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Proteomes 2014, 2(4), 468-484; doi:10.3390/proteomes2040468

Proteomics Advances in the Understanding of Pollen–Pistil Interactions

Key Laboratory of Plant Germplasm Enhancement and Speciality Agriculture, Wuhan Botanical Garden, Chinese Academy of Sciences, Wuhan 430074, China
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Received: 25 July 2014 / Revised: 22 September 2014 / Accepted: 23 September 2014 / Published: 29 September 2014
(This article belongs to the Special Issue Plant Proteomics)
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Abstract

The first key point to the successful pollination and fertilization in plants is the pollen-pistil interaction, referring to the cellular and molecular levels, which mainly involve the haploid pollen and the diploid pistil. The process is defined as “siphonogamy”, which starts from the capture of pollen by the epidermis of stigma and ends up with the fusion of sperm with egg. So far, the studies of the pollen-pistil interaction have been explicated around the self-compatibility and self-incompatibility (SI) process in different species from the molecular genetics and biochemistry to cellular and signal levels, especially the mechanism of SI system. Among them, numerous proteomics studies based on the advanced technologies from gel-system to gel-free system were conducted, focusing on the interaction, in order to uncover the mechanism of the process. The current review mainly focuses on the recent developments in proteomics of pollen-pistil interaction from two aspects: self-incompatible and compatible pollination. It might provide a comprehensive insight on the proteins that were involved in the regulation of pollen-pistil interaction. View Full-Text
Keywords: proteomics; interaction; pollen; pistil; self-incompatibility proteomics; interaction; pollen; pistil; self-incompatibility
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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Fu, Z.; Yang, P. Proteomics Advances in the Understanding of Pollen–Pistil Interactions. Proteomes 2014, 2, 468-484.

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