Better Together: A Hybrid Amyloid Signals Necroptosis

Dan Li; Cong Liu

doi:10.1016/j.cell.2018.04.030

Better Together: A Hybrid Amyloid Signals Necroptosis

Cell. 2018 May 17;173(5):1068-1070. doi: 10.1016/j.cell.2018.04.030.

Authors

Dan Li¹, Cong Liu²

Affiliations

¹ Bio-X Institutes, Key Laboratory for the Genetics of Developmental and Neuropsychiatric Disorders, Ministry of Education, Shanghai Jiao Tong University, Shanghai 200230, China. Electronic address: lidan2017@sjtu.edu.cn.
² Interdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai 201210, China. Electronic address: liulab@sioc.ac.cn.

PMID: 29775589
DOI: 10.1016/j.cell.2018.04.030

Abstract

A new solid-state NMR study determines the high-resolution hetero-amyloid structure of the RIPK1-RIPK3 signaling complex that is involved in mediating necroptosis. The structure demonstrates specific formation of hetero-amyloids over homo-amyloids and the structural basis for a functional amyloid to act as a platform to recruit and activate downstream partners in intracellular signaling.

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MeSH terms

Amyloidogenic Proteins
Apoptosis
Humans
Necrosis*
Receptor-Interacting Protein Serine-Threonine Kinases*
Signal Transduction
Tumor Necrosis Factor-alpha

Substances

Amyloidogenic Proteins
Tumor Necrosis Factor-alpha
RIPK1 protein, human
RIPK3 protein, human
Receptor-Interacting Protein Serine-Threonine Kinases