Lipid transfer proteins: classification, nomenclature, structure, and function

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 tiss...

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Bibliographic Details
Published in:Planta 2016-11, Vol.244 (5), p.971-997
Main Authors: Salminen, Tiina A., Blomqvist, Kristina, Edqvist, Johan
Format: Article
Language:English
Subjects:
Agriculture
Biomedical and Life Sciences
Carrier Proteins - chemistry
Carrier Proteins - classification
Carrier Proteins - metabolism
Cutin
Ecology
embryophytes
epicuticular wax
Forestry
hydrophobicity
Life Sciences
Ligands
lipid transfer proteins
Lipids
LTP
NsLTP
pathogens
plant proteins
Plant Proteins - chemistry
Plant Proteins - classification
Plant Proteins - metabolism
Plant Sciences
Plants - metabolism
plasma membrane
Pollen
Polymers
Protein structure
Proteins
REVIEW
signal peptide
sporopollenin
Suberin
Terminology as Topic
tissues
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Summary: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.
ISSN:0032-0935
1432-2048
1432-2048
DOI:10.1007/s00425-016-2585-4