Date Thesis Awarded

5-2021

Access Type

Honors Thesis -- Access Restricted On-Campus Only

Degree Name

Bachelors of Science (BS)

Department

Biology

Advisor

Shanta D. Hinton

Committee Members

Kurt Williamson

Matthias Leu

Ryan Vinroot

Abstract

MK-STYX [mitogen-activated protein kinase phospho-serine/threonine/tyrosine binding protein] is a pseudophosphatase and a member of the MAP kinase phosphatase family. Due to the absence of cysteine and histidine residues in the signature active site motif (HCX5R), MK-STYX is catalytically inactive. Even so, it maintains the ability to bind phosphorylated residues. MK-STYX is an important molecule in various signaling pathways, including the stress response pathway. Our previous research showed that the expression of MK-STYX decreases stress granules [SG], which are aggregates of untranslated mRNA and misfolded proteins caused by cellular stress. However, the molecular mechanism by which MK-STYX decreases SG remains elusive. Histone deacetylase isoform 6 (HDAC6) serves as a major component of SG. Therefore, we investigated whether MK-STYX affects the dynamics of HDAC6. Our previous findings showed that MK-STYX alters the subcellular localization of HDC6, which became nuclear, and decreased and altered the location of HDAC6-aggregates. Because HDAC6 contains a ubiquitin binding domain, we investigated whether MK-STYX affects the interaction of HDAC6 and ubiquitin. The current study found that neither MK-STYX nor MK-STYXactive mutant affected the total expression of HDAC6 under any of the experimental conditions, and similarly, they did not affect the interactions of HDAC6 and ubiquitin. Understanding the mechanism by which MK-STYX decreases stress granules can contribute to the development of treatments for neurodegenerative diseases, which often have stress granules as a pathology.

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