PYK2 senses calcium through a disordered dimerization and calmodulin-binding element
Protein tyrosine kinase 2-beta is shown to function as a sensor and effector of cellular calcium influx through self-association.
| Main Authors: | , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2022-08-01
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| Series: | Communications Biology |
| Online Access: | https://doi.org/10.1038/s42003-022-03760-8 |
| _version_ | 1811320763184054272 |
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| author | Afaque A. Momin Tiago Mendes Philippe Barthe Camille Faure SeungBeom Hong Piao Yu Gress Kadaré Mariusz Jaremko Jean-Antoine Girault Łukasz Jaremko Stefan T. Arold |
| author_facet | Afaque A. Momin Tiago Mendes Philippe Barthe Camille Faure SeungBeom Hong Piao Yu Gress Kadaré Mariusz Jaremko Jean-Antoine Girault Łukasz Jaremko Stefan T. Arold |
| author_sort | Afaque A. Momin |
| collection | DOAJ |
| description | Protein tyrosine kinase 2-beta is shown to function as a sensor and effector of cellular calcium influx through self-association. |
| first_indexed | 2024-04-13T13:05:06Z |
| format | Article |
| id | doaj.art-5b021a3305b042d591ae0970768c1e8c |
| institution | Directory Open Access Journal |
| issn | 2399-3642 |
| language | English |
| last_indexed | 2024-04-13T13:05:06Z |
| publishDate | 2022-08-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Communications Biology |
| spelling | doaj.art-5b021a3305b042d591ae0970768c1e8c2022-12-22T02:45:47ZengNature PortfolioCommunications Biology2399-36422022-08-015111510.1038/s42003-022-03760-8PYK2 senses calcium through a disordered dimerization and calmodulin-binding elementAfaque A. Momin0Tiago Mendes1Philippe Barthe2Camille Faure3SeungBeom Hong4Piao Yu5Gress Kadaré6Mariusz Jaremko7Jean-Antoine Girault8Łukasz Jaremko9Stefan T. Arold10Computational Bioscience Research Center (CBRC), King Abdullah University of Science and Technology (KAUST)Inserm UMR-S 1270, Sorbonne Université, Faculty of Sciences and Engineering, Institut du Fer à MoulinCentre de Biologie Structurale (CBS), University MontpellierInserm UMR-S 1270, Sorbonne Université, Faculty of Sciences and Engineering, Institut du Fer à MoulinComputational Bioscience Research Center (CBRC), King Abdullah University of Science and Technology (KAUST)Computational Bioscience Research Center (CBRC), King Abdullah University of Science and Technology (KAUST)Inserm UMR-S 1270, Sorbonne Université, Faculty of Sciences and Engineering, Institut du Fer à MoulinBioscience Program, Division of Biological and Environmental Science and Engineering (BESE), King Abdullah University of Science and Technology (KAUST)Inserm UMR-S 1270, Sorbonne Université, Faculty of Sciences and Engineering, Institut du Fer à MoulinBioscience Program, Division of Biological and Environmental Science and Engineering (BESE), King Abdullah University of Science and Technology (KAUST)Computational Bioscience Research Center (CBRC), King Abdullah University of Science and Technology (KAUST)Protein tyrosine kinase 2-beta is shown to function as a sensor and effector of cellular calcium influx through self-association.https://doi.org/10.1038/s42003-022-03760-8 |
| spellingShingle | Afaque A. Momin Tiago Mendes Philippe Barthe Camille Faure SeungBeom Hong Piao Yu Gress Kadaré Mariusz Jaremko Jean-Antoine Girault Łukasz Jaremko Stefan T. Arold PYK2 senses calcium through a disordered dimerization and calmodulin-binding element Communications Biology |
| title | PYK2 senses calcium through a disordered dimerization and calmodulin-binding element |
| title_full | PYK2 senses calcium through a disordered dimerization and calmodulin-binding element |
| title_fullStr | PYK2 senses calcium through a disordered dimerization and calmodulin-binding element |
| title_full_unstemmed | PYK2 senses calcium through a disordered dimerization and calmodulin-binding element |
| title_short | PYK2 senses calcium through a disordered dimerization and calmodulin-binding element |
| title_sort | pyk2 senses calcium through a disordered dimerization and calmodulin binding element |
| url | https://doi.org/10.1038/s42003-022-03760-8 |
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