PKCδ Localization at the Membrane Increases Matrix Traction Force Dependent on PLCγ1/EGFR Signaling
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Jamison-2013-PKC delta Localizati.pdf
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2.27 MB
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Author(s)
Jamison, Joshua
Wang, James C.-H.
Wells, Alan
Lauffenburger, Douglas A.
Date Issued
October 2013
Journal
PLoS ONE
Publisher
Public Library of Science
Citation
Jamison, Joshua, Douglas Lauffenburger, James C.-H. Wang, and Alan Wells. “PKCδ Localization at the Membrane Increases Matrix Traction Force Dependent on PLCγ1/EGFR Signaling.” Edited by Maddy Parsons. PLoS ONE 8, no. 10 (October 14, 2013): e77434.
Version
Final published version
Abstract
During wound healing, fibroblasts initially migrate into the wound bed and later contract the matrix. Relevant mediators of transcellular contractility revealed by systems analyses are protein kinase c delta/myosin light chain-2 (PKCδ/MLC-2). PKCδ is activated by growth factor-driven PLCγ1 hydrolysis of phosphoinositide bisphosphate (PIP[subscript 2]) hydrolysis when it becomes tranlocated to the membrane. This leads to MLC-2 phosphorylation that regulates myosin for contractility. Furthermore, PKCδ n-terminus mediates PKCδ localization to the membrane in relative proximity to PLCγ1 activity. However, the role this localization and the relationship to its activation and signaling of force is not well understood. Therefore, we investigated whether the membrane localization of PKCδ mediates the transcellular contractility of fibroblasts.
MIT Department
Massachusetts Institute of Technology. Department of Biological Engineering
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DOI of Published Version
https://doi.org/10.1371/journal.pone.0077434
