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. 2016 Jul 25;17:91. doi: 10.1186/s12931-016-0415-7

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© The Author(s). 2016

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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Fig. 7 — Proposed regulation of vimentin by protein phosphatase 1(PP1). Upon agonist simulation, PP1 is dissociated from vimentin and inhibited, which increases vimentin phosphorylation at Ser-56. Phosphorylated vimentin promotes the dissociation of p130CAS from cytoskeletal vimentin, which provides more “free” p130CAS for actin polymerization. In addition, PP1 may regulate myosin light chain phosphorylation. Both actin dynamics and myosin activation are indispensable for smooth muscle contraction