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Identification and characterization of the single channel function of human mucolipin‐1 implicated in mucolipidosis type IV, a disorder affecting the lysosomal pathway
Author(s) -
LaPlante Janice M,
Falardeau John,
Sun Mei,
Kanazirska Marie,
Brown Edward M,
Slaugenhaupt Susan A,
Vassilev Peter M
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)03670-0
Subject(s) - mucolipidosis , endosome , transient receptor potential channel , microbiology and biotechnology , chemistry , lysosome , exocytosis , biology , receptor , biochemistry , secretion , enzyme
Mucolipin‐1 (MLN1) is a membrane protein with homology to the transient receptor potential channels and other non‐selective cation channels. It is encoded by the MCOLN1 gene, which is mutated in patients with mucolipidosis type IV (MLIV), an autosomal recessive disease that is characterized by severe abnormalities in neurological development as well as by ophthalmologic defects. At the cellular level, MLIV is associated with abnormal lysosomal sorting and trafficking. Here we identify the channel function of human MLN1 and characterize its properties. MLN1 represents a novel Ca 2+ ‐permeable channel that is transiently modulated by changes in [Ca 2+ ]. It is also permeable to Na + and K + . Large unitary conductances were measured in the presence of these cations. With its Ca 2+ permeability and modulation by [Ca 2+ ], MLN1 could play a major role in Ca 2+ transport regulating lysosomal exocytosis and potentially other phenomena related to the trafficking of late endosomes and lysosomes.