AXER is an ATP/ADP exchanger in the membrane of the endoplasmic reticulum
Marie-Christine Klein,
Katharina Zimmermann,
Stefan Schorr,
Martina Landini,
Patrick A. W. Klemens,
Jacqueline Altensell,
Martin Jung,
Elmar Krause,
Duy Nguyen,
Volkhard Helms,
Jens Rettig,
Claudia Fecher-Trost,
Adolfo Cavalié,
Markus Hoth,
Ivan Bogeski (),
H. Ekkehard Neuhaus (),
Richard Zimmermann (),
Sven Lang and
Ilka Haferkamp
Additional contact information
Marie-Christine Klein: Saarland University
Katharina Zimmermann: CIPMM Saarland University
Stefan Schorr: Saarland University
Martina Landini: Technical University Kaiserslautern
Patrick A. W. Klemens: Technical University Kaiserslautern
Jacqueline Altensell: Technical University Kaiserslautern
Martin Jung: Saarland University
Elmar Krause: CIPMM Saarland University
Duy Nguyen: Saarland University
Volkhard Helms: Saarland University
Jens Rettig: CIPMM Saarland University
Claudia Fecher-Trost: Saarland University
Adolfo Cavalié: Saarland University
Markus Hoth: CIPMM Saarland University
Ivan Bogeski: CIPMM Saarland University
H. Ekkehard Neuhaus: Technical University Kaiserslautern
Richard Zimmermann: Saarland University
Sven Lang: Saarland University
Ilka Haferkamp: Technical University Kaiserslautern
Nature Communications, 2018, vol. 9, issue 1, 1-14
Abstract:
Abstract To fulfill its role in protein biogenesis, the endoplasmic reticulum (ER) depends on the Hsp70-type molecular chaperone BiP, which requires a constant ATP supply. However, the carrier that catalyzes ATP uptake into the ER was unknown. Here, we report that our screen of gene expression datasets for member(s) of the family of solute carriers that are co-expressed with BiP and are ER membrane proteins identifies SLC35B1 as a potential candidate. Heterologous expression of SLC35B1 in E. coli reveals that SLC35B1 is highly specific for ATP and ADP and acts in antiport mode. Moreover, depletion of SLC35B1 from HeLa cells reduces ER ATP levels and, as a consequence, BiP activity. Thus, human SLC35B1 may provide ATP to the ER and was named AXER (ATP/ADP exchanger in the ER membrane). Furthermore, we propose an ER to cytosol low energy response regulatory axis (termed lowER) that appears as central for maintaining ER ATP supply.
Date: 2018
References: Add references at CitEc
Citations:
Downloads: (external link)
https://www.nature.com/articles/s41467-018-06003-9 Abstract (text/html)
Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.
Export reference: BibTeX
RIS (EndNote, ProCite, RefMan)
HTML/Text
Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-06003-9
Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/
DOI: 10.1038/s41467-018-06003-9
Access Statistics for this article
Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie
More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().