ArticleThe Journal of biological chemistry2010
Endoplasmic reticulum export, subcellular distribution, and fibril formation by Pmel17 require an intact N-terminal domain junction.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 28 citations in OpenAlex.
- STIM1-Mitofusin2 interactions tether mitochondria and melanosome contacts that promote melanosome maturation.Nature communications · 2026Article
- Direct observation of the effects of chemical fixation in MNT-1 cells: A SE-ADM and Raman study.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Identification of critical amino acid residues in the regulatory N-terminal domain of PMEL.Scientific reports · 2021Article
- Lysophospholipids induce fibrillation of the repeat domain of Pmel17 through intermediate core-shell structures.Biochimica et biophysica acta. Proteins and proteomics · 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
- Cytosolic Processing Governs TAP-Independent Presentation of a Critical Melanoma Antigen.Journal of immunology (Baltimore, Md. : 1950) · 2018Article
- Reversing the amyloid trend: Mechanism of fibril assembly and dissolution of the repeat domain from a human functional amyloid.Israel journal of chemistry · 2017Article
- Melanosomal formation of PMEL core amyloid is driven by aromatic residues.Scientific reports · 2017Article
- Study of Exosomes Shed New Light on Physiology of Amyloidogenesis.Cellular and molecular neurobiology · 2016Review
- The Kringle-like Domain Facilitates Post-endoplasmic Reticulum Changes to Premelanosome Protein (PMEL) Oligomerization and Disulfide Bond Configuration and Promotes Amyloid Formation.The Journal of biological chemistry · 2016Article
- Toll-like receptor 2 and NLRP3 cooperate to recognize a functional bacterial amyloid, curli.Infection and immunity · 2015Article
- Lysophospholipid-containing membranes modulate the fibril formation of the repeat domain of a human functional amyloid, pmel17.Journal of molecular biology · 2014Article
- Three tapasin docking sites in TAP cooperate to facilitate transporter stabilization and heterodimerization.Journal of immunology (Baltimore, Md. : 1950) · 2014Article
- The PKD domain distinguishes the trafficking and amyloidogenic properties of the pigment cell protein PMEL and its homologue GPNMB.Pigment cell & melanoma research · 2013Article
- CD14 protein acts as an adaptor molecule for the immune recognition of Salmonella curli fibers.The Journal of biological chemistry · 2013Article
- PMEL: a pigment cell-specific model for functional amyloid formation.Pigment cell & melanoma research · 2013Review
- Critical residues in the PMEL/Pmel17 N-terminus direct the hierarchical assembly of melanosomal fibrils.Molecular biology of the cell · 2013Article
- Epithelial cells augment barrier function via activation of the Toll-like receptor 2/phosphatidylinositol 3-kinase pathway upon recognition of Salmonella enterica serovar Typhimurium curli fibrils in the gut.Infection and immunity · 2013Article
- The melanosomal protein PMEL17 as a target for antibody drug conjugate therapy in melanoma.The Journal of biological chemistry · 2012Article
Corrections and comments
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Authors and funding
5 authors at 4 institutions in 2 countries.
Funding
Abstract
Pmel17 is a melanocyte/melanoma-specific protein that subcellularly localizes to melanosomes, where it forms a fibrillar matrix that serves for the sequestration of potentially toxic reaction intermediates of melanin synthesis and deposition of the pigment. As a key factor in melanosomal biogenesis, understanding intracellular trafficking and processing of Pmel17 is of central importance to comprehend how these organelles are formed, how they mature, and how they function in the cell. Using a series of deletion and missense mutants of Pmel17, we are able to show that the integrity of the junction between the N-terminal region and the polycystic kidney disease-like domain is highly crucial for endoplasmic reticulum export, subcellular targeting, and fibril formation by Pmel17 and thus for establishing functional melanosomes.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.