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SRCP1 Conveys Resistance to Polyglutamine Aggregation.

Mol. Cell. 2019; 
SantarriagaStephanie,HaverHolly N,KanackAdam J,FikejsAlicia S,SisonSamantha L,EgnerJohn M,BostromJonathan R,SeminaryEmily R,HillR Blake,LinkBrian A,EbertAllison D,ScaglioneK Mat
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Peptide Synthesis e1–e7, July 19, 2018 e1 Continued REAGENT or RESOURCE SOURCE IDENTIFIER SRCP1 Peptide Amino Acids 71–80 GenScript N/A SRCP1 Peptide Amino Acids 61–70 V65, I69A GenScript N/A Critical Commercial Assays Pierce BCA Protein Assay Kit ThermoFisher Scientific 23225 CellTiter-Glo Kit Promega G7570 Experimental Models: Cell Lines Human Embryonic Kidney Cells ATCC CRL-1573; RRID:CVCL_0045 Control hiPSC Allison Ebert; Schwab et al.... Briefly, 15 mM Htt46Q was mixed with 90 mM SRCP1 peptide (GenScript) (1:6, 1:3, 1:1. Get A Quote

摘要

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 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 po... More

关键词

Dictyostelium discoideum,Huntington's disease,amyloid,chaperone,polyglutamine,proteasome,ubiqu
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