Document Type
Article
Publication Date
4-7-2017
Abstract
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.
Recommended Citation
Filter, Joshua J.; Williams, Byron C.; Eto, Masumi; Shalloway, David; and Goldberg, Michael L., "Unfair competition governs the interaction of pCPI-17 with myosin phosphatase (PP1-MYPT1)." (2017). Department of Molecular Physiology and Biophysics Faculty Papers. Paper 15.
https://jdc.jefferson.edu/physfp/15
Creative Commons License
This work is licensed under a Creative Commons Attribution 4.0 License.
PubMed ID
28387646
Comments
This article has been peer reviewed. It is the author’s final published version in eLife
Volume 6, April 2017, Article number e24665.
The published version is available at DOI: 10.7554/eLife.24665. Copyright © Filter et al.