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Direct cellular delivery of human proteasomes to delay tau aggregation.

Abstract：

:The 26S proteasome is the primary machinery that degrades ubiquitin (Ub)-conjugated proteins, including many proteotoxic proteins implicated in neurodegeneraton. It has been suggested that the elevation of proteasomal activity is tolerable to cells and may be beneficial to prevent the accumulation of protein aggregates. Here we show that purified proteasomes can be directly transported into cells through mesoporous silica nanoparticle-mediated endocytosis. Proteasomes that are loaded onto nanoparticles through non-covalent interactions between polyhistidine tags and nickel ions fully retain their proteolytic activity. Cells treated with exogenous proteasomes are more efficient in degrading overexpressed human tau than endogenous proteasomal substrates, resulting in decreased levels of tau aggregates. Moreover, exogenous proteasome delivery significantly promotes cell survival against proteotoxic stress caused by tau and reactive oxygen species. These data demonstrate that increasing cellular proteasome activity through the direct delivery of purified proteasomes may be an effective strategy for reducing cellular levels of proteotoxic proteins.

journal_name

Nat Commun

journal_title

Nature communications

authors

Han DH,Na HK,Choi WH,Lee JH,Kim YK,Won C,Lee SH,Kim KP,Kuret J,Min DH,Lee MJ

doi

10.1038/ncomms6633

subject

Has Abstract

pub_date

2014-12-05 00:00:00

pages

5633

issn

2041-1723

pii

ncomms6633

journal_volume

5

pub_type

杂志文章

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