Cell Biology

Recruitment Centers

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Science  19 Jul 2002:
Vol. 297, Issue 5580, pp. 303
DOI: 10.1126/science.297.5580.303c

A variety of neurodegenerative disorders involve the misfolding and aggregation of proteins carrying tracts of polyglutamine. Using fluorescent imaging in living cells, Chai et al. studied the dynamic properties of polyglutamine proteins. Different proteins exhibited very different mobilities and propensities to form mixed aggregates. For example, ataxin-3 (the mutated protein in spinocerebellar ataxia type 3) formed aggregated nuclear inclusions, which could recruit the cAMP response element binding protein (CBP). Similarly, huntingtin (mutated in Huntington's disease) formed common aggregates with CBP in the nucleus. However, cells expressing another polyglutamine protein, ataxin-1, did not recruit CBP to immobile protein aggregates. A variety of components of the nuclear transcription machinery may therefore be differentially recruited to nuclear inclusions in different diseases, presumably accounting for some of the distinct pathologies observed. — SMH

Proc. Natl. Acad. Sci. U.S.A.99, 9310 (2002).

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