Department of Biophysics, University of Delhi South Campus, Benito Juarez Road, New Delhi, 110021, India.
J Membr Biol. 2022 Feb;255(1):107-116. doi: 10.1007/s00232-021-00205-x. Epub 2021 Nov 3.
ERK1 is one of the members of the mitogen-activated protein kinases that regulate important cellular functions. VDAC is located at the outer membrane of mitochondria. Here, an interaction between VDAC and ERK1 has been studied on an artificial planar lipid bilayer using in vitro electrophysiology experiments. We report that VDAC is phosphorylated by ERK1 in the presence of Mg-ATP and its single-channel currents are inhibited on the artificial bilayer membrane. Treatment of Alkaline phosphatase on ERK1 phosphorylated VDAC leads to partial recovery of the single-channel VDAC currents. Later, phosphorylation of VDAC was demonstrated by Pro-Q diamond dye. Mass Spectrometric studies indicate phosphorylation of VDAC at Threonine 33, Threonine 55, and Serine 35. In a nutshell, phosphorylation of VDAC leads to the closure of the channel.
ERK1 是丝裂原活化蛋白激酶的成员之一，调节重要的细胞功能。VDAC 位于线粒体的外膜上。在这里，我们使用体外电生理学实验研究了 ERK1 在人工平面脂质双层上与 VDAC 之间的相互作用。我们报告说，在存在 Mg-ATP 的情况下，ERK1 使 VDAC 磷酸化，并且其单通道电流在人工双层膜上受到抑制。用碱性磷酸酶处理 ERK1 磷酸化的 VDAC 会导致单通道 VDAC 电流的部分恢复。随后，通过 Pro-Q 钻石染料证明了 VDAC 的磷酸化。质谱研究表明，VDAC 在苏氨酸 33、苏氨酸 55 和丝氨酸 35 处发生磷酸化。简而言之，VDAC 的磷酸化导致通道关闭。
