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anti-Human MCOLN1 Antibodies:
anti-Mouse (Murine) MCOLN1 Antibodies:
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study characterized mcoln1.1 and mcoln1.2, the putative co-orthologs of human MCOLN1 gene
two electron cryo-microscopy structures of full-length human TRPML1: a 3.72-A apo (show C9orf3 Antibodies) 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 (show CA2 Antibodies)+) release and Ca(2 (show CA2 Antibodies)+) 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 (show PIKFYVE Antibodies) 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 (show PIKFYVE Antibodies) 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 (show CA2 Antibodies)+) 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 (show FRAP1 Antibodies)/TFEB (show TFEB Antibodies)-dependent, lysosome-to-nucleus regulation of lysosomal ML1 channels and Ca(2 (show CA2 Antibodies)+) signaling.
TRPML1 has a novel role in protecting against lysosomotropic amine toxicity.
an NAADP-sensitive Ca(2 (show CA2 Antibodies)+) 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 (show FRAP1 Antibodies) activator propranolol also attenuated the amyloid beta-protein (1 (show DLX4 Antibodies)-42)-inhibited mTOR (show FRAP1 Antibodies)/S6K (show RPS6KB1 Antibodies) signalling pathway and theamyloid beta-protein(1 (show DLX4 Antibodies)-42)-induced autophagic lysosome reformation -related protein expression levels.
It has been proposed that TRPML1 is regulated by pH, Ca2 (show CA2 Antibodies)+, 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.
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.
Data identified proteins as candidate TRPML1 interactors, and some false-positive interactors.
Transfection of CAMs with plasmids containing a full-length TRP-ML1 gene enhanced FasL (show FASL Antibodies)-induced two-phase Ca2 (show CA2 Antibodies)+ release.
Loss of Trpml1 causes reduced levels and mislocalization of the gastric proton pump and alters the secretory canaliculi, causing hypochlorhydria and hypergastrinemia.
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