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- Title
MAPKs 对磷酸酶MKP1-CD 催化的激活作用研究.
- Authors
刘文桐; 郭国光; 何倩倩; 徐荣; 何青霞
- Abstract
MAPKs (Mitogen-activated Protein Kinases) are pivotal pathways of cellular signal transduction, they are dephosphorylated by MKPs (Mitogen-activate Protein Kinase Phosphatases), the latter negatively regulate MAPKs signal delivery. During reactions of MKPs dephosphorylating MAPKs, MAPKs activate some MKPs catalytic abilities in turn. MKP1 is one of MKPs that can be activated by MAPKs. In this study, three typical MAPKs, ERK2, JNK1 and p38琢, are compared with their activation on MKP1 catalysis to facilitate understanding the substrate selective mechanisms between MAPKs and MKPs. : Use small molecular pNPP as substrate, adjust concentrations of present unphosphorylated ERK2, JNK1 and p38琢to determine different reactive velocities of MKP1 catalytic-domain fragments if catalytic velocities change. Compare and analyze enzymatic kinetic parameters to identify MAPKs activations on MKP1-CD catalytic activities. ERK2 and JNK1 can activate the catalytic capacity of MKP1 and increase catalytic rates by 1.5 to 2 times, but binding affinity of ERK2 to MKP1 is 6 times weaker than that of JNK1. No activated effects observed by p38琢to MKP1 dephosphorylated activities. Among three typical MAPKs, MKP1 can be activated by ERK2 and JNK1, but not p38琢, which further reveals specific interactions between MAPKs and MKPs as well as substrate impacts on MKPs catalytic activities.
- Subjects
MITOGEN-activated protein kinases; CELLULAR signal transduction; PHOSPHOPROTEIN phosphatases; PROTEIN kinases; CATALYTIC activity
- Publication
Progress in Modern Biomedicine, 2019, Vol 19, Issue 18, p3401
- ISSN
1673-6273
- Publication type
Article
- DOI
10.13241/j.cnki.pmb.2019.18.001