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study characterized mcoln1.1 and mcoln1.2, the putative co-orthologs of human MCOLN1 gene
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 ELISA Kits) 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 ELISA Kits) 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 ELISA Kits)+) 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 ELISA Kits)/TFEB-dependent, lysosome-to-nucleus regulation of lysosomal ML1 channels and Ca(2 (show CA2 ELISA Kits)+) 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.
Data identified proteins as candidate TRPML1 interactors, and some false-positive interactors.
TRPML1 works in concert with ZnT4 (show SLC30A4 ELISA Kits) to regulate zinc translocation between the cytoplasm and lysosomes.
an NAADP-sensitive Ca(2 (show CA2 ELISA Kits)+) release channel is characteristic of TRP-ML1 channels
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.
Transfection of CAMs with plasmids containing a full-length TRP-ML1 gene enhanced FasL (show FASL ELISA Kits)-induced two-phase Ca2 (show CA2 ELISA Kits)+ 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.
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