Sialylated Core 1 O-Glycans Influence the Sorting of Pmel17/gp100 and Determine Its Capacity to Form Fibrils
Open accessAbstract
Pmel17 is a melanocyte/melanoma-specific protein that is essential for the maturation of melanosomes to form mature, fibrillar, and pigmented organelles. Recently, we reported that the less glycosylated form of Pmel17 (termed iPmel17) is sorted via the plasma membrane in a manner distinct from mature Pmel17 (termed mPmel17), which is sorted directly to melanosomes. To clarify the mechanism(s) underlying the distinct processing and sorting of Pmel17, we generated a highly specific antibody (termed alphaPEP25h) against an epitope within the repeat domain of Pmel17 that is sensitive to changes in O-glycosylation. alphaPEP25h recognizes only iPmel17 and allows analysis of the processing and sorting of iPmel17 when compared with alphaPEP13h, an antibody that recognizes both iPmel17 and mPmel17. Our novel findings using alphaPEP25h demonstrate that iPmel17 differs from mPmel17 not only in its sensitivity to endoglycosidase H, but also in the content of core 1 O-glycans modified with sialic acid. This evidence reveals that iPmel17 is glycosylated differently in the Golgi and that it is sorted through the secretory pathway. Analysis of Pmel17 processing in glycosylation-deficient mutant cells reveals that Pmel17 lacking the correct addition of sialic acid and galactose loses the ability to form fibrils. Furthermore, we show that addition of sialic acid affects the stability and sorting of Pmel17 and reduces pigmentation. Alterations in sialyltransferase activity and substrates differ between normal and transformed melanocytes and may represent a critical change during malignant transformation.
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NCKX5 has a role in early melanosome biogenesis.
“A role for NCKX5 in early melanosome biogenesis is also supported by the reduction in partially processed 85-kDa pmel17 protein observed after SLC24A5 knockdown (Fig. 7), as this is a marker of early melanosomes (25).”
From SLC24A5 encodes a trans-Golgi network protein with potassium-dependent sodium-calcium exchange activity that regulates human epidermal melanogenesis (2008) · cites this paper as [25]
The 85-kDa form of pmel17 that is down-regulated by SLC24A5 knockdown is a marker of early melanosomes.
“The 85-kDa form of pmel17 that is down-regulated by SLC24A5 knockdown is a marker of early melanosomes (25), whereas Lamp1 is enriched in lysosomes (47).”
From SLC24A5 encodes a trans-Golgi network protein with potassium-dependent sodium-calcium exchange activity that regulates human epidermal melanogenesis (2008) · cites this paper as [25]
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Self-citationpH-Dependent fibril maturation of a Pmel17 repeat domain isoform revealed by tryptophan fluorescence
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Nonsense mutation in PMEL is associated with yellowish plumage colour phenotype in Japanese quail
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The yin and yang of amyloid: insights from α-synuclein and repeat domain of Pmel17
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Self-citationRepeat domain-associated O-glycans govern PMEL fibrillar sheet architecture
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Functional Domains and Evolutionary History of the PMEL and GPNMB Family Proteins
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Study of Exosomes Shed New Light on Physiology of Amyloidogenesis
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PMEL is mutated in oculocutaneous albinism
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Identification of critical amino acid residues in the regulatory N-terminal domain of PMEL
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Factors influencing amyloid fibril formation
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N-Acetylneuraminic Acid Inhibits Melanogenesis via Induction of Autophagy
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An Investigation of Autoantibodies against Tyrosine Hydroxylase in Patients with Vitiligo
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- Authors
- Valencia, J. C., Rouzaud, F., Julien, S., Chen, K. G., Passeron, T., Yamaguchi, Y., Abu-Asab, M., Tsokos, M., Costin, G. E., Yamaguchi, H., Jenkins, L. M. M., Nagashima, K., Appella, E., & Hearing, V. J.
- Affiliations
- National Institutes of Health (US)
- Guy's Hospital (GB)
- Corresponding author
- Valencia, Julio C.
- Hearing, Vincent J.
- ORCID
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2007-04
- Volume
- 282
- Issue
- 15
- Pages
- 11266-11280
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2057452550
- Cited by
- 50
- References
- 69
- Citations by year
- 2026: 1 · 2024: 5 · 2023: 1 · 2022: 1 · 2021: 3 · 2020: 2 · 2019: 3 · 2018: 3 · 2017: 1 · 2016: 3 · 2015: 2 · 2014: 1 · 2013: 3 · 2012: 3
- FWCI
- 1.99
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (Z99 NS999999)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › melanin and skin pigmentation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Keywords
- gp100, core 1 O-glycans, sialic acid, O-glycosylation, melanosome biogenesis, protein sorting, secretory pathway, Golgi processing, fibril formation, melanocyte pigmentation, sialyltransferase, malignant transformation, melanoma
- MeSH terms
- Animals, Antibodies, Endoplasmic Reticulum, Cricetinae, Humans, Membrane Glycoproteins, Polysaccharides, Time Factors, Microscopy, Immunoelectron, N-Acetylneuraminic Acid, Melanosomes, Protein Transport, Cell Line, Tumor, gp100 Melanoma Antigen
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