ArticleStructure (London, England : 1993)2018
The Structure of Melanoregulin Reveals a Role for Cholesterol Recognition in the Protein's Ability to Promote Dynein Function.
Article in Structure (London, England : 1993), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
9 citing papers in PubMed, 11 citations in OpenAlex.
- Proteomic Profiling of Plasma to Uncover Novel Intervention Targets and Prognostic Biomarkers for Chronic Liver Diseases.Diabetes, obesity & metabolism · 2026Article
- Comparison of Transcriptome Differences in Scales of Two Closely Related Snake Species (Animals : an open access journal from MDPI · 2025Article
- Transition to Piscivory Seen Through Brain Transcriptomics in a Juvenile Percid Fish: Complex Interplay of Differential Gene Transcription, Alternative Splicing, and ncRNA Activity.Journal of experimental zoology. Part A, Ecological and integrative physiology · 2025Article
- Xplor-NIH: Better parameters and protocols for NMR protein structure determination.Protein science : a publication of the Protein Society · 2024Article
- New Antimicrobial Peptide with Two CRAC Motifs: Activity againstMicroorganisms · 2022Article
- Kv7 channel trafficking by the microtubule network in vascular smooth muscle.Acta physiologica (Oxford, England) · 2021Review
- Dynein regulates Kv7.4 channel trafficking from the cell membrane.The Journal of general physiology · 2021Article
- Recent advances in understanding the molecular basis of melanogenesis in melanocytes.F1000Research · 2020Review
- Modulation of the Cholesterol-Dependent Activity of Macrophages IC-21 by CRAC Peptides with Substituted Motif-Forming Amino Acids.Biochemistry (Moscow) Supplement. Series A, Membrane and cell biology · 2020Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Melanoregulin (Mreg) is a small, highly charged, multiply palmitoylated protein present on the membrane of melanosomes. Mreg is implicated in the transfer of melanosomes from melanocytes to keratinocytes, and in promoting the microtubule minus end-directed transport of these organelles. The possible molecular function of Mreg was identified by solving its structure using nuclear magnetic resonance (NMR) spectroscopy. Mreg contains six α helices forming a fishhook-like fold in which positive and negative charges occupy opposite sides of the protein's surface and sandwich a putative, cholesterol recognition sequence (CRAC motif). Mreg containing a point mutation within its CRAC motif still targets to late endosomes/lysosomes, but no longer promotes their microtubule minus end-directed transport. Moreover, wild-type Mreg does not promote the microtubule minus end-directed transport of late endosomes/lysosomes in cells transiently depleted of cholesterol. Finally, reversing the charge of three clustered acidic residues partially inhibits Mreg's ability to drive these organelles to microtubule minus ends.
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