The abstract mentions that CMA requires KFERQ-like motifs for substrate recognition and that mutant Htt with expanded polyglutamine is a CMA substrate, but doesn't explain how the pathogenic expansion influences motif accessibility or chaperone binding. This mechanistic gap is crucial for understanding CMA efficiency in disease. Gap type: unexplained_observation Source paper: Role of chaperone-mediated autophagy in degrading Huntington's disease-associated huntingtin protein. (2014, Acta biochimica et biophysica Sinica, PMID:24323530)
Landscape Summary: How does polyglutamine expansion affect huntingtin's KFERQ-like motif recognition by CMA machinery? is a 0.76 priority gap in neurodegeneration. It has 0 linked hypotheses with average composite score 0.000. Status: open.
Colonna, Sevlever, et al. (TREM2 biology)
How does polyglutamine expansion affect huntingtin's KFERQ-like motif recognition by CMA machinery? — INVOKE-2 (completed)
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