Noncanonical transnitrosylation network contributes to synapse loss in Alzheimer’s disease | Zendy

Tomohiro Nakamura | Zendy; Chang-ki Oh | Zendy; Lujian Liao | Zendy; Xu Zhang | Zendy; Kevin Lopez | Zendy; Daniel Gibbs | Zendy; Amanda K. Deal | Zendy; Henry Scott | Zendy; Brian Spencer | Zendy; Eliezer Masliah | Zendy; Robert A. Rissman | Zendy; John R. Yates | Zendy; Stuart A. Lipton | Zendy

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Noncanonical transnitrosylation network contributes to synapse loss in Alzheimer’s disease

Author(s) -

Tomohiro Nakamura,

Chang-ki Oh,

Lujian Liao,

Xu Zhang,

Kevin Lopez,

Daniel Gibbs,

Amanda K. Deal,

Henry Scott,

Brian Spencer,

Eliezer Masliah,

Robert A. Rissman,

John R. Yates,

Stuart A. Lipton

Publication year - 2020

Publication title -

science

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 12.556

H-Index - 1186

eISSN - 1095-9203

pISSN - 0036-8075

DOI - 10.1126/science.aaw0843

Subject(s) - s nitrosylation , neuroscience , cyclin dependent kinase 5 , nitric oxide , alzheimer's disease , disease , biology , microbiology and biotechnology , loss function , dynamin , chemistry , enzyme , kinase , biochemistry , medicine , cysteine , receptor , protein kinase a , endocrinology , gene , phenotype , mitogen activated protein kinase kinase , endocytosis

A cascade of NO in Alzheimer's disease One of the ill effects of the amyloid-β peptide that accumulates in Alzheimer's disease (AD) is the promotion of the production of nitric oxide (NO) and consequent nitrosylation of thiols in proteins such as dynamin-related protein 1 (Drp1), which can lead to loss of neuronal synapses. Nakamuraet al. found that this S-nitrosylation occurs in an unusual way. They detected a series of transnitrosylation events in which an NO group is passed between at least three proteins. The deubiquinating enzyme Uch-L1 was S-nitrosylated in brains from human AD patients or in mouse models of AD. Uch-L1 could lead to S-nitrosylation of Drp1 after transferring the NO group to another enzyme, Cdk5 (cyclin-dependent kinase 5). The results implicate a mechanism in which unrelated enzymes might aberrantly function together to disrupt brain function.Science , this issue p.eaaw0843

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