IKKε inhibits PKC to promote Fascin-dependent actin bundling

IKKε inhibits PKC to promote Fascin-dependent actin bundling

Signaling molecules have pleiotropic functions and are activated by various extracellular stimuli. Protein kinase C (PKC) is activated by diverse receptors, and its dysregulation is associated with diseases including cancer. However, how the undesired activation of PKC is prevented during developmen...

Full description

Bibliographic Details
Main Authors: Otani, Tetsuhisa, Ogura, Yosuke, Misaki, Kazuyo, Maeda, Takuya, Kimpara, Akiyo, Yonemura, Shigenobu, Hayashi, Shigeo
Format: Online
Language:English
Published: The Company of Biologists Ltd 2016
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5087637/
id pubmed-5087637
recordtype oai_dc
spelling pubmed-50876372016-11-07 IKKε inhibits PKC to promote Fascin-dependent actin bundling Otani, Tetsuhisa Ogura, Yosuke Misaki, Kazuyo Maeda, Takuya Kimpara, Akiyo Yonemura, Shigenobu Hayashi, Shigeo Research Article Signaling molecules have pleiotropic functions and are activated by various extracellular stimuli. Protein kinase C (PKC) is activated by diverse receptors, and its dysregulation is associated with diseases including cancer. However, how the undesired activation of PKC is prevented during development remains poorly understood. We have previously shown that a protein kinase, IKKε, is active at the growing bristle tip and regulates actin bundle organization during Drosophila bristle morphogenesis. Here, we demonstrate that IKKε regulates the actin bundle localization of a dynamic actin cross-linker, Fascin. IKKε inhibits PKC, thereby protecting Fascin from inhibitory phosphorylation. Excess PKC activation is responsible for the actin bundle defects in IKKε-deficient bristles, whereas PKC is dispensable for bristle morphogenesis in wild-type bristles, indicating that PKC is repressed by IKKε in wild-type bristle cells. These results suggest that IKKε prevents excess activation of PKC during bristle morphogenesis. The Company of Biologists Ltd 2016-10-15 /pmc/articles/PMC5087637/ /pubmed/27578797 http://dx.doi.org/10.1242/dev.138495 Text en © 2016. Published by The Company of Biologists Ltd http://creativecommons.org/licenses/by/3.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0), which permits unrestricted use, distribution and reproduction in any medium provided that the original work is properly attributed.
repository_type Open Access Journal
institution_category Foreign Institution
institution US National Center for Biotechnology Information
building NCBI PubMed
collection Online Access
language English
format Online
author Otani, Tetsuhisa
Ogura, Yosuke
Misaki, Kazuyo
Maeda, Takuya
Kimpara, Akiyo
Yonemura, Shigenobu
Hayashi, Shigeo
spellingShingle Otani, Tetsuhisa
Ogura, Yosuke
Misaki, Kazuyo
Maeda, Takuya
Kimpara, Akiyo
Yonemura, Shigenobu
Hayashi, Shigeo
IKKε inhibits PKC to promote Fascin-dependent actin bundling
author_facet Otani, Tetsuhisa
Ogura, Yosuke
Misaki, Kazuyo
Maeda, Takuya
Kimpara, Akiyo
Yonemura, Shigenobu
Hayashi, Shigeo
author_sort Otani, Tetsuhisa
title IKKε inhibits PKC to promote Fascin-dependent actin bundling
title_short IKKε inhibits PKC to promote Fascin-dependent actin bundling
title_full IKKε inhibits PKC to promote Fascin-dependent actin bundling
title_fullStr IKKε inhibits PKC to promote Fascin-dependent actin bundling
title_full_unstemmed IKKε inhibits PKC to promote Fascin-dependent actin bundling
title_sort ikkε inhibits pkc to promote fascin-dependent actin bundling
description Signaling molecules have pleiotropic functions and are activated by various extracellular stimuli. Protein kinase C (PKC) is activated by diverse receptors, and its dysregulation is associated with diseases including cancer. However, how the undesired activation of PKC is prevented during development remains poorly understood. We have previously shown that a protein kinase, IKKε, is active at the growing bristle tip and regulates actin bundle organization during Drosophila bristle morphogenesis. Here, we demonstrate that IKKε regulates the actin bundle localization of a dynamic actin cross-linker, Fascin. IKKε inhibits PKC, thereby protecting Fascin from inhibitory phosphorylation. Excess PKC activation is responsible for the actin bundle defects in IKKε-deficient bristles, whereas PKC is dispensable for bristle morphogenesis in wild-type bristles, indicating that PKC is repressed by IKKε in wild-type bristle cells. These results suggest that IKKε prevents excess activation of PKC during bristle morphogenesis.
publisher The Company of Biologists Ltd
publishDate 2016
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5087637/
_version_ 1613705349262475264

Similar Items