Identification of a protein that inhibits ubiquitination and aggregation of α-synuclein, a causative factor of Parkinson's disease
September 10, 2019
Parkinson's disease is a progressive neurodegenerative disorder characterized by loss of dopaminergic neurons in the substantia nigra and striatum of brains. α-synuclein is the causative protein of Parkinson's disease. Ubiquitinated α-synuclein aggregates in nerve cells play a central role in the development of disease. A research team at Niigata University has discovered that G3BP1 protein inhibits ubiquitination and aggregation of α-synuclein. This study suggested that the G3BP1 plays a protective role in the development of Parkinson's disease by reducing α-synuclein ubiquitination and aggregation. Therefore, G3BP1 is a promising drug target for the treatment of Parkinson's disease.
Publication Details
Title:?G3BP1 inhibits ubiquitinated protein aggregations induced by p62 and USP10
Journal:?Scientific Reports
Authors:?Sergei Anisimov, Masahiko Takahashi, Taichi Kakihana,Yoshinori Katsuragi, Hiroki Kitaura, Lu Zhang, Akiyoshi Kakita, Masahiro Fujii
DOI:?10.1038/s41598-019-46237-1
More 篮球比分直播
-
Newly discovered role of amyloid precursor protein (APP) in nuclear waste disposal
Research results
-
iPatax: a Tablet-based Tool for Quantitative Assessment of Cerebellar Ataxia
Research results
-
Scg2 drives corticospinal circuit reorganization with spinal premotor interneurons and astrocytes for motor recovery after stroke in mice.
Research results
-
A newly discovered kofun (ancient Japanese burial mound) on a forested hillslope in the Kamigiri of Nagaoka City via topographical surveying using an uncrewed aerial vehicle (UAV)
Research results