Introduction of MCOLN1
Mucolipin-1, also known as transient receptor potential mucolipin-1 (TRPML1), is a membrane protein consisting of 580 amino acids encoded by the MCOLN1 gene and has a molecular weight of approximately 65 kDa. Mucolipin-1 is predicted to have six transmembrane domains and is a member of the large family of transient receptor potential (TRP) cation channels. Mutations of the MCOLN1 gene result in the lysosomal storage disorder mucolipidosis type IV (MLIV). The efficient targeting of mucolipin-1 to lysosomes requires di-leucine motifs in both the N-terminal and the C-terminal cytosolic tails. Mucolipin-1 is widely expressed in mammalian cells of lysosome or endosomal membrane and is the main channel for lysosomal Ca2+ release, as well as a key regulator of lysosomal storage and transport. In addition, it is considered to be a regulator of amyloid-β autophagy and accumulation within neurons.
|Basic Information of MCOLN1|
|Aliases||MG-2, Mucolipidin, Transient receptor potential channel mucolipin 1|
|Organism||Homo sapiens (Human)|
Function of MCOLN1 Membrane Protein
Mucolipins-1 is a non-selective, pH-regulated cation channel with a preference for monovalent cations, which might mediate the release of Ca2+ from the lysosomal or late endosomal lumen into the cytosol, thus regulating membrane trafficking, lysosomal biogenesis, and signal transduction. Mutations of MCOLN1 gene cause a severe lysosomal storage disorder called mucolipidosis type IV (MLIV), therefore, mucolipin-1 may have multiple functions in cells that are reflected by the general biochemical and clinical aspects of MLIV pathology. The constitutive achlorhydria in MLIV patients and the selective vacuolation in stomach parietal cells of MLIV patients suggests that mucolipin-1 is critical in HCI secretion. Moreover, the study of polycystin-2 in primary kidney cell cultures indicates that it is involved in lipid transport toward basolateral membranes. Finally, mucolipin-1 may also play a major role in the development of white matter tracts and in the maintenance of neurons and retinal cell integrity.
Fig.1 The structure of TRP protein. (Takahashi, 2012)
Application of MCOLN1 Membrane Protein in Literature
This article reports the cloning of a novel transient receptor potential cation channel gene and shows that this gene is mutated in patients with the disorder.
This article suggests that, to some extent, the effects of curcumin on the pathogenesis of AD are at least partially related to PI(3,5)P2 and TRPML1 expression levels.
This article finds that mice lacking the lysosomal channels mucolipins 3 and mucolipins1 accelerate ARHL due to degeneration of auditory outer hair cells, and this is the most common cause of human hearing loss and neurodegenerative diseases.
This article reveals the application of MOLE online for structural analyses of α-hemolysin and transient receptor potential mucolipin 1 (TRMP1) pores.
This article identifies key residues critical for Ca2+-induced TRPML1 channel current inhibition and reveals pH-dependent regulation of this channel, providing important information for the detailed mechanism of action of human TRPM.
MCOLN1 Preparation Options
Membrane protein studies have advanced significantly over the past few years. Based on our versatile Magic™ membrane protein production platform, we could offer a series of membrane protein preparation services for worldwide customers in reconstitution forms as well as multiple active formats. Aided by our versatile Magic™ anti-membrane protein antibody discovery platform, we also provide customized anti-MCOLN1 antibody development services.
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