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. 2019 Jun 6;9:8337. doi: 10.1038/s41598-019-44841-9

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© The Author(s) 2019

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as 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 images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Negative feedback between PknB and PstP allow a transient response to stimulation. 1 Transient stimulation of PknB. 2 PknB autophosphorylates becoming activated. 3 Activated PknB phosphorylates its substrates. 4 Activated PknB phosphorylates PstP, activating PstP. 5 Activated PstP dephosphorylates PknB, returning it to the unactivated form. 6 Activated PstP dephosphorylates PknB substrates (including itself). PknB and PstP oppose each other, so that the response to PknB stimulation is transient. When PstP is knocked down there is no negative regulator to counter the positive feedback of PknB autoactivation, so transient stimuli lead to lasting PknB activation and widespread hyperphosphorylation of PknB substrates. Structures deposited in the PDB are used in this scheme (1O6Y, 2KUI, 2CM1), although the structural changes that occur during signalling are unknown. Similar feedback loops may exist for other Mycobacterial protein kinases.