Kinase domain dimerization drives RIPK3-dependent necroptosis-Reference-Cited by-同舟云学术

Kinase domain dimerization drives RIPK3-dependent necroptosis

Published:2018-08-21 Issue:544 Volume:11 Page:
ISSN:1945-0877
Container-title:Science Signaling
language:en
Short-container-title:Sci. Signal.

Author:

Raju Saravanan¹,Whalen Daniel M.²,Mengistu Meron³,Swanson Carter³,Quinn John G.⁴^ORCID,Taylor Susan S.⁵^ORCID,Webster Joshua D.⁶,Newton Kim⁷,Shaw Andrey S.¹³^ORCID

Affiliation:

1. Department of Pathology and Immunology, Washington University School of Medicine, St. Louis, MO 63110, USA.

2. Department of Structural Biology, Genentech, South San Francisco, CA 94080, USA.

3. Department of Research Biology, Genentech, South San Francisco, CA 94080, USA.

4. Department of Biochemical and Cellular Pharmacology, Genentech, South San Francisco, CA 94080, USA.

5. Departments of Chemistry/Biochemistry and Pharmacology, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093, USA.

6. Department of Pathology, Genentech, South San Francisco, CA 94080, USA.

7. Department of Physiological Chemistry, Genentech, South San Francisco, CA 94080, USA.

Abstract

Necroptotic cell death is promoted by the dimerization-dependent activation of the kinase RIPK3.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference47 articles.

1. Phosphorylation-Driven Assembly of the RIP1-RIP3 Complex Regulates Programmed Necrosis and Virus-Induced Inflammation

2. Mixed Lineage Kinase Domain-like Protein MLKL Causes Necrotic Membrane Disruption upon Phosphorylation by RIP3

3. A helix scaffold for the assembly of active protein kinases

4. Dynamics-Driven Allostery in Protein Kinases

5. An Allosteric Mechanism for Activation of the Kinase Domain of Epidermal Growth Factor Receptor

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