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Controlling Cell Death through Post-translational Modifications of DED Proteins. / Seyrek, Kamil; Ivanisenko, Nikita V.; Richter, Max et al.

In: Trends in Cell Biology, Vol. 30, No. 5, 05.2020, p. 354-369.

Research output: Contribution to journal › Review article › peer-review

Harvard

Seyrek, K, Ivanisenko, NV, Richter, M, Hillert, LK, König, C & Lavrik, IN 2020, 'Controlling Cell Death through Post-translational Modifications of DED Proteins', Trends in Cell Biology, vol. 30, no. 5, pp. 354-369. https://doi.org/10.1016/j.tcb.2020.02.006

APA

Seyrek, K., Ivanisenko, N. V., Richter, M., Hillert, L. K., König, C., & Lavrik, I. N. (2020). Controlling Cell Death through Post-translational Modifications of DED Proteins. Trends in Cell Biology, 30(5), 354-369. https://doi.org/10.1016/j.tcb.2020.02.006

Vancouver

Seyrek K, Ivanisenko NV, Richter M, Hillert LK, König C, Lavrik IN. Controlling Cell Death through Post-translational Modifications of DED Proteins. Trends in Cell Biology. 2020 May;30(5):354-369. doi: 10.1016/j.tcb.2020.02.006

Author

Seyrek, Kamil ; Ivanisenko, Nikita V. ; Richter, Max et al. / Controlling Cell Death through Post-translational Modifications of DED Proteins. In: Trends in Cell Biology. 2020 ; Vol. 30, No. 5. pp. 354-369.

BibTeX

@article{f9a0f154af3b4dbf936e96b89a6b1d6d,
title = "Controlling Cell Death through Post-translational Modifications of DED Proteins",
abstract = "Apoptosis is a form of programmed cell death, deregulation of which occurs in multiple disorders, including neurodegenerative and autoimmune diseases as well as cancer. The formation of a death-inducing signaling complex (DISC) and death effector domain (DED) filaments are critical for initiation of the extrinsic apoptotic pathway. Post-translational modifications (PTMs) of DED-containing DISC components such as FADD, procaspase-8, and c-FLIP comprise an additional level of apoptosis regulation, which is necessary to overcome the threshold for apoptosis induction. In this review we discuss the influence of PTMs of FADD, procaspase-8, and c-FLIP on DED filament assembly and cell death induction, with a focus on the 3D organization of the DED filament.",
keywords = "apoptosis, DED proteins, nitrosylation, phosphorylation, SUMOylation, ubiquitylation, EXTRINSIC APOPTOSIS, ACTIVATION, PHOSPHORYLATION, MODEL, C-FLIP, DEGRADATION, CASPASE-8, FADD, UBIQUITIN-MEDIATED REGULATION, REVEALS",
author = "Kamil Seyrek and Ivanisenko, {Nikita V.} and Max Richter and Hillert, {Laura K.} and Corinna K{\"o}nig and Lavrik, {Inna N.}",
note = "Copyright {\textcopyright} 2020 The Authors. Published by Elsevier Ltd.. All rights reserved.",
year = "2020",
month = may,
doi = "10.1016/j.tcb.2020.02.006",
language = "English",
volume = "30",
pages = "354--369",
journal = "Trends in Cell Biology",
issn = "0962-8924",
publisher = "Elsevier Ltd",
number = "5",

}

RIS

TY - JOUR

T1 - Controlling Cell Death through Post-translational Modifications of DED Proteins

AU - Seyrek, Kamil

AU - Ivanisenko, Nikita V.

AU - Richter, Max

AU - Hillert, Laura K.

AU - König, Corinna

AU - Lavrik, Inna N.

N1 - Copyright © 2020 The Authors. Published by Elsevier Ltd.. All rights reserved.

PY - 2020/5

Y1 - 2020/5

N2 - Apoptosis is a form of programmed cell death, deregulation of which occurs in multiple disorders, including neurodegenerative and autoimmune diseases as well as cancer. The formation of a death-inducing signaling complex (DISC) and death effector domain (DED) filaments are critical for initiation of the extrinsic apoptotic pathway. Post-translational modifications (PTMs) of DED-containing DISC components such as FADD, procaspase-8, and c-FLIP comprise an additional level of apoptosis regulation, which is necessary to overcome the threshold for apoptosis induction. In this review we discuss the influence of PTMs of FADD, procaspase-8, and c-FLIP on DED filament assembly and cell death induction, with a focus on the 3D organization of the DED filament.

AB - Apoptosis is a form of programmed cell death, deregulation of which occurs in multiple disorders, including neurodegenerative and autoimmune diseases as well as cancer. The formation of a death-inducing signaling complex (DISC) and death effector domain (DED) filaments are critical for initiation of the extrinsic apoptotic pathway. Post-translational modifications (PTMs) of DED-containing DISC components such as FADD, procaspase-8, and c-FLIP comprise an additional level of apoptosis regulation, which is necessary to overcome the threshold for apoptosis induction. In this review we discuss the influence of PTMs of FADD, procaspase-8, and c-FLIP on DED filament assembly and cell death induction, with a focus on the 3D organization of the DED filament.

KW - apoptosis

KW - DED proteins

KW - nitrosylation

KW - phosphorylation

KW - SUMOylation

KW - ubiquitylation

KW - EXTRINSIC APOPTOSIS

KW - ACTIVATION

KW - PHOSPHORYLATION

KW - MODEL

KW - C-FLIP

KW - DEGRADATION

KW - CASPASE-8

KW - FADD

KW - UBIQUITIN-MEDIATED REGULATION

KW - REVEALS

UR - http://www.scopus.com/inward/record.url?scp=85082821770&partnerID=8YFLogxK

U2 - 10.1016/j.tcb.2020.02.006

DO - 10.1016/j.tcb.2020.02.006

M3 - Review article

C2 - 32302548

AN - SCOPUS:85082821770

VL - 30

SP - 354

EP - 369

JO - Trends in Cell Biology

JF - Trends in Cell Biology

SN - 0962-8924

IS - 5

ER -

ID: 23949522