Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, Texas.
Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, Texas
Mol Pharmacol. 2022 Apr;101(4):201-212. doi: 10.1124/molpharm.121.000307. Epub 2021 Jul 26.
The WNK [with no lysine (K)] kinases and their downstream effector kinases, oxidative stress responsive 1 (OSR1) and SPS/STE20-related proline-alanine-rich kinase (SPAK), have well established functions in the maintenance of cell volume and ion homeostasis. Mutations in these kinases have been linked to an inherited form of hypertension, neurologic defects, and other pathologies. A rapidly expanding body of evidence points to the involvement of WNKs in regulating multiple diverse cellular processes as well as the progression of some forms of cancer. How OSR1 and SPAK contribute to these processes is well understood in some cases but completely unknown in others. OSR1 and SPAK are targeted to both WNKs and substrates via their conserved C-terminal (CCT) protein interaction domains. Considerable effort has been put forth to understand the structure, function, and interaction specificity of the CCT domains in relation to WNK signaling, and multiple inhibitors of WNK signaling target these domains. The domains bind RFxV and RxFxV protein sequence motifs with the consensus sequence R-F-x-V/I or R-x-F-x-V/I, but residues outside the core motif also contribute to specificity. CCT interactions are required for OSR1 and SPAK activation and deactivation as well as cation-chloride cotransporter substrate phosphorylation. All four WNKs also contain CCT-like domains that have similar structures and conserved binding residues when compared with CCT domains, but their functions and interaction specificities are mostly unknown. A better understanding of the varied actions of these domains and their interactions will better define the known signaling mechanisms of the WNK pathway as well as uncover new ones. SIGNIFICANCE STATEMENT: WNK [with no lysine (K)] kinases and their downstream effector kinases, oxidative stress responsive 1 (OSR1) and SPS/STE20-related proline-alanine-rich kinase (SPAK), have been shown to be involved in an array of diverse cellular processes. Here we review the function of modular protein interaction domains found in OSR1 and SPAK as well as related domains found in WNKs.
WNK [无赖氨酸 (K)] 激酶及其下游效应激酶,氧化应激反应蛋白 1(OSR1)和 SPS/STE20 相关脯氨酸-丙氨酸丰富激酶(SPAK),在维持细胞体积和离子稳态方面具有重要作用。这些激酶的突变与遗传性高血压、神经缺陷和其他病理学有关。越来越多的证据表明,WNK 参与调节多种不同的细胞过程以及某些形式的癌症的进展。在某些情况下,OSR1 和 SPAK 如何促进这些过程已经得到很好的理解,但在其他情况下则完全未知。OSR1 和 SPAK 通过其保守的 C 端(CCT)蛋白相互作用结构域靶向 WNK 和底物。人们已经付出了相当大的努力来理解 CCT 结构域与 WNK 信号转导的结构、功能和相互作用特异性,并且多种 WNK 信号转导抑制剂靶向这些结构域。这些结构域与 RFxV 和 RxFxV 蛋白序列基序结合,具有 R-F-x-V/I 或 R-x-F-x-V/I 的保守序列,但核心基序之外的残基也有助于特异性。CCT 相互作用对于 OSR1 和 SPAK 的激活和失活以及阳离子-氯离子共转运体底物磷酸化是必需的。所有四个 WNK 还包含 CCT 样结构域,与 CCT 结构域相比具有相似的结构和保守的结合残基,但它们的功能和相互作用特异性大多未知。更好地了解这些结构域的不同作用及其相互作用将更好地定义 WNK 途径的已知信号转导机制,并揭示新的机制。意义陈述:WNK [无赖氨酸 (K)] 激酶及其下游效应激酶,氧化应激反应蛋白 1(OSR1)和 SPS/STE20 相关脯氨酸-丙氨酸丰富激酶(SPAK)已被证明参与了一系列不同的细胞过程。在这里,我们综述了 OSR1 和 SPAK 中发现的模块化蛋白相互作用结构域以及在 WNK 中发现的相关结构域的功能。