The presumptive altered dynamics of transient molecular interactions in vivo contributing to neurodegenerative diseases have remained elusive. Here, using single-molecule localization microscopy, we show that disease-inducing Huntingtin (mHtt) protein fragments display three distinct dynamic states in living cells - 1) fast diffusion, 2) dynamic clustering and 3) stable aggregation. Large, stable aggregates of mHtt exclude chromatin and form 'sticky' decoy traps that impede target search processes of key regulators involved in neurological disorders. Functional domain mapping based on super-resolution imaging reveals an unexpected role of aromatic amino acids in promoting protein-mHtt aggregate interactions. Genome-wide expression analysis and numerical simulation experiments suggest mHtt aggregates reduce transcription factor target site sampling frequency and impair critical gene expression programs in striatal neurons. Together, our results provide insights into how mHtt dynamically forms aggregates and disrupts the finely-balanced gene control mechanisms in neuronal cells.
Keyphrases
- single molecule
- living cells
- genome wide
- transcription factor
- genome wide identification
- amino acid
- high resolution
- gene expression
- dna methylation
- atomic force microscopy
- copy number
- cerebral ischemia
- fluorescent probe
- induced apoptosis
- dna binding
- public health
- spinal cord
- binding protein
- functional connectivity
- cell proliferation
- high speed
- subarachnoid hemorrhage
- small molecule
- photodynamic therapy
- signaling pathway
- endoplasmic reticulum stress