Identifying polyglutamine protein species in situ that best predict neurodegeneration

Jason Miller, Montserrat Arrasate, Elizabeth Brooks, Clare Peters Libeu, Justin Legleiter, Danny Hatters, Jessica Curtis, Kenneth Cheung, Preethi Krishnan, Siddhartha Mitra, Kartika Widjaja, Benjamin A. Shaby, Gregor P. Lotz, Yvonne Newhouse, Emily J. Mitchell, Alex Osmand, Michelle Gray, Vanitha Thulasiramin, Fräric Saudou, Mark SegalX. William Yang, Eliezer Masliah, Leslie M. Thompson, Paul J. Muchowski, Karl H. Weisgraber, Steven Finkbeiner

Research output: Contribution to journalArticlepeer-review

162 Scopus citations

Abstract

Polyglutamine (polyQ) stretches exceeding a threshold length confer a toxic function to proteins that contain them and cause at least nine neurological disorders. The basis for this toxicity threshold is unclear. Although polyQ expansions render proteins prone to aggregate into inclusion bodies, this may be a neuronal coping response to more toxic forms of polyQ. The exact structure of these more toxic forms is unknown. Here we show that the monoclonal antibody 3B5H10 recognizes a species of polyQ protein in situ that strongly predicts neuronal death. The epitope selectively appears among some of the many low-molecular-weight conformational states assumed by expanded polyQ and disappears in higher-molecular-weight aggregated forms, such as inclusion bodies. These results suggest that protein monomers and possibly small oligomers containing expanded polyQ stretches can adopt a conformation that is recognized by 3B5H10 and is toxic or closely related to a toxic species.

Original languageEnglish (US)
Pages (from-to)925-934
Number of pages10
JournalNature Chemical Biology
Volume7
Issue number12
DOIs
StatePublished - Dec 2011

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cell Biology

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