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Vps33B is required for delivery of endocytosed cargo to lysosomes
Author(s) -
Galmes Romain,
ten Brink Corlinda,
Oorschot Viola,
Veenendaal Tineke,
Jonker Caspar,
van der Sluijs Peter,
Klumperman Judith
Publication year - 2015
Publication title -
traffic
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.677
H-Index - 130
eISSN - 1600-0854
pISSN - 1398-9219
DOI - 10.1111/tra.12334
Subject(s) - endosome , endocytic cycle , microbiology and biotechnology , lysosome , biology , endocytosis , vacuole , transport protein , lipid bilayer fusion , vesicular transport proteins , cell , vacuolar protein sorting , biochemistry , cytoplasm , intracellular , membrane , enzyme
Prion is an alternate conformer of a normal protein. The conversion of the normal protein to its prion form requires the sequential action of proteins that are also involved in various cellular functions including endocytosis, membrane trafficking and the protein‐quality control system called ‘insoluble protein deposit’ (IPOD). The IPOD is presumably the site for the delivery of prion to the autophagy system for degradation, whereas molecular chaperones, which act prior to transport to and at the IPOD, promote prion propagation and prevail against degradation.