14-3-3 proteins inactivate DAPK2 by promoting its dimerization and protecting key regulatory phosphosites

Horvath et al. structurally and biochemically characterize the full-length human DAPK2-14-3-3 complex to investigate the effects of binding to DAPK2 on its dimerization, activation by dephosphorylation of Ser318, and Ca2+/calmodulin binding. Their results provide mechanistic insights into 14- 3-3-me...

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Autores principales:	Matej Horvath, Olivia Petrvalska, Petr Herman, Veronika Obsilova, Tomas Obsil
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/b760ecb751c143968c2d8af2223e83c8
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spelling	oai:doaj.org-article:b760ecb751c143968c2d8af2223e83c82021-12-02T18:51:45Z14-3-3 proteins inactivate DAPK2 by promoting its dimerization and protecting key regulatory phosphosites10.1038/s42003-021-02518-y2399-3642https://doaj.org/article/b760ecb751c143968c2d8af2223e83c82021-08-01T00:00:00Zhttps://doi.org/10.1038/s42003-021-02518-yhttps://doaj.org/toc/2399-3642Horvath et al. structurally and biochemically characterize the full-length human DAPK2-14-3-3 complex to investigate the effects of binding to DAPK2 on its dimerization, activation by dephosphorylation of Ser318, and Ca2+/calmodulin binding. Their results provide mechanistic insights into 14- 3-3-mediated DAPK2 inhibition and highlight the potential of the DAPK2:14-3-3 complex as a target for anti-inflammatory therapies.Matej HorvathOlivia PetrvalskaPetr HermanVeronika ObsilovaTomas ObsilNature PortfolioarticleBiology (General)QH301-705.5ENCommunications Biology, Vol 4, Iss 1, Pp 1-14 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Matej Horvath Olivia Petrvalska Petr Herman Veronika Obsilova Tomas Obsil 14-3-3 proteins inactivate DAPK2 by promoting its dimerization and protecting key regulatory phosphosites
description	Horvath et al. structurally and biochemically characterize the full-length human DAPK2-14-3-3 complex to investigate the effects of binding to DAPK2 on its dimerization, activation by dephosphorylation of Ser318, and Ca2+/calmodulin binding. Their results provide mechanistic insights into 14- 3-3-mediated DAPK2 inhibition and highlight the potential of the DAPK2:14-3-3 complex as a target for anti-inflammatory therapies.
format	article
author	Matej Horvath Olivia Petrvalska Petr Herman Veronika Obsilova Tomas Obsil
author_facet	Matej Horvath Olivia Petrvalska Petr Herman Veronika Obsilova Tomas Obsil
author_sort	Matej Horvath
title	14-3-3 proteins inactivate DAPK2 by promoting its dimerization and protecting key regulatory phosphosites
title_short	14-3-3 proteins inactivate DAPK2 by promoting its dimerization and protecting key regulatory phosphosites
title_full	14-3-3 proteins inactivate DAPK2 by promoting its dimerization and protecting key regulatory phosphosites
title_fullStr	14-3-3 proteins inactivate DAPK2 by promoting its dimerization and protecting key regulatory phosphosites
title_full_unstemmed	14-3-3 proteins inactivate DAPK2 by promoting its dimerization and protecting key regulatory phosphosites
title_sort	14-3-3 proteins inactivate dapk2 by promoting its dimerization and protecting key regulatory phosphosites
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/b760ecb751c143968c2d8af2223e83c8
work_keys_str_mv	AT matejhorvath 1433proteinsinactivatedapk2bypromotingitsdimerizationandprotectingkeyregulatoryphosphosites AT oliviapetrvalska 1433proteinsinactivatedapk2bypromotingitsdimerizationandprotectingkeyregulatoryphosphosites AT petrherman 1433proteinsinactivatedapk2bypromotingitsdimerizationandprotectingkeyregulatoryphosphosites AT veronikaobsilova 1433proteinsinactivatedapk2bypromotingitsdimerizationandprotectingkeyregulatoryphosphosites AT tomasobsil 1433proteinsinactivatedapk2bypromotingitsdimerizationandprotectingkeyregulatoryphosphosites
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14-3-3 proteins inactivate DAPK2 by promoting its dimerization and protecting key regulatory phosphosites

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