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final blog

Thus far, Dr. Emtage and I were able to conclude the molecular chaperone, Hsp42, helps to target and metabolize mutant Huntingtin protein aggregates in S. cerevisiea models. What we have set out to do has been successful! There is very literature out now which elaborates on Hsp42′s, in particular, role in processing mutant Huntingtin.

Currently, Dr. Emtage has pushed our research even deeper.  We are now working on figuring out how Hsp42 proteins localize within the cells. To do this, we are attempting to label specific proteins associated with the spindle pole body (SPB), such as Spc42, with a fluorescent protein( FP) in order to image both the SPB and Hsp42 proteins. This will allow use to determine if Hsp42 does move about the cytoplasm using the SPB. We are currently looking at other SPB proteins to label with FP as well.

I am currently working on making ¬†inducible mutant Huntingtin plasmids with polyglutamine lengths of 25Q (control) and 72Q (pathogenic) controlled under a GAL1 promoter. This will allow us to essentially mediate the amount of Huntingtin protein aggregates generated within the cells. Our current Huntingtin plasmids use a constitutive promoter, GPD, which means the Huntingtin is always expressed. With a GAL1 promoter, we will be able to “switch on and off” Huntingtin expression. With these new plasmids, we hope to investigate how aggregates are processed and in what amount of time within our models. Doing this in conjunction with FP labeling certain proteosome proteins will hopefully allow use to determine the individual steps of mutant Huntingtin metabolism or catabolism. The hypothesis here is the Huntingtin aggregates are targeted by Hsp42 either for re-folding or ubiquitination. We hope to determine which one to be the case very soon.

This will be my last blog. Thank you for reading and thank you Pace University for allowing this research to reach this point.

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