Premelanosome amyloid-like fibrils are composed of only golgi-processed forms of Pmel17 that have been proteolytically processed in endosomes.
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The ocular albinism type 1 (OA1) G-protein-coupled receptor functions with MART-1 at early stages of melanogenesis to control melanosome identity and compositionThe tetraspanin CD63 regulates ESCRT-independent and -dependent endosomal sorting during melanogenesisPMEL Amyloid Fibril Formation: The Bright Steps of PigmentationThe recycling endosome protein Rab17 regulates melanocytic filopodia formation and melanosome traffickingInactivation of Pmel alters melanosome shape but has only a subtle effect on visible pigmentationMHC class II presentation of gp100 epitopes in melanoma cells requires the function of conventional endosomes and is influenced by melanosomes.The secreted form of a melanocyte membrane-bound glycoprotein (Pmel17/gp100) is released by ectodomain shedding.Endoplasmic reticulum export, subcellular distribution, and fibril formation by Pmel17 require an intact N-terminal domain junction.Glycoprotein nonmetastatic melanoma protein b, a melanocytic cell marker, is a melanosome-specific and proteolytically released protein.Mutations in or near the transmembrane domain alter PMEL amyloid formation from functional to pathogenicEffects of pH on aggregation kinetics of the repeat domain of a functional amyloid, Pmel17.Myosin vc interacts with Rab32 and Rab38 proteins and works in the biogenesis and secretion of melanosomesProprotein convertases process Pmel17 during secretion.Amyloid form of ovalbumin evokes native antigen-specific immune response in the host: prospective immuno-prophylactic potential.Mechanisms of protein delivery to melanosomes in pigment cells.The melanosomal protein PMEL17 as a target for antibody drug conjugate therapy in melanoma.The Kringle-like Domain Facilitates Post-endoplasmic Reticulum Changes to Premelanosome Protein (PMEL) Oligomerization and Disulfide Bond Configuration and Promotes Amyloid Formation.Critical residues in the PMEL/Pmel17 N-terminus direct the hierarchical assembly of melanosomal fibrils.PMEL: a pigment cell-specific model for functional amyloid formationThe PKD domain distinguishes the trafficking and amyloidogenic properties of the pigment cell protein PMEL and its homologue GPNMB.BACE2 processes PMEL to form the melanosome amyloid matrix in pigment cells.The repeat domain of the melanosome fibril protein Pmel17 forms the amyloid core promoting melanin synthesisA mutation within the transmembrane domain of melanosomal protein Silver (Pmel17) changes lumenal fragment interactions.Gpnmb is a melanosome-associated glycoprotein that contributes to melanocyte/keratinocyte adhesion in a RGD-dependent fashion.Melanoma-associated antigen expression in lymphangioleiomyomatosis renders tumor cells susceptible to cytotoxic T cells.N-terminal domains elicit formation of functional Pmel17 amyloid fibrilsPreferential secretion of inducible HSP70 by vitiligo melanocytes under stressMelanosomal formation of PMEL core amyloid is driven by aromatic residues.Control of amyloid assembly by autoregulation.Study of Exosomes Shed New Light on Physiology of Amyloidogenesis.The feelgood mutation in zebrafish dysregulates COPII-dependent secretion of select extracellular matrix proteins in skeletal morphogenesis.Glycolipid-dependent sorting of melanosomal from lysosomal membrane proteins by lumenal determinants.NET amyloidogenic backbone in human activated neutrophils.Identification of an amyloid fibril forming segment of human Pmel17 repeat domain (RPT domain).Classical autophagy proteins LC3B and ATG4B facilitate melanosome movement on cytoskeletal tracks.Hyperacidification of trans-Golgi network and endo/lysosomes in melanocytes by glucosylceramide-dependent V-ATPase activity.A β-solenoid model of the Pmel17 repeat domain: insights to the formation of functional amyloid fibrils.Layer-by-Layer Assembly of κ-Casein Amyloid Fibrils for the Preparation of Hollow MicrocapsulesBiogenesis of Melanosomes
P2860
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P2860
Premelanosome amyloid-like fibrils are composed of only golgi-processed forms of Pmel17 that have been proteolytically processed in endosomes.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
2007年论文
@zh
2007年论文
@zh-cn
name
Premelanosome amyloid-like fib ...... ically processed in endosomes.
@ast
Premelanosome amyloid-like fib ...... ically processed in endosomes.
@en
type
label
Premelanosome amyloid-like fib ...... ically processed in endosomes.
@ast
Premelanosome amyloid-like fib ...... ically processed in endosomes.
@en
prefLabel
Premelanosome amyloid-like fib ...... ically processed in endosomes.
@ast
Premelanosome amyloid-like fib ...... ically processed in endosomes.
@en
P2093
P2860
P356
P1476
Premelanosome amyloid-like fib ...... ically processed in endosomes.
@en
P2093
Alexander C Theos
Dawn C Harper
Graça Raposo
Kathryn E Herman
Michael S Marks
P2860
P304
P356
10.1074/JBC.M708007200
P407
P577
2007-11-08T00:00:00Z