Unfair competition governs the interaction of pCPI-17 with myosin phosphatase (PP1-MYPT1)
| Autor: | Joshua J Filter, Masumi Eto, Byron C. Williams, David Shalloway, Michael L. Goldberg |
|---|---|
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Mouse QH301-705.5 unfair competition Science Phosphatase Slow rate Muscle Proteins smooth muscle contraction/relaxation Biology myosin phosphatase Biochemistry General Biochemistry Genetics and Molecular Biology Dephosphorylation 03 medical and health sciences Myosin-Light-Chain Phosphatase CPI-17 Myosin Phosphoprotein Phosphatases Humans Biology (General) Phosphorylation General Immunology and Microbiology General Neuroscience Intracellular Signaling Peptides and Proteins General Medicine Cell Biology Cell biology 030104 developmental biology Muscle relaxation HEK293 Cells Phosphoprotein Medicine Protein Processing Post-Translational Research Article Human |
| Zdroj: | eLife eLife, Vol 6 (2017) |
| ISSN: | 2050-084X |
| Popis: | The small phosphoprotein pCPI-17 inhibits myosin light-chain phosphatase (MLCP). Current models postulate that during muscle relaxation, phosphatases other than MLCP dephosphorylate and inactivate pCPI-17 to restore MLCP activity. We show here that such hypotheses are insufficient to account for the observed rapidity of pCPI-17 inactivation in mammalian smooth muscles. Instead, MLCP itself is the critical enzyme for pCPI-17 dephosphorylation. We call the mutual sequestration mechanism through which pCPI-17 and MLCP interact inhibition by unfair competition: MLCP protects pCPI-17 from other phosphatases, while pCPI-17 blocks other substrates from MLCP’s active site. MLCP dephosphorylates pCPI-17 at a slow rate that is, nonetheless, both sufficient and necessary to explain the speed of pCPI-17 dephosphorylation and the consequent MLCP activation during muscle relaxation. DOI: http://dx.doi.org/10.7554/eLife.24665.001 |
| Databáze: | OpenAIRE |
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