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LDIP cooperates with SEIPIN and LDAP to facilitate lipid droplet biogenesis in Arabidopsis

Journal Article · · The Plant Cell
 [1];  [2];  [3];  [4];  [5];  [6];  [2];  [7];  [3];  [8];  [8];  [9];  [5];  [5];  [5];  [5];  [4];  [10];  [2]
  1. Univ. of Guelph, ON (Canada); Willow Biosciences, Burnaby, BC (Canada); OSTI
  2. Univ. of Guelph, ON (Canada)
  3. US Dept. of Agriculture (USDA), Maricopa, AZ (United States). ARS-Arid-Land Agricultural Research Center
  4. Univ. of North Texas, Denton, TX (United States)
  5. Gottingen Univ. (Germany)
  6. Univ. of North Texas, Denton, TX (United States); Brookhaven National Lab. (BNL), Upton, NY (United States)
  7. Univ. of North Texas, Denton, TX (United States); Willow Biosciences, Calgary, AB (Canada)
  8. Université de Bordeaux, Villenave d’Ornon (France). Centre National de la Recherche Scientifique (CNRS)
  9. US Dept. of Agriculture (USDA), Maricopa, AZ (United States). ARS-Arid-Land Agricultural Research Center; Purdue Univ., West Lafayette, IN (United States)
  10. US Dept. of Agriculture (USDA), Maricopa, AZ (United States). ARS-Arid-Land Agricultural Research Center; US Dept. of Agriculture (USDA), Albany, CA (United States). Agricultural Research Service (ARS)
Cytoplasmic lipid droplets (LDs) are evolutionarily conserved organelles that store neutral lipids and play critical roles in plant growth, development, and stress responses. However, the molecular mechanisms underlying their biogenesis at the endoplasmic reticulum (ER) remain obscure. Here we show that a recently identified protein termed LD-associated protein [LDAP]-interacting protein (LDIP) works together with both endoplasmic reticulum-localized SEIPIN and the LD-coat protein LDAP to facilitate LD formation in Arabidopsis thaliana. Heterologous expression in insect cells demonstrated that LDAP is required for the targeting of LDIP to the LD surface, and both proteins are required for the production of normal numbers and sizes of LDs in plant cells. LDIP also interacts with SEIPIN via a conserved hydrophobic helix in SEIPIN and LDIP functions together with SEIPIN to modulate LD numbers and sizes in plants. Further, the co-expression of both proteins is required to restore normal LD production in SEIPIN-deficient yeast cells. These data, combined with the analogous function of LDIP to a mammalian protein called LD Assembly Factor 1, are discussed in the context of a new model for LD biogenesis in plant cells with evolutionary connections to LD biogenesis in other eukaryotes.
Research Organization:
Univ. of North Texas, Denton, TX (United States)
Sponsoring Organization:
USDOE Office of Science (SC), Basic Energy Sciences (BES); USDA; Natural Sciences and Engineering Research Council of Canada (NSERC); German Research Foundation (DFG); European Research Council (ERC); French National Centre for Scientific Research
Grant/Contract Number:
SC0016536
OSTI ID:
1852282
Journal Information:
The Plant Cell, Journal Name: The Plant Cell Journal Issue: 9 Vol. 33; ISSN 1040-4651
Publisher:
American Society of Plant Biologists (ASPB)Copyright Statement
Country of Publication:
United States
Language:
English

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Here, there and everywhere – the importance of neutral lipids in plant growth and development journal November 2021

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