NMNAT2 Functions as Chaperone Protein in Complex with HSP90

Many neurodegenerative diseases are associated with accumulation of pathological protein aggregates, which wreak havoc in the cells. Identification of cellular mechanisms for protection against protein misfolding and aggregation can yield insight on what goes awry in disease, and how to protect the cell from damage. In the June 2 PLOS Biology, a team of researcher, led by Hui-Chen Lu from Indiana University in Bloomington, describe a chaperone function for NMNAT2, an enzyme known for its role in synthesis of nicotinamide adenine dinucleotide (NAD) and protection from excitotoxic stress. NMNAT2 form as complex with heat shock protein 90 (HSP90) that promotes folding of protein aggregates, and can toggle between different neuroprotective functions in a context-dependent manner. NMNAT2 could merit exploration in the context of ALS, as approaches to potentiate the heat shock response are under investigation in the lab and the clinic (see Oct 2011 news,  March 2016 news).

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Primary Reference:
Ali Y, Allen HM, Yu L, Li-Kroeger D, Bakhshizadehmahmoudi D, Hatcher A, McCabe C, Xu J, Bjorklund N, Taglialatela G, Bennett DA, De Jager PL, Shulman JM, Bellen HJ, Lu HC. NMNAT2:HSP90 Complex Mediates Proteostasis in Proteinopathies. PLoS Biol. 2016 Jun 2;14(6):e1002472.[Pubmed]

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