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Check out our latest paper on @biorxivpreprint!
Phosphorylation of the overlooked #tyrosine 310 regulates the structure, #aggregation, and #microtubule- and #lipid-binding properties of #Tau
biorxiv.org/content/10.110…
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#AcademicTwitter #biochemistry #threadstory
Phosphorylation of the overlooked #tyrosine 310 regulates the structure, #aggregation, and #microtubule- and #lipid-binding properties of #Tau
biorxiv.org/content/10.110…
Short #thread!
#AcademicTwitter #biochemistry #threadstory
Tau misfolding and aggregation are implicated in tauopathies such as #Alzheimers and #PSP. Tau is extensively post-translationally modified and aberrant pattern of PTMs are found in disease. Tyrosine PTMs have received the least attention, especially Y310.
Tau has 5 tyrosines, and Y310 is in the crucial position within the aggregation-prone MT- and lipid-binding repeat domain. It compacts and folds into beta-sheet structure. We asked:
How would addition of bulky negatively charged phosphogroups to tyrosines impact Tau properties?
How would addition of bulky negatively charged phosphogroups to tyrosines impact Tau properties?
