12/14/2023 0 Comments Jnk1 regulate jun protein turnoverAmong these modifications, protein phosphorylation is one of the most studied PTMs. PTM plays a vital role in the control of protein activity, stability, and subcellular localization, thereby contributing to intracellular regulation. Post-translational modification (PTM) indicates covalent modifications of proteins after translation, such as protein methylation, glycosylation, acetylation, sumoylation, and ubiquitination. Phosphorylation-Dephosphorylation: The Scope of ThermodynamicsĬellular regulatory mechanisms respond specifically and robustly to extracellular stimuli. In this review, we will discuss the dynamics of phosphorylation/dephosphorylation, the mechanism of JNK pathway regulation by DUSPs, and the new possibilities of targeting DUSPs in JNK-related diseases elucidated in recent studies.ġ. Dual specificity phosphatases (DUSPs) regulate the magnitude and duration of signal transduction of the JNK pathway by dephosphorylating their substrates. Therefore, the proper balance between activation and inactivation of the JNK pathway needs to be tightly regulated. However, the activation of the JNK pathway is also implicated in human pathologies such as cancer, neurodegenerative diseases, and inflammatory diseases. The c-Jun N-terminal kinase (JNK) signaling pathway, a mitogen-activated protein kinase pathway, is regulated by a cascade of kinases and in turn regulates other physiological processes, such as cell differentiation, apoptosis, neuronal functions, and embryonic development. Kinases function as phosphorylating enzymes, and phosphatases dephosphorylate their target substrates, typically in a much shorter time. Because the post-modification of proteins regulates diverse cellular signaling pathways, the precise control of phosphorylation states is essential for maintaining cellular homeostasis. Protein phosphorylation affects conformational change, interaction, catalytic activity, and subcellular localization of proteins.
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