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Structural basis for proton coupled cystine transport by cystinosin

Abstract:

Amino acid transporters play a key role controlling the flow of nutrients across the lysosomal membrane and regulating metabolism in the cell. Mutations in the gene encoding the transporter cystinosin result in cystinosis, an autosomal recessive metabolic disorder characterised by the accumulation of cystine crystals in the lysosome. Cystinosin is a member of the PQ-loop family of solute carrier (SLC) transporters and uses the proton gradient to drive cystine export into the cytoplasm. However, the molecular basis for cystinosin function remains elusive, hampering efforts to develop novel treatments for cystinosis and understand the mechanisms of ion driven transport in the PQ-loop family. To address these questions, we present the crystal structures of cystinosin from Arabidopsis thaliana in both apo and cystine bound states. Using a combination of in vitro and in vivo based assays, we establish a mechanism for cystine recognition and proton coupled transport. Mutational mapping and functional characterisation of human cystinosin further provide a framework for understanding the molecular impact of disease-causing mutations.

Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1038/s41467-022-32589-2

Authors


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Role:
Author
ORCID:
0000-0002-6558-0590
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Role:
Author
ORCID:
0000-0001-5938-5185
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Institution:
University of Oxford
Department:
SOMERVILLE COLLEGE
Oxford college:
Somerville College
Role:
Author
ORCID:
0000-0003-3506-6045
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Role:
Author
ORCID:
0000-0001-8995-7324
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Institution:
University of Oxford
Division:
MPLS
Department:
Physics
Sub department:
Condensed Matter Physics
Oxford college:
Green Templeton College
Role:
Author
ORCID:
0000-0001-8996-2000


Publisher:
Springer Nature
Journal:
Nature Communications More from this journal
Volume:
13
Issue:
1
Article number:
4845
Publication date:
2022-08-17
Acceptance date:
2022-08-08
DOI:
EISSN:
2041-1723
ISSN:
2041-1723
Pmid:
35977944


Language:
English
Keywords:
Pubs id:
1274864
Local pid:
pubs:1274864
Deposit date:
2022-11-30

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