Inactivation of Pmel alters melanosome shape but has only a subtle effect on visible pigmentation.

Autor: Anders R Hellström, Brenda Watt, Shahrzad Shirazi Fard, Danièle Tenza, Paula Mannström, Kristina Narfström, Björn Ekesten, Shosuke Ito, Kazumasa Wakamatsu, Jimmy Larsson, Mats Ulfendahl, Klas Kullander, Graça Raposo, Susanne Kerje, Finn Hallböök, Michael S Marks, Leif Andersson

Publikováno v: PLoS Genetics, Vol 7, Iss 9, p e1002285 (2011)

PMEL is an amyloidogenic protein that appears to be exclusively expressed in pigment cells and forms intralumenal fibrils within early stage melanosomes upon which eumelanins deposit in later stages. PMEL is well conserved among vertebrates, and alle

Externí odkaz: https://doaj.org/article/421f79eca213475d87b146fc6194252f

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

Autor: Brenda Watt, Dawn C. Harper, Karolina J. Janczura, Alexander C. Theos, Kathryn E. Herman, Michael S. Marks, Sarah C. Theos

Publikováno v: Pigment Cell & Melanoma Research. 26:470-486

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 melano

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6b4248a88dd1fdc247a05e750d865c77
https://doi.org/10.1111/pcmr.12084

BACE2 processes PMEL to form the melanosome amyloid matrix in pigment cells

Autor: Michael S. Marks, Guillaume van Niel, Ilse Hurbain, Bart De Strooper, Leila Rochin, Cecile Fort, Graça Raposo, Brenda Watt, Pascal Leblanc, Lutgarde Serneels

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2013, 110 (26), pp.10658-10663. ⟨10.1073/pnas.1220748110⟩

Amyloids are often associated with pathologic processes such as in Alzheimer’s disease (AD), but can also underlie physiological processes such as pigmentation. Formation of pathological and functional amyloidogenic substrates can require precursor

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f2968026497eb4de7c1830e27d133da9
https://europepmc.org/articles/PMC3696817/

Mutations in or near the transmembrane domain alter PMEL amyloid formation from functional to pathogenic

Autor: Graça Raposo, Susanne Kerje, Mark A. Lemmon, Danièle Tenza, Michael S. Marks, Leif Andersson, Brenda Watt

Publikováno v: PLoS Genetics
PLoS Genetics, Vol 7, Iss 9, p e1002286 (2011)

PMEL is a pigment cell-specific protein that forms physiological amyloid fibrils upon which melanins ultimately deposit in the lumen of the pigment organelle, the melanosome. Whereas hypomorphic PMEL mutations in several species result in a mild pigm

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::14f26a4a937ef8fcea672ba49d60e8eb
https://pubmed.ncbi.nlm.nih.gov/21949659

Mutations in or near the Transmembrane Domain Alter PMEL Amyloid Formation from Functional to Pathogenic

Autor: Leif Andersson, Shosuke Ito, Paula Mannström, Kristina Narfström, Graça Raposo, Kazumasa Wakamatsu, Susanne Kerje, Danièle Tenza, Michael S. Marks, Mats Ulfendahl, Finn Hallböök, Anders R. Hellström, Björn Ekesten, Shahrzad Shirazi Fard, Jimmy Larsson, Klas Kullander, Brenda Watt

Publikováno v: PLoS Genetics
PLoS Genetics, Vol 7, Iss 9, p e1002285 (2011)

PMEL is an amyloidogenic protein that appears to be exclusively expressed in pigment cells and forms intralumenal fibrils within early stage melanosomes upon which eumelanins deposit in later stages. PMEL is well conserved among vertebrates, and alle

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f9eccdafdd703d3f07f5251af97e563e
https://doi.org/10.1371/journal.pgen.1002285