Unusual roles of secretory SNARE SYP132 in plasma membrane H+-ATPase traffic and vegetative plant growth

阅读量:

52

作者:

L XiaMM Marquès-BuenoCG BruceRA Karnik

展开

摘要:

The plasma membrane proton (H+)-ATPases of plants generate steep electrochemical gradients and activate osmotic solute uptake. H+-ATPase-mediated proton pumping orchestrates cellular homeostasis and is a prerequisite for plastic cell expansion and plant growth. All evidence suggests that the population of H+-ATPase proteins at the plasma membrane reflects a balance of their roles in exocytosis, endocytosis, and recycling. Auxin governs both traffic and activation of the plasma membrane H+-ATPase proteins already present at the membrane. As in other eukaryotes, in plants, SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor)-mediated membrane traffic influences the density of several proteins at the plasma membrane. Even so, H+-ATPase traffic, its relationship with SNAREs, and its regulation by auxin have remained enigmatic. Here, we identify the Arabidopsis (Arabidopsis thaliana) Qa-SNARE SYP132 (Syntaxin of Plants 132) as a key factor in H+-ATPase traffic and demonstrate its association with endocytosis. SYP132 is a low abundant, secretory SNARE that primarily localizes to the plasma membrane. We find that SYP132 expression is tightly regulated by auxin and that augmented SYP132 expression reduces the amount of H+-ATPase proteins at the plasma membrane. The physiological consequences of SYP132 over-expression include reduced apoplast acidification and suppressed vegetative growth. Thus, SYP132 plays unexpected and vital roles in auxin-regulated H+-ATPase traffic and associated functions at the plasma membrane.

展开

DOI:

10.1104/pp.19.00266

年份:

2019

通过文献互助平台发起求助,成功后即可免费获取论文全文。

我们已与文献出版商建立了直接购买合作。

你可以通过身份认证进行实名认证,认证成功后本次下载的费用将由您所在的图书馆支付

您可以直接购买此文献,1~5分钟即可下载全文,部分资源由于网络原因可能需要更长时间,请您耐心等待哦~

身份认证 全文购买

相似文献

参考文献

引证文献

来源期刊

Plant physiology
2019/03/29

站内活动

辅助模式

0

引用

文献可以批量引用啦~
欢迎点我试用!

关于我们

百度学术集成海量学术资源,融合人工智能、深度学习、大数据分析等技术,为科研工作者提供全面快捷的学术服务。在这里我们保持学习的态度,不忘初心,砥砺前行。
了解更多>>

友情链接

百度云百度翻译

联系我们

合作与服务

期刊合作 图书馆合作 下载产品手册

©2025 Baidu 百度学术声明 使用百度前必读

引用