Cryo-EM structure of the human ATP13A2
Ontology highlight
ABSTRACT:
SUBMITTER: Osamu Nureki
PROVIDER: EMPIAR-10975 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Cryo-EM reveals mechanistic insights into lipid-facilitated polyamine export by human ATP13A2.
Tomita Atsuhiro A Daiho Takashi T Kusakizako Tsukasa T Yamashita Keitaro K Ogasawara Satoshi S Murata Takeshi T Nishizawa Tomohiro T Nureki Osamu O
Molecular cell 20211118 23
The cytoplasmic polyamine maintains cellular homeostasis by chelating toxic metal cations, regulating transcriptional activity, and protecting DNA. ATP13A2 was identified as a lysosomal polyamine exporter responsible for polyamine release into the cytosol, and its dysfunction is associated with Alzheimer's disease and other neural degradation diseases. ATP13A2 belongs to the P5 subfamily of the P-type ATPase family, but its mechanisms remain unknown. Here, we report the cryoelectron microscopy ( ...[more]
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