ArticleTraffic (Copenhagen, Denmark)2006
Two di-leucine motifs regulate trafficking of mucolipin-1 to lysosomes.
Article in Traffic (Copenhagen, Denmark), 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 101 papers.
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Who cites it
101 citing papers in PubMed.
- MCOLN1/TRPML1-MCOLN3/TRPML3 heteromer and its coupling to CaAutophagy · 2025Article
- Lysosomal LRRC8 complex impacts lysosomal pH, morphology, and systemic glucose metabolism.Science advances · 2025Article
- What Does Iron Mean to an Oligodendrocyte?Glia · 2025Review
- Article
- Requirement of the N-terminal region of nonstructural protein 1 in cis for SARS-CoV-2 defective RNA replication.Journal of virology · 2024Article
- TRPML1 gating modulation by allosteric mutations and lipids.bioRxiv : the preprint server for biology · 2024Article
- The ion channels of endomembranes.Physiological reviews · 2024Review
- Residence of the Nucleotide Sugar Transporter Family Members SLC35F1 and SLC35F6 in the Endosomal/Lysosomal Pathway.International journal of molecular sciences · 2024Article
- S-acylation of Ca2+ transport proteins: molecular basis and functional consequences.Biochemical Society transactions · 2024Review
- TRPML1 and TFEB, an Intimate Affair.Handbook of experimental pharmacology · 2023Article
- A Structural Overview of TRPML1 and the TRPML Family.Handbook of experimental pharmacology · 2023Article
- Lysosomal KEMBO reports · 2022Article
- Structural mechanism of allosteric activation of TRPML1 by PI(3,5)PProceedings of the National Academy of Sciences of the United States of America · 2022Article
- MemDis: Predicting Disordered Regions in Transmembrane Proteins.International journal of molecular sciences · 2021Article
- Atomic insights into ML-SI3 mediated human TRPML1 inhibition.Structure (London, England : 1993) · 2021Article
- A weak COPI binding motif in the cytoplasmic tail of SARS-CoV-2 spike glycoprotein is necessary for its cleavage, glycosylation, and localization.FEBS letters · 2021Article
- The genetic cause of intellectual deficiency and/or congenital malformations in two parental reciprocal translocation carriers and implications for assisted reproduction.Journal of assisted reproduction and genetics · 2021Article
- Lysosomal TRPML1 Channel: Implications in Cardiovascular and Kidney Diseases.Advances in experimental medicine and biology · 2021Article
- Membrane Transport Proteins in Osteoclasts: The Ins and Outs.Frontiers in cell and developmental biology · 2021Review
- Vascular Dysfunction in Diabetes and Obesity: Focus on TRP Channels.Frontiers in physiology · 2021Review
41 more citing papers are in PubMed but not listed here.
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2 authors.
Funding
Abstract
Mutations in the mucolipin-1 gene have been linked to mucolipidosis type IV, a lysosomal storage disorder characterized by severe neurological and ophthalmologic abnormalities. Mucolipin-1 is a membrane protein containing six putative transmembrane domains with both its N- and C-termini localized facing the cytosol. To gain information on the sorting motifs that mediate the trafficking of this protein to lysosomes, we have generated chimeras in which the N- and C- terminal tail portions of mucolipin-1 were fused to a reporter gene. In this article, we report the identification of two separate di-leucine-type motifs that co-operate to regulate the transport of mucolipin-1 to lysosomes. One di-leucine motif is positioned at the N-terminal cytosolic tail and mediates direct transport to lysosomes, whereas the other di-leucine motif is found at the C-terminal tail and functions as an adaptor protein 2-dependent internalization motif. We have also found that the C-terminal tail of mucolipin-1 is palmitoylated and that this modification might regulate the efficiency of endocytosis. Finally, the mutagenesis of both di-leucine motifs abrogated lysosomal accumulation and resulted in cell-surface redistribution of mucolipin-1. Taken together, these results reveal novel information regarding the motifs that regulate mucolipin-1 trafficking and suggest a role for palmitoylation in protein sorting.
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