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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...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Portland Press Ltd.
2011
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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. |
format | Online Article Text |
id | pubmed-3195331 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | Portland Press Ltd. |
record_format | MEDLINE/PubMed |
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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