کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
3070793 1580742 2007 11 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
α-Synuclein and its disease-related mutants interact differentially with the microtubule protein tau and associate with the actin cytoskeleton
موضوعات مرتبط
علوم زیستی و بیوفناوری علم عصب شناسی عصب شناسی
پیش نمایش صفحه اول مقاله
α-Synuclein and its disease-related mutants interact differentially with the microtubule protein tau and associate with the actin cytoskeleton
چکیده انگلیسی

α-Synuclein is a primarily neuronal protein that is enriched at the pre-synapse. α-Synuclein and the microtubule binding protein tau have been implicated in neurodegenerative diseases. α-Synuclein is known to associate with phospholipid vesicles, regulates dopamine metabolism and exhibits chaperone activity, but its main role remains largely unknown. Furthermore, knowledge on its interactions and post-translational modifications is essential for a molecular understanding of α-synucleinopathies.We investigated α-synuclein mutations, causative for autosomal dominant forms of Parkinson’s disease (A30P, A53T and E46K), and phosphorylation mutants at serine 129 (S129A and S129D) using fluorescently labelled α-synuclein, actin and tau.The investigation of colocalization, and protein–protein interactions by Förster resonance energy transfer and fluorescence lifetime imaging showed that α-synuclein associates with the actin cytoskeleton and interacts with tau. The A30P mutation and cytoskeletal destabilization decreased this interaction. Given the concurrent loss of membrane binding by this mutation, we propose a membrane-bound functional complex with tau that might involve the actin cytoskeleton.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Neurobiology of Disease - Volume 26, Issue 3, June 2007, Pages 521–531
نویسندگان
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