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Arabidopsis Synaptotagmin 2 Participates in Pollen Germination and Tube Growth and Is Delivered to Plasma Membrane via Conventional Secretion

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Molecular Plant 2015年第12期8卷 1737-1750页

作者： Hui Wang Shengcheng Han Wei Siao Chunqing Song Yun Xiang Xiaorong Wu Pengyu Cheng Hongjuan Li JAn Jasik Karol Micieta JAn Turna Boris Voigtt Frantisek Baluska Jin Liu Yingdian Wang Heping Zhao Beijing Key Laboratory of Gene Resource and Molecular Development College of Life Science Beijing Normal University Beijing 100875 China Department of Plant Cell Biology IZMB University of Bonn Kirschallee 153115 Bonn Germany School of Life Science Lanzhou University Lanzhou 730000 China Comenius University Science Park Comenius University Bratislava Mlynska dolina 842 15 Bratislava 4 Slovakia Department of Botany Faculty of Natural Sciences Comenius University Revova 39 811 02 Bratislava 1 SIovakia Department of Botany Faculty of Natural Sciences Comenius University Revova 39 811 02 Bratislava 1 Slovakia Institute of Botany Slovak Academy of Sciences Dubravska cesta 9 SK-84523 Bratislava Slovak Republic These authors contributed equally to this article. present address: Office of Teaching Affairs Handan University Handan 056005 China

Arabidopsis synaptotagmin 2 （SYT2） has been reported to participate in an unconventional secretory pathway in somatic cells. Our results showed that SYT2 was expressed mainly in the pollen ofArabidopsis thaliana. The pollen of syt2 T-DNA and RNA interference mutant lines exhibited reduced total germination and impeded pollen tube growth. Analysis of the expression of SYT2-GFP fusion protein in the pollen tube indicates that SYT2 was localized to distinct, patchy compartments but could co-localize with the Golgi markers, BODIPY TR C5 ceramide and GmManl-mCherry. However, SYT2-DsRed-E5 was localized to the plasma membrane in Arabidopsis suspension cells, in addition to the Golgi apparatus. The localization of SYT2 at the plasma membrane was further supported by immunofluorescence staining in pollen tubes. Moreover, brefeldin A treatment inhibited the transport of SYT2 to the plasma membrane and caused SYT2 to aggregate and form enlarged compartments. Truncation of the SYT2-C2AB domains also resulted in retention of SYT2 in the Golgi apparatus. An in vitro phospholipid-binding assay showed that SYT2-C2AB domains bind to the phospholipid membrane in a calcium-dependent manner. Take together, our results indicated that SYT2 was required for pollen germination and pollen tube growth, and was involved in conventional exocytosis.

关键词： synaptotagmins pollen germination calcium-dependent phospholipid binding C2 domains conventional secretion

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