ArticleThe Journal of investigative dermatology2003
A novel splice variant of Pmel17 expressed by human melanocytes and melanoma cells lacking some of the internal repeats.
Article in The Journal of investigative dermatology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
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Who cites it
21 citing papers in PubMed, 38 citations in OpenAlex.
- Modulating functional amyloid formation via alternative splicing of the premelanosomal protein PMEL17.The Journal of biological chemistry · 2020Article
- pH-Dependent fibril maturation of a Pmel17 repeat domain isoform revealed by tryptophan fluorescence.Biochimica et biophysica acta. Proteins and proteomics · 2019Article
- Reversing the amyloid trend: Mechanism of fibril assembly and dissolution of the repeat domain from a human functional amyloid.Israel journal of chemistry · 2017Article
- PMEL Amyloid Fibril Formation: The Bright Steps of Pigmentation.International journal of molecular sciences · 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
- WASH and Tsg101/ALIX-dependent diversion of stress-internalized EGFR from the canonical endocytic pathway.Nature communications · 2015Article
- The yin and yang of amyloid: insights from α-synuclein and repeat domain of Pmel17.Physical chemistry chemical physics : PCCP · 2011Review
- Proprotein convertases process Pmel17 during secretion.The Journal of biological chemistry · 2011Article
- Repeat domains of melanosome matrix protein Pmel17 orthologs form amyloid fibrils at the acidic melanosomal pH.The Journal of biological chemistry · 2011Article
- Endoplasmic reticulum export, subcellular distribution, and fibril formation by Pmel17 require an intact N-terminal domain junction.The Journal of biological chemistry · 2010Article
- The secreted form of a melanocyte membrane-bound glycoprotein (Pmel17/gp100) is released by ectodomain shedding.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2010Article
- N-terminal domains elicit formation of functional Pmel17 amyloid fibrils.The Journal of biological chemistry · 2009Article
- The repeat domain of the melanosome fibril protein Pmel17 forms the amyloid core promoting melanin synthesis.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Formation of Pmel17 amyloid is regulated by juxtamembrane metalloproteinase cleavage, and the resulting C-terminal fragment is a substrate for gamma-secretase.The Journal of biological chemistry · 2009Article
- Premelanosome amyloid-like fibrils are composed of only golgi-processed forms of Pmel17 that have been proteolytically processed in endosomes.The Journal of biological chemistry · 2008Article
- Multiple splice variants within the bovine silver homologue (SILV) gene affecting coat color in cattle indicate a function additional to fibril formation in melanophores.BMC genomics · 2007Article
- Dual loss of ER export and endocytic signals with altered melanosome morphology in the silver mutation of Pmel17.Molecular biology of the cell · 2006Article
- Retrotransposon insertion in SILV is responsible for merle patterning of the domestic dog.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- The Silver locus product Pmel17/gp100/Silv/ME20: controversial in name and in function.Pigment cell research · 2005Review
- Molecular mechanisms regulating the tumor-targeting potential of splice-activated gene expression.Cancer gene therapy · 2004Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Pmel17 is a approximately 100 kDa pigment cell specific glycoprotein that plays a crucial part in the morphogenesis of melanosome precursors. Anti-Pmel17 immunoprecipitates from metabolically pulse labeled melanoma cells and melanocytes contain, in addition to full-length Pmel17, a glycoprotein that migrates with a lower relative molecular weight. Here we show that this glycoprotein is encoded by an mRNA that results from alternative splicing of the human Pmel17 gene from which a cryptic intron is excised. Immunoprecipitation recapture experiments showed that this glycoprotein contained both the N- and C-termini of full-length Pmel17. Sequence analysis of cDNA corresponding to the alternatively spliced form reveals the loss of three of 10 imperfect direct repeats from the central region of the lumenal domain. The product of the splice variant is processed with similar kinetics to full-length Pmel17, and localizes similarly to late endosomes when expressed ectopically in nonpigment cells. We speculate that truncation of the repeat region within Pmel17 alters either fibrillogenic activity or the interaction of Pmel17 with melanin intermediates. The expression of an alternatively spliced product may furthermore affect the cohort of peptides generated for recognition of melanoma cells by tumor-directed T lymphocytes.
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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.