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Plant Sec14-like Phosphatidylinositol Transfer Proteins: Diverse Structures and Multi-Functions |
MAO Hua-Ying, SU Ya-Chun, QUE You-Xiong* |
Key Laboratory of Sugarcane Biology and Genetic Breeding, Ministry of Agriculture, Fujian Agriculture and Forestry University / Key Laboratory of Ministry of Education for Genetics, Breeding and Multiple Utilization of Crops, Fujian Agriculture and Forestry University, Fuzhou 350002, China |
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Abstract Sec14p, one of the phosphatidylinositol transfer proteins (PITPs), is originally found in Saccharomyces cerevisiae that has the functions of transporting phosphatidylinositol (phosphatidylinositol, PI) and phosphatidylcholine (phosphatidylcholine, PC) and is widely present in eukaryotes. Plant Sec14-like phosphatidylinositol transfer protein has high sequence homology with yeast Sec14p. In recent years, with the development of molecular biology and lipid genomics, more and more plant phosphatidylinositol transfer proteins have been excavated. In plants, the structure of those proteins has evolved from the original Sec14p domain to integrate with the membrane-localized Nlj16 domain and the vesicle transport Golgi dynamics (GOLD) domain, resulting in multi-functions, such as osmotic regulation, cell polarity growth, nodule development, protein transport, plant immune regulation and virus interactions. This paper reviews the differences and associations of structures and functions among Sec14-only proteins, Sec14-nodulin proteins and Sec14-GOLD proteins in plants, and highlights their multiple biological functions.
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Received: 30 July 2018
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Corresponding Authors:
* , queyouxiong@126.com
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