dictyNews

Electronic Edition

Volume 44, number 18

July 6, 2018



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Abstracts

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SRCP1 conveys resistance to polyglutamine aggregation





Stephanie Santarriaga1, Holly N. Haver1, Adam J. Kanack1, Alicia S. Fikejs1, 

Samantha L. Sison2, John M. Egner1, Jonathan R. Bostrom2, Emily R. 

Seminary2, R. Blake Hill1, Brian A. Link2, Allison D. Ebert2, & 

K. Matthew Scaglione1,3,*



1Department of Biochemistry and the Neuroscience Research Center, 

Medical College of Wisconsin, Milwaukee, Wisconsin 53226, USA

2Department of Cell Biology, Neurobiology, and Anatomy, Medical College 

of Wisconsin, Milwaukee, Wisconsin 53226, USA

3Lead Contact



*For correspondence: [log in to unmask]





Molecular Cell, accepted



The polyglutamine (polyQ) diseases are a group of nine neurodegenerative 

diseases caused by the expansion of a polyQ tract that results in protein 

aggregation. Unlike other model organisms Dictyostelium discoideum is a 

proteostatic outlier, naturally encoding long polyQ tracts yet resistant to polyQ 

aggregation. Here we identify serine-rich chaperone protein 1 (SRCP1) as a 

novel molecular chaperone that is necessary and sufficient to suppress polyQ 

aggregation. SRCP1 inhibits aggregation of polyQ-expanded proteins allowing 

for their degradation via the proteasome where SRCP1 is also degraded. 

SRCP1’s C-terminal domain is essential for its activity in cells, and peptides that 

mimic this domain suppress polyQ aggregation in vitro. Together our results 

identify a novel type of molecular chaperone and reveal how nature has dealt 

with the problem of polyQ aggregation.





submitted by:  Matt Scaglione  [[log in to unmask]]

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[End dictyNews, volume 44, number 18]