Ubiquitin is conjugated with amino-terminally processed tau in paired helical filaments.

Abstract:

:We have investigated ubiquitinated paired helical filaments, which produce a proteinaceous smear in SDS-polyacrylamide gel electrophoresis and immunoblotting. The smear consisted largely of the carboxy-terminal portion of tau and ubiquitin. The ubiquitin-targeted protein was identified as tau in paired helical filaments, and the conjugation sites were localized to the microtubule-binding region. Most ubiquitin in paired helical filaments occurred as a monoubiquitinated form, and only a small proportion of ubiquitin formed multiubiquitin chains. There was a ubiquitin-negative smear, in which tau was much less processed in the amino-terminal portion. This strongly suggests that the amino-terminal processing of tau in paired helical filaments precedes its ubiquitination.

journal_name

Neuron

journal_title

Neuron

authors

Morishima-Kawashima M,Hasegawa M,Takio K,Suzuki M,Titani K,Ihara Y

doi

10.1016/0896-6273(93)90063-w

subject

Has Abstract

pub_date

1993-06-01 00:00:00

pages

1151-60

issue

6

eissn

0896-6273

issn

1097-4199

pii

0896-6273(93)90063-W

journal_volume

10

pub_type

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