a College of Biological Sciences , China Agricultural University , Beijing , China.
b Key Laboratory of Plant Stress , Life Science College, Shandong Normal University , Jinan , China.
Plant Signal Behav. 2019;14(3):e1573097. doi: 10.1080/15592324.2019.1573097. Epub 2019 Feb 5.
The plasma membrane (PM) H-ATPase plays an important role in response to environmental stress, such as salt-alkaline stress. We have reported that the N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) protein Vesicle-associated membrane protein 711 (VAMP711) is involved in drought stress by regulating PM H-ATPase activity directly. In this study, we report that VAMP7C (VAMP711-14) represses PM H-ATPase activity in response to high-pH stress. The Arabidopsis PM H-ATPase AHA2 interacts with VAMP7C. The longin domain of VAMP711 interacts with AHA2 to inhibit PM H-ATPase activity on the plasma membrane. The alkaline phenotype of vamp711 and vamp711 vamp712 vamp713 triple mutants suggested that VAMP7C was functionally redundant in regulating PM H-ATPase activity in response to high-pH stress.
质膜（PM）H+-ATP 酶在应对环境胁迫（如盐碱性胁迫）中发挥着重要作用。我们曾报道，N-乙基马来酰亚胺敏感因子附着蛋白受体（SNARE）蛋白囊泡相关膜蛋白 711（VAMP711）通过直接调节 PM H+-ATP 酶活性参与干旱胁迫。在本研究中，我们报告 VAMP7C（VAMP711-14）在应对高 pH 胁迫时抑制 PM H+-ATP 酶活性。拟南芥质膜 H+-ATP 酶 AHA2 与 VAMP7C 相互作用。VAMP711 的长链结构域与 AHA2 相互作用，抑制质膜上 PM H+-ATP 酶的活性。vamp711、vamp711vamp712、vamp713 三重突变体的碱性表型表明 VAMP7C 在调节 PM H+-ATP 酶活性以应对高 pH 胁迫方面具有功能冗余性。
