Year: 2007
Type: article
Abstract: NEDD8 is developmentally down-regulated ubiquitin-like protein, which can conjugate covalently to their\ntarget proteins. Recently, we identifi ed NUB1 as a NEDD8-interacting protein, which is composed of 601 amino acid\nresidues with a calculated molecular mass of 69.1 kDa. More recently, we showed that NUB1 is an interferon-induced\nprotein and also recruits NEDD8 to the proteasome for degradation. Here, we performed a yeast two-hybrid screening\nusing NUB1 as bait and isolated the cDNA of synphilin-1 from a human testis cDNA library. Synphilin-1 is a major\ncomponent of inclusion bodies found in the brains of patients with α-synucleinopathies, including Parkinson’s disease.\nOur biochemical study showed that NUB1 directly interacts with synphilin-1 through its NEDD8-binding site. In\naddition, our immunohistochemical study showed that NUB1, as well as synphilin-1, accumulates in the inclusion bodies\nfound in the brains of patients with α-synucleinopathies. These fi ndings imply that NUB1 plays a role in the formation\nof synphilin-1-positive inclusions.
Language: English
Subfield: Clinical Neurology
Field: Medicine
Domain: Health Sciences
Open Access status: green
OpenAlex ID: W2183189384