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Novel regulation of PLCζ activity via its XY-linker

The XY-linker region of somatic cell PLC (phospholipase)-β, -γ, -δ and -ϵ isoforms confers potent catalytic inhibition, suggesting a common auto-regulatory role. Surprisingly, the sperm PLCζ XY-linker does not mediate auto-inhibition. Unlike for somatic PLCs, the absence of the PLCζ XY-linker signif...

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Autores principales: Nomikos, Michail, Elgmati, Khalil, Theodoridou, Maria, Georgilis, Athena, Gonzalez-Garcia, J. Raul, Nounesis, George, Swann, Karl, Lai, F. Anthony
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Portland Press Ltd. 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3195331/
https://www.ncbi.nlm.nih.gov/pubmed/21767260
http://dx.doi.org/10.1042/BJ20110953
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author Nomikos, Michail
Elgmati, Khalil
Theodoridou, Maria
Georgilis, Athena
Gonzalez-Garcia, J. Raul
Nounesis, George
Swann, Karl
Lai, F. Anthony
author_facet Nomikos, Michail
Elgmati, Khalil
Theodoridou, Maria
Georgilis, Athena
Gonzalez-Garcia, J. Raul
Nounesis, George
Swann, Karl
Lai, F. Anthony
author_sort Nomikos, Michail
collection PubMed
description The XY-linker region of somatic cell PLC (phospholipase)-β, -γ, -δ and -ϵ isoforms confers potent catalytic inhibition, suggesting a common auto-regulatory role. Surprisingly, the sperm PLCζ XY-linker does not mediate auto-inhibition. Unlike for somatic PLCs, the absence of the PLCζ XY-linker significantly diminishes both in vitro PIP(2) (phosphatidylinositol 4,5-bisphosphate) hydrolysis and in vivo Ca(2+)-oscillation-inducing activity, revealing evidence for a novel PLCζ enzymatic mechanism.
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spelling pubmed-31953312011-11-01 Novel regulation of PLCζ activity via its XY-linker Nomikos, Michail Elgmati, Khalil Theodoridou, Maria Georgilis, Athena Gonzalez-Garcia, J. Raul Nounesis, George Swann, Karl Lai, F. Anthony Biochem J Accelerated Publication The XY-linker region of somatic cell PLC (phospholipase)-β, -γ, -δ and -ϵ isoforms confers potent catalytic inhibition, suggesting a common auto-regulatory role. Surprisingly, the sperm PLCζ XY-linker does not mediate auto-inhibition. Unlike for somatic PLCs, the absence of the PLCζ XY-linker significantly diminishes both in vitro PIP(2) (phosphatidylinositol 4,5-bisphosphate) hydrolysis and in vivo Ca(2+)-oscillation-inducing activity, revealing evidence for a novel PLCζ enzymatic mechanism. Portland Press Ltd. 2011-08-26 2011-09-15 /pmc/articles/PMC3195331/ /pubmed/21767260 http://dx.doi.org/10.1042/BJ20110953 Text en © 2011 The Author(s) The author(s) has paid for this article to be freely available under the terms of the Creative Commons Attribution Non-Commercial Licence (http://creativecommons.org/licenses/by-nc/2.5/) which permits unrestricted non-commercial use, distribution and reproduction in any medium, provided the original work is properly cited. http://creativecommons.org/licenses/by-nc/2.5/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Accelerated Publication
Nomikos, Michail
Elgmati, Khalil
Theodoridou, Maria
Georgilis, Athena
Gonzalez-Garcia, J. Raul
Nounesis, George
Swann, Karl
Lai, F. Anthony
Novel regulation of PLCζ activity via its XY-linker
title Novel regulation of PLCζ activity via its XY-linker
title_full Novel regulation of PLCζ activity via its XY-linker
title_fullStr Novel regulation of PLCζ activity via its XY-linker
title_full_unstemmed Novel regulation of PLCζ activity via its XY-linker
title_short Novel regulation of PLCζ activity via its XY-linker
title_sort novel regulation of plcζ activity via its xy-linker
topic Accelerated Publication
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3195331/
https://www.ncbi.nlm.nih.gov/pubmed/21767260
http://dx.doi.org/10.1042/BJ20110953
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