NDLI: A mutation within the transmembrane domain of melanosomal protein Silver (Pmel17) changes lumenal fragment interactions

Please wait, while we are loading the content...

A mutation within the transmembrane domain of melanosomal protein Silver (Pmel17) changes lumenal fragment interactions

Content Provider	PubMed Central
Author	Regina, Kuliawat Santambrogio, Laura
Abstract	Melanocytes synthesize and store melanin within tissue-specific organelles, the melanosomes. Melanin deposition takes place along fibrils found within these organelles and fibril formation is known to depend on trafficking of the membrane glycoprotein Silver/Pmel17. However, correctly targeted, full-length Silver/Pmel17 cannot form fibers. Proteolytic processing in endosomal compartments and the generation of a lumenal Mα fragment that is incorporated into amyloid-like structures is also essential. Dominant White (DWhite), a mutant form of Silver/Pmel17 first described in chicken, causes disorganized fibers and severe hypopigmentation due to melanocyte death. Surprisingly, the DWhite mutation is an insertion of three amino acids into the transmembrane domain; the DWhite-Mα fragment is unaffected. To determine the functional importance of the transmembrane domain in organized fibril assembly, we investigated membrane trafficking and multimerization of Silver/Pmel17/DWhite proteins. We demonstrate that the DWhite mutation changes lipid interactions and disulfide bond-mediated associations of lumenal domains. Thus, partitioning into membrane microdomains and effects on conformation explain how the transmembrane region may contribute to the structural integrity of Silver/Pmel17 oligomers or influence toxic, amyloidogenic properties.
Related Links	http://dx.doi.org/10.1016/j.ejcb.2009.07.001
Ending Page	667
Page Count	15
Starting Page	653
File Format	PDF
ISSN	01719335
e-ISSN	16181298
Journal	European journal of cell biology
Issue Number	11
Volume Number	88
Language	English
Publisher Date	2009-11-01
Access Restriction	Open
Subject Keyword	Pathology and Forensic Medicine Cell Biology Histology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Cell Biology Histology Pathology and Forensic Medicine

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

The Melanosomal Protein PMEL17 as a Target for Antibody Drug Conjugate Therapy in Melanoma

The Repeat Domain of the Melanosomal Matrix Protein PMEL17/GP100 Is Required for the Formation of Organellar Fibers

FRET: Signals Hidden Within the Noise

Förster resonance energy transfer microscopy and spectroscopy for localizing protein-protein interactions in living cells

Deletion of the endothelin-A receptor gene within the developing mandible

Repeat Domains of Melanosome Matrix Protein Pmel17 Orthologs Form Amyloid Fibrils at the Acidic Melanosomal pH*

Heterogeneous Immunoreactivity of Emerin, a Nuclear Envelope LEM-domain Protein, in Normal Thyroid Follicles

High throughput flow cytometry based yeast two-hybrid array approach for large-scale analysis of protein-protein interactions

On the significance of Surfactant Protein-A within the human lungs

A mutation within the transmembrane domain of melanosomal protein Silver (Pmel17) changes lumenal fragment interactions

Similar Documents

The Melanosomal Protein PMEL17 as a Target for Antibody Drug Conjugate Therapy in Melanoma

The Repeat Domain of the Melanosomal Matrix Protein PMEL17/GP100 Is Required for the Formation of Organellar Fibers

FRET: Signals Hidden Within the Noise

Förster resonance energy transfer microscopy and spectroscopy for localizing protein-protein interactions in living cells

Deletion of the endothelin-A receptor gene within the developing mandible

Repeat Domains of Melanosome Matrix Protein Pmel17 Orthologs Form Amyloid Fibrils at the Acidic Melanosomal pH*

Heterogeneous Immunoreactivity of Emerin, a Nuclear Envelope LEM-domain Protein, in Normal Thyroid Follicles

High throughput flow cytometry based yeast two-hybrid array approach for large-scale analysis of protein-protein interactions

On the significance of Surfactant Protein-A within the human lungs

A mutation within the transmembrane domain of melanosomal protein Silver (Pmel17) changes lumenal fragment interactions