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Fig. 10 | Cell & Bioscience

Fig. 10

From: Siah-1-interacting protein regulates mutated huntingtin protein aggregation in Huntington’s disease models

Fig. 10

Dysregulation of SIP dimer/monomer ratio decreases SIP activity in the ubiquitination of mHTT, causing an increase in its aggregation. SIP functions as a regulator of mutant huntingtin (mHTT) protein levels by supporting mHTT ubiquitination (Ub) for its further degradation in the proteasome (P). During the progression of Huntington’s disease (HD), based on the presence of mHTT, dysregulation of the SIP dimer/monomer ratio occurs, leading to lower SIP activity in the ubiquitination of mHTT (dashed arrow) and a decrease in the degradation of mHTT in proteasomes, resulting in an increase in the aggregation of mHTT in HD MSNs

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Cell & Bioscience

ISSN: 2045-3701

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