ALA10, a Phospholipid Flippase, Controls FAD2/FAD3 Desaturation of Phosphatidylcholine in the ER and Affects Chloroplast Lipid Composition in Arabidopsis thaliana. Issue 3 (30th November 2015)
- Record Type:
- Journal Article
- Title:
- ALA10, a Phospholipid Flippase, Controls FAD2/FAD3 Desaturation of Phosphatidylcholine in the ER and Affects Chloroplast Lipid Composition in Arabidopsis thaliana. Issue 3 (30th November 2015)
- Main Title:
- ALA10, a Phospholipid Flippase, Controls FAD2/FAD3 Desaturation of Phosphatidylcholine in the ER and Affects Chloroplast Lipid Composition in Arabidopsis thaliana
- Authors:
- Botella, César
Sautron, Emeline
Boudiere, Laurence
Michaud, Morgane
Dubots, Emmanuelle
Yamaryo-Botté, Yoshiki
Albrieux, Catherine
Marechal, Eric
Block, Maryse A.
Jouhet, Juliette - Abstract:
- Abstract : The ALA10 phospholipid flippase reduces phosphatidylcholine desaturation and stimulates galactolipid-tophosphatidylcholine ratio in photosynthetic tissues. Abstract: The biogenesis of photosynthetic membranes relies on galactoglycerolipids, which are synthesized via pathways that are dispatched over several cell compartments. This membrane biogenesis requires both trafficking of lipid intermediates and a tight homeostatic regulation. In this work, we address the role of ALA10 (for aminophospholipid ATPase), a P4 -type ATPase, in a process counteracting the monogalactosyldiacylglycerol (MGDG ) shortage in Arabidopsis ( Arabidopsis thaliana ) leaves. ALA10 can interact with protein partners, ALIS1 (for ALA-interacting subunit1) or ALIS5, leading to differential endomembrane localizations of the interacting proteins, close to the plasma membrane with ALIS1 or to chloroplasts with ALIS5. ALA10 interacts also with FATTY ACID DESATURASE2 (FAD2), and modification of ALA10 expression affects phosphatidylcholine (PC ) fatty acyl desaturation by disturbing the balance between FAD2 and FAD3 activities. Modulation of ALA10 expression downstream impacts the fatty acyl composition of chloroplast PC . ALA10 expression also enhances leaf growth and improves the MGDG -PC ratio, possibly through MGDG SYNTHASE1 (MGD1) activation by phosphatidic acid. The positive effect of ALA10 on leaf development is significant in conditions such as upon treatment of plants with Galvestine-1, anAbstract : The ALA10 phospholipid flippase reduces phosphatidylcholine desaturation and stimulates galactolipid-tophosphatidylcholine ratio in photosynthetic tissues. Abstract: The biogenesis of photosynthetic membranes relies on galactoglycerolipids, which are synthesized via pathways that are dispatched over several cell compartments. This membrane biogenesis requires both trafficking of lipid intermediates and a tight homeostatic regulation. In this work, we address the role of ALA10 (for aminophospholipid ATPase), a P4 -type ATPase, in a process counteracting the monogalactosyldiacylglycerol (MGDG ) shortage in Arabidopsis ( Arabidopsis thaliana ) leaves. ALA10 can interact with protein partners, ALIS1 (for ALA-interacting subunit1) or ALIS5, leading to differential endomembrane localizations of the interacting proteins, close to the plasma membrane with ALIS1 or to chloroplasts with ALIS5. ALA10 interacts also with FATTY ACID DESATURASE2 (FAD2), and modification of ALA10 expression affects phosphatidylcholine (PC ) fatty acyl desaturation by disturbing the balance between FAD2 and FAD3 activities. Modulation of ALA10 expression downstream impacts the fatty acyl composition of chloroplast PC . ALA10 expression also enhances leaf growth and improves the MGDG -PC ratio, possibly through MGDG SYNTHASE1 (MGD1) activation by phosphatidic acid. The positive effect of ALA10 on leaf development is significant in conditions such as upon treatment of plants with Galvestine-1, an inhibitor of MGDG synthases, or when plants are grown at chilling temperature. … (more)
- Is Part Of:
- Plant physiology. Volume 170:Issue 3(2016)
- Journal:
- Plant physiology
- Issue:
- Volume 170:Issue 3(2016)
- Issue Display:
- Volume 170, Issue 3 (2016)
- Year:
- 2016
- Volume:
- 170
- Issue:
- 3
- Issue Sort Value:
- 2016-0170-0003-0000
- Page Start:
- 1300
- Page End:
- 1314
- Publication Date:
- 2015-11-30
- Subjects:
- Plant physiology -- Periodicals
Botany -- Periodicals
Periodicals
Electronic journals
571.2 - Journal URLs:
- https://academic.oup.com/plphys/issue ↗
http://www.plantphysiol.org/ ↗
http://www.jstor.org/journals/00320889.html ↗
http://www.pubmedcentral.nih.gov/tocrender.fcgi?journal=69 ↗
http://www-us.ebsco.com/online/direct.asp?JournalID=101725 ↗
http://www.oxfordjournals.org/ ↗ - DOI:
- 10.1104/pp.15.01557 ↗
- Languages:
- English
- ISSNs:
- 0032-0889
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 16198.xml