ArticleThe Journal of biological chemistry2008
Premelanosome amyloid-like fibrils are composed of only golgi-processed forms of Pmel17 that have been proteolytically processed in endosomes.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed, 77 citations in OpenAlex.
- Functional amyloids as molecular switches: emerging roles in diverse signalling pathways.Biochemical Society transactions · 2026Review
- Atomic structure and in situ visualization of native PMEL lamellae in melanosomes.Nature communications · 2025Article
- Cryo-EM of wild-type and mutant PMEL amyloid cores reveals structural mechanism of pigment dispersion syndrome.Nature communications · 2025Article
- Disrupting the Repeat Domain of Premelanosome Protein (PMEL) Produces Dysamyloidosis and Dystrophic Ocular Pigment Reflective of Pigmentary Glaucoma.International journal of molecular sciences · 2023Article
- Co-aggregation and secondary nucleation in the life cycle of human prolactin/galanin functional amyloids.eLife · 2022Article
- Innate immunity to prions: anti-prion systems turn a tsunami of prions into a slow drip.Current genetics · 2021Review
- Functional Domains and Evolutionary History of the PMEL and GPNMB Family Proteins.Molecules (Basel, Switzerland) · 2021Article
- Identification of critical amino acid residues in the regulatory N-terminal domain of PMEL.Scientific reports · 2021Article
- Functional Mammalian Amyloids and Amyloid-Like Proteins.Life (Basel, Switzerland) · 2020Review
- MCF7 Spheroid Development: New Insight about Spatio/Temporal Arrangements of TNTs, Amyloid Fibrils, Cell Connections, and Cellular Bridges.International journal of molecular sciences · 2020Article
- Article
- Research Techniques Made Simple: Cell Biology Methods for the Analysis of Pigmentation.The Journal of investigative dermatology · 2020Review
- pH-Dependent fibril maturation of a Pmel17 repeat domain isoform revealed by tryptophan fluorescence.Biochimica et biophysica acta. Proteins and proteomics · 2019Article
- Non-Synonymous variants in premelanosome protein (PMEL) cause ocular pigment dispersion and pigmentary glaucoma.Human molecular genetics · 2019Article
- Repeat domain-associated O-glycans govern PMEL fibrillar sheet architecture.Scientific reports · 2019Article
- Why Study Functional Amyloids? Lessons from the Repeat Domain of Pmel17.Journal of molecular biology · 2018Review
- Classical autophagy proteins LC3B and ATG4B facilitate melanosome movement on cytoskeletal tracks.Autophagy · 2017Article
- Melanosomal formation of PMEL core amyloid is driven by aromatic residues.Scientific reports · 2017Article
- PMEL Amyloid Fibril Formation: The Bright Steps of Pigmentation.International journal of molecular sciences · 2016Review
- Study of Exosomes Shed New Light on Physiology of Amyloidogenesis.Cellular and molecular neurobiology · 2016Review
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
Melanin pigments are synthesized within specialized organelles called melanosomes and polymerize on intraluminal fibrils that form within melanosome precursors. The fibrils consist of proteolytic fragments derived from Pmel17, a pigment cell-specific integral membrane protein. The intracellular pathways by which Pmel17 accesses melanosome precursors and the identity of the Pmel17 derivatives within fibrillar melanosomes have been a matter of debate. We show here that antibodies that detect Pmel17 within fibrillar melanosomes recognize only the luminal products of proprotein convertase cleavage and not the remaining products linked to the transmembrane domain. Moreover, antibodies to the N and C termini detect only Pmel17 isoforms present in early biosynthetic compartments, which constitute a large fraction of detectable steady state Pmel17 in cell lysates because of slow early biosynthetic transport and rapid consumption by fibril formation. Using an antibody to a luminal epitope that is destroyed upon modification by O-linked oligosaccharides, we show that all post-endoplasmic reticulum Pmel17 isoforms are modified by Golgi-associated oligosaccharide transferases, and that only processed forms contribute to melanosome biogenesis. These data indicate that Pmel17 follows a single biosynthetic route from the endoplasmic reticulum through the Golgi complex and endosomes to melanosomes, and that only fragments encompassing previously described functional luminal determinants are present within the fibrils. These data have important implications for the site and mechanism of fibril formation.
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Registered trials
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