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Identification of ubiquitin‐interacting proteins in purified polyglutamine aggregates
Author(s) -
Doi Hiroshi,
Mitsui Kenichi,
Kurosawa Masaru,
Machida Yoko,
Kuroiwa Yoshiyuki,
Nukiobuyuki
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.06.077
Subject(s) - huntingtin , nuclear protein , ubiquitin , huntingtin protein , chemistry , mutant , microbiology and biotechnology , function (biology) , protein aggregation , nuclear localization sequence , biochemistry , biology , nucleus , transcription factor , gene
Nuclear aggregates of enhanced green fluorescent protein and nuclear localization signal‐fused truncated N‐terminal huntingtin containing 150 repeats of glutamine residue were purified from ecdysine‐inducible mutant neuro2A cell line by sequential extraction of nuclear soluble proteins. To analyze the aggregate‐interacting proteins, we subjected the nuclear aggregates to high performance liquid chromatography–mass spectrometry analysis. The resulting data revealed the presence of three new putative aggregate‐interacting proteins: ubiquilin 1, ubiquilin 2 and Tollip. These proteins also associated with neuronal intranuclear inclusions in a mouse model of Huntington disease (HD). These aggregate‐interacting proteins contain ubiquitin‐interacting motifs, suggesting that they are recruited to the aggregates where they may lose their normal function.