دورية أكاديمية
أعرض في EDS

The PKD domain distinguishes the trafficking and amyloidogenic properties of the pigment cell protein PMEL and its homologue GPNMB.

التفاصيل البيبلوغرافية
العنوان: The PKD domain distinguishes the trafficking and amyloidogenic properties of the pigment cell protein PMEL and its homologue GPNMB.
المؤلفون: Theos AC; Department of Pathology & Laboratory Medicine and Physiology, University of Pennsylvania School of Medicine, Philadelphia, PA, USA., Watt B, Harper DC, Janczura KJ, Theos SC, Herman KE, Marks MS
المصدر: Pigment cell & melanoma research [Pigment Cell Melanoma Res] 2013 Jul; Vol. 26 (4), pp. 470-86. Date of Electronic Publication: 2013 Apr 02.
نوع المنشور: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: Blackwell Munksgaard Country of Publication: England NLM ID: 101318927 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1755-148X (Electronic) Linking ISSN: 17551471 NLM ISO Abbreviation: Pigment Cell Melanoma Res Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Oxford : Blackwell Munksgaard,
مواضيع طبية MeSH: Amyloid/*chemistry , Endosomes/*metabolism , Melanosomes/*metabolism , Membrane Glycoproteins/*chemistry , gp100 Melanoma Antigen/*chemistry, Cell Line, Tumor ; DNA, Complementary/metabolism ; Glycoside Hydrolases/metabolism ; Glycosylation ; HeLa Cells ; Humans ; Melanins/chemistry ; Melanocytes/metabolism ; Protein Structure, Tertiary ; Protein Transport ; Recombinant Proteins/metabolism
مستخلص: Proteolytic fragments of the pigment cell-specific glycoprotein, PMEL, form the amyloid fibrillar matrix underlying melanins in melanosomes. The fibrils form within multivesicular endosomes to which PMEL is selectively sorted and that serve as melanosome precursors. GPNMB is a tissue-restricted glycoprotein with substantial sequence homology to PMEL, but no known function, and was proposed to localize to non-fibrillar domains of distinct melanosome subcompartments in melanocytes. Here we confirm that GPNMB localizes to compartments distinct from the PMEL-containing multivesicular premelanosomes or late endosomes in melanocytes and HeLa cells, respectively, and is largely absent from fibrils. Using domain swapping, the unique PMEL localization is ascribed to its polycystic kidney disease (PKD) domain, whereas the homologous PKD domain of GPNMB lacks apparent sorting function. The difference likely reflects extensive modification of the GPNMB PKD domain by N-glycosylation, nullifying its sorting function. These results reveal the molecular basis for the distinct trafficking and morphogenetic properties of PMEL and GPNMB and support a deterministic function of the PMEL PKD domain in both protein sorting and amyloidogenesis.
(© 2013 John Wiley & Sons A/S.)
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معلومات مُعتمدة: F31 GM08917 United States GM NIGMS NIH HHS; T32 CA009140 United States CA NCI NIH HHS; T32 GN997229 United States PHS HHS; R01 AR048155 United States AR NIAMS NIH HHS; 5 T32 CA09140 United States CA NCI NIH HHS
المشرفين على المادة: 0 (Amyloid)
0 (DNA, Complementary)
0 (GPNMB protein, human)
0 (Melanins)
0 (Membrane Glycoproteins)
0 (PMEL protein, human)
0 (Recombinant Proteins)
0 (gp100 Melanoma Antigen)
EC 3.2.1.- (Glycoside Hydrolases)
تواريخ الأحداث: Date Created: 20130305 Date Completed: 20140206 Latest Revision: 20211021
رمز التحديث: 20240628
مُعرف محوري في PubMed: PMC3695043
DOI: 10.1111/pcmr.12084
PMID: 23452376
قاعدة البيانات: MEDLINE
الوصف
تدمد:1755-148X
DOI:10.1111/pcmr.12084