Sar1, a Novel Regulator of ER-Mitochondrial Contact Sites.
Endoplasmic reticulum (ER)-mitochondrial contact sites play a pivotal role in exchange of lipids and ions between the two organelles. How size and function of these contact sites are regulated remains elusive. Here we report a previously unanticipated, but conserved role of the small GTPase Sar1 in...
| Main Authors: | , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2016-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC4839682?pdf=render |
| _version_ | 1818539831176724480 |
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| author | Karin B Ackema Cristina Prescianotto-Baschong Jürgen Hench Shyi Chyi Wang Zhi Hui Chia Heidi Mergentaler Fredéric Bard Stephan Frank Anne Spang |
| author_facet | Karin B Ackema Cristina Prescianotto-Baschong Jürgen Hench Shyi Chyi Wang Zhi Hui Chia Heidi Mergentaler Fredéric Bard Stephan Frank Anne Spang |
| author_sort | Karin B Ackema |
| collection | DOAJ |
| description | Endoplasmic reticulum (ER)-mitochondrial contact sites play a pivotal role in exchange of lipids and ions between the two organelles. How size and function of these contact sites are regulated remains elusive. Here we report a previously unanticipated, but conserved role of the small GTPase Sar1 in the regulation of ER-mitochondrial contact site size. Activated Sar1 introduces membrane curvature through its N-terminal amphiphatic helix at the ER-mitochondria interphase and thereby reducing contact size. Conversely, the S. cerevisiae N3-Sar1 mutant, in which curvature induction is decreased, caused an increase in ER-mitochondrial contacts. As a consequence, ER tubules are no longer able to mark the prospective scission site on mitochondria, thereby impairing mitochondrial dynamics. Consistently, blocking mitochondrial fusion partially rescued, whereas deletion of the dynamin-like protein enhanced the phenotype in the sar1D32G mutant. We conclude that Sar1 regulates the size of ER-mitochondria contact sites through its effects on membrane curvature. |
| first_indexed | 2024-12-11T21:47:18Z |
| format | Article |
| id | doaj.art-d5ad16fffdd44bb8ba7c9b99b7959e9f |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-11T21:47:18Z |
| publishDate | 2016-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-d5ad16fffdd44bb8ba7c9b99b7959e9f2022-12-22T00:49:34ZengPublic Library of Science (PLoS)PLoS ONE1932-62032016-01-01114e015428010.1371/journal.pone.0154280Sar1, a Novel Regulator of ER-Mitochondrial Contact Sites.Karin B AckemaCristina Prescianotto-BaschongJürgen HenchShyi Chyi WangZhi Hui ChiaHeidi MergentalerFredéric BardStephan FrankAnne SpangEndoplasmic reticulum (ER)-mitochondrial contact sites play a pivotal role in exchange of lipids and ions between the two organelles. How size and function of these contact sites are regulated remains elusive. Here we report a previously unanticipated, but conserved role of the small GTPase Sar1 in the regulation of ER-mitochondrial contact site size. Activated Sar1 introduces membrane curvature through its N-terminal amphiphatic helix at the ER-mitochondria interphase and thereby reducing contact size. Conversely, the S. cerevisiae N3-Sar1 mutant, in which curvature induction is decreased, caused an increase in ER-mitochondrial contacts. As a consequence, ER tubules are no longer able to mark the prospective scission site on mitochondria, thereby impairing mitochondrial dynamics. Consistently, blocking mitochondrial fusion partially rescued, whereas deletion of the dynamin-like protein enhanced the phenotype in the sar1D32G mutant. We conclude that Sar1 regulates the size of ER-mitochondria contact sites through its effects on membrane curvature.http://europepmc.org/articles/PMC4839682?pdf=render |
| spellingShingle | Karin B Ackema Cristina Prescianotto-Baschong Jürgen Hench Shyi Chyi Wang Zhi Hui Chia Heidi Mergentaler Fredéric Bard Stephan Frank Anne Spang Sar1, a Novel Regulator of ER-Mitochondrial Contact Sites. PLoS ONE |
| title | Sar1, a Novel Regulator of ER-Mitochondrial Contact Sites. |
| title_full | Sar1, a Novel Regulator of ER-Mitochondrial Contact Sites. |
| title_fullStr | Sar1, a Novel Regulator of ER-Mitochondrial Contact Sites. |
| title_full_unstemmed | Sar1, a Novel Regulator of ER-Mitochondrial Contact Sites. |
| title_short | Sar1, a Novel Regulator of ER-Mitochondrial Contact Sites. |
| title_sort | sar1 a novel regulator of er mitochondrial contact sites |
| url | http://europepmc.org/articles/PMC4839682?pdf=render |
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