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  Structural insight into the TRIAP1/PRELI-like domain family of mitochondrial phospholipid transfer complexes

Miliara, X., Garnett, J. A., Tatsuta, T., Abid Ali, F., Baldie, H., Perez-Dorado, I., et al. (2015). Structural insight into the TRIAP1/PRELI-like domain family of mitochondrial phospholipid transfer complexes. EMBO Rep, 16(7), 824-35. doi:10.15252/embr.201540229.

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Miliara, X., Author
Garnett, J. A., Author
Tatsuta, T.1, Author           
Abid Ali, F., Author
Baldie, H., Author
Perez-Dorado, I., Author
Simpson, P., Author
Yague, E., Author
Langer, T.1, Author           
Matthews, S., Author
Affiliations:
1Department Langer - Mitochondrial Proteostasis, Max Planck Institute for Biology of Ageing, Max Planck Society, ou_3393994              

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Free keywords: Adaptor Proteins, Signal Transducing/*chemistry/*metabolism Amino Acid Sequence Binding Sites Biological Transport Crystallography, X-Ray Endoplasmic Reticulum/metabolism Humans Hydrophobic and Hydrophilic Interactions Intracellular Signaling Peptides and Proteins/*chemistry/*metabolism Membrane Proteins/*chemistry/*metabolism Mitochondria/*metabolism Mitochondrial Membranes/*metabolism Mitochondrial Proteins/metabolism Molecular Chaperones/metabolism Molecular Sequence Data Phospholipids/chemistry/*metabolism Protein Structure, Secondary Protein Structure, Tertiary Sequence Alignment
 Abstract: The composition of the mitochondrial membrane is important for its architecture and proper function. Mitochondria depend on a tightly regulated supply of phospholipid via intra-mitochondrial synthesis and by direct import from the endoplasmic reticulum. The Ups1/PRELI-like family together with its mitochondrial chaperones (TRIAP1/Mdm35) represent a unique heterodimeric lipid transfer system that is evolutionary conserved from yeast to man. Work presented here provides new atomic resolution insight into the function of a human member of this system. Crystal structures of free TRIAP1 and the TRIAP1-SLMO1 complex reveal how the PRELI domain is chaperoned during import into the intermembrane mitochondrial space. The structural resemblance of PRELI-like domain of SLMO1 with that of mammalian phoshatidylinositol transfer proteins (PITPs) suggest that they share similar lipid transfer mechanisms, in which access to a buried phospholipid-binding cavity is regulated by conformationally adaptable loops.

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 Dates: 2015-072015-06-14
 Publication Status: Issued
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 Identifiers: Other: 26071602
DOI: 10.15252/embr.201540229
ISSN: 1469-3178 (Electronic)1469-221X (Linking)
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Title: EMBO Rep
Source Genre: Journal
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Pages: - Volume / Issue: 16 (7) Sequence Number: - Start / End Page: 824 - 35 Identifier: -