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Lipid transfer proteins: classification, nomenclature, structure, and function.
Structural Bioinformatics Laboratory, Biochemistry, Faculty of Science and EngineeringÅbo Akademi UniversityTurkuFinland.
Linköping University, Department of Physics, Chemistry and Biology, Biology. Linköping University, Faculty of Science & Engineering.
Linköping University, Department of Physics, Chemistry and Biology, Biology. Linköping University, Faculty of Science & Engineering.
2016 (English)In: Planta, ISSN 0032-0935, E-ISSN 1432-2048, Vol. 244, no 5, 971-997 p.Article, review/survey (Refereed) Published
Abstract [en]

The non-specific lipid transfer proteins (LTPs) constitute a large protein family found in all land plants. They are small proteins characterized by a tunnel-like hydrophobic cavity, which makes them suitable for binding and transporting various lipids. The LTPs are abundantly expressed in most tissues. In general, they are synthesized with an N-terminal signal peptide that localizes the protein to spaces exterior to the plasma membrane. The in vivo functions of LTPs are still disputed, although evidence has accumulated for a role in the synthesis of lipid barrier polymers, such as cuticular waxes, suberin, and sporopollenin. There are also reports suggesting that LTPs are involved in signaling during pathogen attacks. LTPs are considered as key proteins for the plant's survival and colonization of land. In this review, we aim to present an overview of the current status of LTP research and also to discuss potential future applications of these proteins. We update the knowledge on 3D structures and lipid binding and review the most recent data from functional investigations, such as from knockout or overexpressing experiments. We also propose and argument for a novel system for the classification and naming of the LTPs.

Place, publisher, year, edition, pages
Heidelberg: Springer, 2016. Vol. 244, no 5, 971-997 p.
Keyword [en]
NsLTP, LTP, Cutin, Suberin, Pollen, Protein structure
National Category
Natural Sciences Biochemistry and Molecular Biology
URN: urn:nbn:se:liu:diva-131810DOI: 10.1007/s00425-016-2585-4ISI: 000385251200001PubMedID: 27562524OAI: diva2:1033587

Funding agencies:Carl Tryggers Stiftelse

Available from: 2016-10-07 Created: 2016-10-07 Last updated: 2016-11-14Bibliographically approved

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