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拟南芥肌球蛋白 XIK 与外泌体复合物相互作用，以促进胞吐作用期间囊泡的连接。

Arabidopsis myosin XIK interacts with the exocyst complex to facilitate vesicle tethering during exocytosis.

机构信息

Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907, USA.

Department of Botany and Plant Pathology, Purdue University, West Lafayette, Indiana 47907, USA.

出版信息

Plant Cell. 2021 Aug 13;33(7):2454-2478. doi: 10.1093/plcell/koab116.

DOI:10.1093/plcell/koab116
PMID:33871640
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC8364239/
Abstract

Myosin motors are essential players in secretory vesicle trafficking and exocytosis in yeast and mammalian cells; however, similar roles in plants remain a matter for debate, at least for diffusely growing cells. Here, we demonstrate that Arabidopsis (Arabidopsis thaliana) myosin XIK, via its globular tail domain (GTD), participates in the vesicle tethering step of exocytosis through direct interactions with the exocyst complex. Specifically, myosin XIK GTD bound directly to several exocyst subunits in vitro and functional fluorescently tagged XIK colocalized with multiple exocyst subunits at plasma membrane (PM)-associated stationary foci. Moreover, genetic and pharmacological inhibition of myosin XI activity reduced the rate of appearance and lifetime of stationary exocyst complexes at the PM. By tracking single exocytosis events of cellulose synthase (CESA) complexes with high spatiotemporal resolution imaging and pair-wise colocalization of myosin XIK, exocyst subunits, and CESA6, we demonstrated that XIK associates with secretory vesicles earlier than exocyst and is required for the efficient localization and normal dynamic behavior of exocyst complex at the PM tethering site. This study reveals an important functional role for myosin XI in secretion and provides insights about the dynamic regulation of exocytosis in plants.

摘要

肌球蛋白马达是酵母和哺乳动物细胞中分泌小泡运输和胞吐作用的重要参与者；然而，在植物中类似的作用仍存在争议，至少对于扩散生长的细胞是如此。在这里，我们证明拟南芥（Arabidopsis thaliana）肌球蛋白 XIK 通过其球状尾部结构域（GTD），通过与外泌体复合物的直接相互作用，参与胞吐作用的囊泡连接步骤。具体来说，肌球蛋白 XIK GTD 在体外直接结合多个外泌体亚基，并且功能荧光标记的 XIK 与质膜（PM）相关的固定焦点处的多个外泌体亚基共定位。此外，肌球蛋白 XI 活性的遗传和药理学抑制降低了 PM 处固定外泌体复合物的出现速度和寿命。通过高时空分辨率成像跟踪纤维素合酶（CESA）复合物的单个胞吐事件以及肌球蛋白 XIK、外泌体亚基和 CESA6 的成对共定位，我们证明 XIK 与分泌囊泡的结合早于外泌体，并且对于外泌体复合物在 PM 连接位点的有效定位和正常动态行为是必需的。这项研究揭示了肌球蛋白 XI 在分泌中的重要功能作用，并提供了关于植物胞吐作用动态调节的见解。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/86d9/8364239/5ea2f1b11c1a/koab116f9.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/86d9/8364239/51f322acabcb/koab116f10.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/86d9/8364239/2428de838785/koab116f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/86d9/8364239/9eadc22f45e0/koab116f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/86d9/8364239/591c954f5f1b/koab116f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/86d9/8364239/7ca1395ad148/koab116f4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/86d9/8364239/b55bccab57b0/koab116f5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/86d9/8364239/26734f1e31bb/koab116f6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/86d9/8364239/8f7fc717470e/koab116f7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/86d9/8364239/a9d90c2588ab/koab116f8.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/86d9/8364239/5ea2f1b11c1a/koab116f9.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/86d9/8364239/51f322acabcb/koab116f10.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/86d9/8364239/2428de838785/koab116f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/86d9/8364239/9eadc22f45e0/koab116f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/86d9/8364239/591c954f5f1b/koab116f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/86d9/8364239/7ca1395ad148/koab116f4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/86d9/8364239/b55bccab57b0/koab116f5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/86d9/8364239/26734f1e31bb/koab116f6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/86d9/8364239/8f7fc717470e/koab116f7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/86d9/8364239/a9d90c2588ab/koab116f8.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/86d9/8364239/5ea2f1b11c1a/koab116f9.jpg

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