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- Title
Demonstration of a role for α-synuclein as a functional microtubule-associated protein.
- Authors
Abdul Alim, Muhammad; Qiu-Lan Ma; Takeda, Kazuya; Aizawa, Takako; Matsubara, Mamoru; Nakamura, Minako; Asada, Akiko; Saito, Taro; Kaji, Hiroyuki; Yoshii, Mitsunobu; Hisanaga, Shinichi; Uéda, Kenji
- Abstract
α-Synuclein is a major constituent of pathological intracellular inclusion bodies, a common feature of several neurodegenerative diseases. Two missense mutations in the α-synuclein gene have been identified in confirmed autosomal-dominant familial Parkinson's disease, which segregate with the illness. However, the physiological function of α-synuclein remains unknown. After biochemical investigations we have revealed tubulin to be an α-synuclein associated/binding protein. Here, we show that α-synuclein induces polymerization of purified tubulin into microtubules. Mutant forms of α-synuclein lose this potential. The binding site of α-synuclein to tubulin is identified, and co-localization of α-synuclein with microtubules is shown in cultured cells. To our knowledge, this is the first demonstration of microtubule-polymerizing activity of α-synuclein. Now we can see a striking resemblance between α-synuclein and tau: both have the same physiological function and pathological features, making abnormal structures in diseased brains known as synucleinopathies and tauopathies. The discovery of a physiological role for α-synuclein may provide a new dimension in researches into the mechanisms of α-synuclein-associated neurodegenerative diseases.
- Publication
Journal of Alzheimer's Disease, 2004, Vol 6, Issue 4, p435
- ISSN
1387-2877
- Publication type
Academic Journal
- DOI
10.3233/JAD-2004-6412