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蓝光揭示了单个磷酸丝氨酸在 CFTR 通道激活中的作用。

Blue flash sheds light on the roles of individual phosphoserines in CFTR channel activation.

机构信息

Department of Biochemistry, Semmelweis University , Budapest, Hungary.

HCEMM-SE Molecular Channelopathies Research Group , Budapest, Hungary.

出版信息

J Gen Physiol. 2023 Jun 5;155(6). doi: 10.1085/jgp.202313336. Epub 2023 Apr 5.

Abstract

Light-controlled availability for phosphorylation reveals dominant roles of select R-domain serines in CFTR channel activation.

摘要

光控磷酸化可用性揭示了选择的 CFTR 通道激活 R 域丝氨酸的主要作用。

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本文引用的文献

1
Real-time observation of functional specialization among phosphorylation sites in CFTR.
J Gen Physiol. 2023 Apr 3;155(4). doi: 10.1085/jgp.202213216. Epub 2023 Jan 25.
2
Simple binding of protein kinase A prior to phosphorylation allows CFTR anion channels to be opened by nucleotides.
Proc Natl Acad Sci U S A. 2020 Sep 1;117(35):21740-21746. doi: 10.1073/pnas.2007910117. Epub 2020 Aug 17.
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Useful Caged Compounds for Cell Physiology.
Acc Chem Res. 2020 Aug 18;53(8):1593-1604. doi: 10.1021/acs.accounts.0c00292. Epub 2020 Jul 21.
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An Ancient CFTR Ortholog Informs Molecular Evolution in ABC Transporters.
Dev Cell. 2019 Nov 18;51(4):421-430.e3. doi: 10.1016/j.devcel.2019.09.017. Epub 2019 Oct 31.
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CFTR channel opening by ATP-driven tight dimerization of its nucleotide-binding domains.
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Preferential phosphorylation of R-domain Serine 768 dampens activation of CFTR channels by PKA.
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