Cargando…
AXER is an ATP/ADP exchanger in the membrane of the endoplasmic reticulum
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 m...
Autores principales: | , , , , , , , , , , , , , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2018
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6113206/ https://www.ncbi.nlm.nih.gov/pubmed/30154480 http://dx.doi.org/10.1038/s41467-018-06003-9 |
_version_ | 1783350968898813952 |
---|---|
author | Klein, Marie-Christine Zimmermann, Katharina Schorr, Stefan Landini, Martina Klemens, Patrick A. W. Altensell, Jacqueline Jung, Martin Krause, Elmar Nguyen, Duy Helms, Volkhard Rettig, Jens Fecher-Trost, Claudia Cavalié, Adolfo Hoth, Markus Bogeski, Ivan Neuhaus, H. Ekkehard Zimmermann, Richard Lang, Sven Haferkamp, Ilka |
author_facet | Klein, Marie-Christine Zimmermann, Katharina Schorr, Stefan Landini, Martina Klemens, Patrick A. W. Altensell, Jacqueline Jung, Martin Krause, Elmar Nguyen, Duy Helms, Volkhard Rettig, Jens Fecher-Trost, Claudia Cavalié, Adolfo Hoth, Markus Bogeski, Ivan Neuhaus, H. Ekkehard Zimmermann, Richard Lang, Sven Haferkamp, Ilka |
author_sort | Klein, Marie-Christine |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-6113206 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-61132062018-08-30 AXER is an ATP/ADP exchanger in the membrane of the endoplasmic reticulum Klein, Marie-Christine Zimmermann, Katharina Schorr, Stefan Landini, Martina Klemens, Patrick A. W. Altensell, Jacqueline Jung, Martin Krause, Elmar Nguyen, Duy Helms, Volkhard Rettig, Jens Fecher-Trost, Claudia Cavalié, Adolfo Hoth, Markus Bogeski, Ivan Neuhaus, H. Ekkehard Zimmermann, Richard Lang, Sven Haferkamp, Ilka Nat Commun Article 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. Nature Publishing Group UK 2018-08-28 /pmc/articles/PMC6113206/ /pubmed/30154480 http://dx.doi.org/10.1038/s41467-018-06003-9 Text en © The Author(s) 2018 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Klein, Marie-Christine Zimmermann, Katharina Schorr, Stefan Landini, Martina Klemens, Patrick A. W. Altensell, Jacqueline Jung, Martin Krause, Elmar Nguyen, Duy Helms, Volkhard Rettig, Jens Fecher-Trost, Claudia Cavalié, Adolfo Hoth, Markus Bogeski, Ivan Neuhaus, H. Ekkehard Zimmermann, Richard Lang, Sven Haferkamp, Ilka AXER is an ATP/ADP exchanger in the membrane of the endoplasmic reticulum |
title | AXER is an ATP/ADP exchanger in the membrane of the endoplasmic reticulum |
title_full | AXER is an ATP/ADP exchanger in the membrane of the endoplasmic reticulum |
title_fullStr | AXER is an ATP/ADP exchanger in the membrane of the endoplasmic reticulum |
title_full_unstemmed | AXER is an ATP/ADP exchanger in the membrane of the endoplasmic reticulum |
title_short | AXER is an ATP/ADP exchanger in the membrane of the endoplasmic reticulum |
title_sort | axer is an atp/adp exchanger in the membrane of the endoplasmic reticulum |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6113206/ https://www.ncbi.nlm.nih.gov/pubmed/30154480 http://dx.doi.org/10.1038/s41467-018-06003-9 |
work_keys_str_mv | AT kleinmariechristine axerisanatpadpexchangerinthemembraneoftheendoplasmicreticulum AT zimmermannkatharina axerisanatpadpexchangerinthemembraneoftheendoplasmicreticulum AT schorrstefan axerisanatpadpexchangerinthemembraneoftheendoplasmicreticulum AT landinimartina axerisanatpadpexchangerinthemembraneoftheendoplasmicreticulum AT klemenspatrickaw axerisanatpadpexchangerinthemembraneoftheendoplasmicreticulum AT altenselljacqueline axerisanatpadpexchangerinthemembraneoftheendoplasmicreticulum AT jungmartin axerisanatpadpexchangerinthemembraneoftheendoplasmicreticulum AT krauseelmar axerisanatpadpexchangerinthemembraneoftheendoplasmicreticulum AT nguyenduy axerisanatpadpexchangerinthemembraneoftheendoplasmicreticulum AT helmsvolkhard axerisanatpadpexchangerinthemembraneoftheendoplasmicreticulum AT rettigjens axerisanatpadpexchangerinthemembraneoftheendoplasmicreticulum AT fechertrostclaudia axerisanatpadpexchangerinthemembraneoftheendoplasmicreticulum AT cavalieadolfo axerisanatpadpexchangerinthemembraneoftheendoplasmicreticulum AT hothmarkus axerisanatpadpexchangerinthemembraneoftheendoplasmicreticulum AT bogeskiivan axerisanatpadpexchangerinthemembraneoftheendoplasmicreticulum AT neuhaushekkehard axerisanatpadpexchangerinthemembraneoftheendoplasmicreticulum AT zimmermannrichard axerisanatpadpexchangerinthemembraneoftheendoplasmicreticulum AT langsven axerisanatpadpexchangerinthemembraneoftheendoplasmicreticulum AT haferkampilka axerisanatpadpexchangerinthemembraneoftheendoplasmicreticulum |