Pryor, P.R., Reimann, F., Gribble, F.M. et al. (1 more author) (2006) Mucolipin-1 is a lysosomal membrane protein required for intracellular lactosylceramide traffic. Traffic, 7 (10). pp. 1388-1398. ISSN 1398-9219
Abstract
Mucolipin-1 is a membrane protein encoded by the gene MCOLN1, mutations in which result in the lysosomal storage disorder mucolipidosis type IV (MLIV). Efficient lysosomal targeting of mucolipin-1 requires di-leucine motifs in both the N-terminal and the C-terminal cytosolic tails. We have shown that aberrant lactosylceramide trafficking in MLIV cells may be rescued by wild-type mucolipin-1 expression but not by mucolipin-1 mistargeted to the plasma membrane or by lysosome-localized mucolipin-1 mutated in its predicted ion pore-selectivity region. Our data demonstrate that the correct localization of mucolipin-1 and the integrity of its ion pore are essential for its physiological function in the late endocytic pathway.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Dates: |
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Institution: | The University of York |
Academic Units: | The University of York > Faculty of Sciences (York) > Biology (York) |
Depositing User: | York RAE Import |
Date Deposited: | 10 Feb 2009 19:06 |
Last Modified: | 10 Feb 2009 19:07 |
Published Version: | http://dx.doi.org/10.1111/j.1600-0854.2006.00475.x |
Status: | Published |
Publisher: | Blackwell Publishing |
Identification Number: | 10.1111/j.1600-0854.2006.00475.x |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:7782 |