Literature DB >> 11698390

Tubulin seeds alpha-synuclein fibril formation.

Muhammad Abdul Alim1, Mosammat Shahanara Hossain, Kunimasa Arima, Kazuya Takeda, Yoko Izumiyama, Minako Nakamura, Hiroyuki Kaji, Tomotaka Shinoda, Shinichi Hisanaga, Kenji Ueda.   

Abstract

Increasing evidence suggests that alpha-synuclein is a common pathogenic molecule in several neurodegenerative diseases, particularly in Parkinson's disease. To understand alpha-synuclein pathology, we investigated molecules that interact with alpha-synuclein in human and rat brains and identified tubulin as an alpha-synuclein binding/associated protein. Tubulin co-localized with alpha-synuclein in Lewy bodies and other alpha-synuclein-positive pathological structures. Tubulin initiated and promoted alpha-synuclein fibril formation under physiological conditions in vitro. These findings suggest that an interaction between tubulin and alpha-synuclein might accelerate alpha-synuclein aggregation in diseased brains, leading to the formation of Lewy bodies.

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Year:  2001        PMID: 11698390     DOI: 10.1074/jbc.M102981200

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  59 in total

1.  LRRK2 function on actin and microtubule dynamics in Parkinson disease.

Authors:  Loukia Parisiadou; Huaibin Cai
Journal:  Commun Integr Biol       Date:  2010-09

2.  A pilot trial of the microtubule-interacting peptide (NAP) in mice overexpressing alpha-synuclein shows improvement in motor function and reduction of alpha-synuclein inclusions.

Authors:  Sheila M Fleming; Caitlin K Mulligan; Franziska Richter; Farzad Mortazavi; Vincent Lemesre; Carmen Frias; Chunni Zhu; Alistair Stewart; Illana Gozes; Bruce Morimoto; Marie-Françoise Chesselet
Journal:  Mol Cell Neurosci       Date:  2010-12-27       Impact factor: 4.314

3.  Role of gamma-synuclein in microtubule regulation.

Authors:  Hong Zhang; Ange Kouadio; Donna Cartledge; Andrew K Godwin
Journal:  Exp Cell Res       Date:  2010-10-23       Impact factor: 3.905

4.  The Roc domain of leucine-rich repeat kinase 2 is sufficient for interaction with microtubules.

Authors:  Payal N Gandhi; Xinglong Wang; Xiongwei Zhu; Shu G Chen; Amy L Wilson-Delfosse
Journal:  J Neurosci Res       Date:  2008-06       Impact factor: 4.164

5.  Molecular interaction of α-synuclein with tubulin influences on the polymerization of microtubule in vitro and structure of microtubule in cells.

Authors:  R M Zhou; Y X Huang; X L Li; C Chen; Q Shi; G R Wang; C Tian; Z Y Wang; Y Y Jing; C Gao; X P Dong
Journal:  Mol Biol Rep       Date:  2009-10-14       Impact factor: 2.316

6.  β-III Tubulin fragments inhibit α-synuclein accumulation in models of multiple system atrophy.

Authors:  Yasuyo Suzuki; Chenghua Jin; Tamaki Iwase; Ikuru Yazawa
Journal:  J Biol Chem       Date:  2014-07-15       Impact factor: 5.157

Review 7.  Microtubule Destabilization Paves the Way to Parkinson's Disease.

Authors:  D Cartelli; G Cappelletti
Journal:  Mol Neurobiol       Date:  2016-10-18       Impact factor: 5.590

8.  α-Synuclein can inhibit SNARE-mediated vesicle fusion through direct interactions with lipid bilayers.

Authors:  David C DeWitt; Elizabeth Rhoades
Journal:  Biochemistry       Date:  2013-03-27       Impact factor: 3.162

9.  Microtubule depolymerization potentiates alpha-synuclein oligomerization.

Authors:  A Raquel Esteves; Daniela M Arduíno; Russell H Swerdlow; Catarina R Oliveira; Sandra M Cardoso
Journal:  Front Aging Neurosci       Date:  2010-01-04       Impact factor: 5.750

10.  Cross-talk between mitochondria and proteasome in Parkinson's disease pathogenesis.

Authors:  Diogo Martins Branco; Daniela M Arduino; A Raquel Esteves; Diana F F Silva; Sandra M Cardoso; Catarina Resende Oliveira
Journal:  Front Aging Neurosci       Date:  2010-05-21       Impact factor: 5.750

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