repair proteins are expressed normally, but membrane resealing was defective in ML1-null muscle fibers.
Transfection of CAMs with plasmids containing a full-length TRP-ML1 gene enhanced FasL-induced two-phase Ca2+ release.
Loss of Trpml1 causes reduced levels and mislocalization of the gastric proton pump and alters the secretory canaliculi, causing hypochlorhydria and hypergastrinemia.
This study describes, for the first time, a defect in macroautophagy in mucolipin-1-deficient mouse neurons.
the loss of TRPML1 function results in intracellular chelatable zinc dyshomeostasis.
TRPML1 is expressed in the mouse inner ear.
there is a hierarchy controlling the subcellular distributions of the TRPMLs such that TRPML1 and TRPML2 dictate the localization of TRPML3 and not vice versa
Mucolipin-1 functions in the efficient exit of molecules, destined for various cellular organelles, from lysosomal compartments
TRPML1 functions as a Fe(2+) permeable channel in late endosomes and lysosomes
This neuropathological characterization of the Mcoln1(-/-) mouse provides an important step in understanding how mucolipin 1 loss of function affects the CNS and contributes to mucolipidosis type IV disease.
This gene encodes a memberof the transient receptor potential (TRP) cation channel gene family. The transmembrane protein localizes to intracellular vesicular membranes including lysosomes, and functions in the late endocytic pathway and in the regulation of lysosomal exocytosis. The channel is permeable to Ca(2+), Fe(2+), Na(+), K(+), and H(+), and is modulated by changes in Ca(2+) concentration. Mutations in this gene result in mucolipidosis type IV.
, mucolipin 1.1
, mucolipidosis type IV protein