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Tytuł:
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Solution structure of c-FLIP death effector domains.
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Autorzy:
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Bai ZQ; State Key Laboratory of Phytochemistry and Plant Resources in West China, Kunming Institute of Botany, Chinese Academy of Sciences, 132 Lanhei Road, Heilongtan, Kunming, 650201, Yunnan, China; Innovative Institute of Chinese Medicine and Pharmacy, Chengdu University of Traditional Chinese Medicine, Chengdu, 611137, China; University of Chinese Academy of Sciences, Beijing, 100049, China.
Ma X; Innovative Institute of Chinese Medicine and Pharmacy, Chengdu University of Traditional Chinese Medicine, Chengdu, 611137, China.
Liu B; State Key Laboratory of Phytochemistry and Plant Resources in West China, Kunming Institute of Botany, Chinese Academy of Sciences, 132 Lanhei Road, Heilongtan, Kunming, 650201, Yunnan, China; University of Chinese Academy of Sciences, Beijing, 100049, China.
Huang T; State Key Laboratory of Phytochemistry and Plant Resources in West China, Kunming Institute of Botany, Chinese Academy of Sciences, 132 Lanhei Road, Heilongtan, Kunming, 650201, Yunnan, China; University of Chinese Academy of Sciences, Beijing, 100049, China.
Hu K; State Key Laboratory of Phytochemistry and Plant Resources in West China, Kunming Institute of Botany, Chinese Academy of Sciences, 132 Lanhei Road, Heilongtan, Kunming, 650201, Yunnan, China; Innovative Institute of Chinese Medicine and Pharmacy, Chengdu University of Traditional Chinese Medicine, Chengdu, 611137, China. Electronic address: .
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Źródło:
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Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2022 Aug 30; Vol. 617 (Pt 2), pp. 1-6. Date of Electronic Publication: 2022 May 29.
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Typ publikacji:
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Journal Article; Research Support, Non-U.S. Gov't
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Język:
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English
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Imprint Name(s):
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Publication: <2002- >: San Diego, CA : Elsevier
Original Publication: New York, Academic Press.
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MeSH Terms:
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CASP8 and FADD-Like Apoptosis Regulating Protein*/metabolism
Death Effector Domain*
Apoptosis ; Caspase 8/metabolism ; Signal Transduction
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Contributed Indexing:
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Keywords: Anti-apoptosis; Death effector domains; c-FLIP
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Substance Nomenclature:
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0 (CASP8 and FADD-Like Apoptosis Regulating Protein)
EC 3.4.22.- (Caspase 8)
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Entry Date(s):
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Date Created: 20220610 Date Completed: 20220621 Latest Revision: 20220727
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Update Code:
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20240105
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DOI:
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10.1016/j.bbrc.2022.05.086
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PMID:
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35688044
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The formation of death-inducing signaling complex (DISC) and death effector domain (DED) filament initiates extrinsic apoptosis. Recruitment and activation of procaspase-8 at the DISC are regulated by c-FLIP. The interaction between c-FLIP and procaspase-8 is mediated by their tandem DEDs (tDED). However, the structure of c-FLIP tDED and how c-FLIP interferes with procaspase-8 activation at the DISC remain elusive. Here, we solved the monomeric structure of c-FLIP tDED (F114G) at near physiological pH by solution nuclear magnetic resonance (NMR). Structural superimposition reveals c-FLIP tDED (F114G) adopts a structural topology similar to that of procaspase-8 tDED . Our results provide a structural basis for understanding how c-FLIP interacts with procaspase-8 and the molecular mechanisms of c-FLIP in regulating cell death.
Competing Interests: Declaration of competing interest The authors declare no conflict of interest.
(Copyright © 2022 Elsevier Inc. All rights reserved.)
