# MINDY4

## Overview
MINDY4 is a gene that encodes the protein MINDY lysine 48 deubiquitinase 4, which is a member of the MINDY family of deubiquitinating enzymes. This protein is categorized as a deubiquitinase, an enzyme that plays a pivotal role in the regulation of protein degradation pathways by specifically targeting lysine 48 (K48)-linked polyubiquitin chains. These chains are typically signals for proteasomal degradation, and the activity of MINDY lysine 48 deubiquitinase 4 is essential for maintaining cellular protein homeostasis (Snyder2021Deubiquitinating). The enzyme is characterized by a unique catalytic triad composed of cysteine, histidine, and glutamine, which facilitates its high specificity for K48 linkages, impacting cellular processes such as cell cycle regulation, DNA repair, and signal transduction (Snyder2021Deubiquitinating).

## Function
MINDY4, a member of the MINDY family of deubiquitinating enzymes, plays a crucial role in the regulation of protein degradation pathways by specifically targeting lysine 48 (K48)-linked polyubiquitin chains. These chains are typically signals for proteasomal degradation, and MINDY4's activity is essential for maintaining cellular protein homeostasis (Snyder2021Deubiquitinating). The enzyme is characterized by a unique catalytic triad composed of cysteine, histidine, and glutamine, which facilitates its high specificity for K48 linkages. This specificity suggests that MINDY4 is involved in regulating protein degradation pathways, impacting cellular processes such as cell cycle regulation, DNA repair, and signal transduction (Snyder2021Deubiquitinating).

MINDY4 is primarily localized in the cytoplasm, where it modulates protein stability and turnover. This localization allows MINDY4 to influence cellular homeostasis and organismal development by ensuring the proper degradation of proteins marked for destruction by K48-linked ubiquitin chains. The enzyme's activity is regulated through a conformational shift that activates the enzyme upon substrate binding, allowing the reactive cysteine residue to perform a nucleophilic attack on the isopeptide bond linking ubiquitin to its substrate (Snyder2021Deubiquitinating).


## References


[1. (Snyder2021Deubiquitinating) Nathan A. Snyder and Gustavo M. Silva. Deubiquitinating enzymes (dubs): regulation, homeostasis, and oxidative stress response. Journal of Biological Chemistry, 297(3):101077, September 2021. URL: http://dx.doi.org/10.1016/j.jbc.2021.101077, doi:10.1016/j.jbc.2021.101077. This article has 83 citations and is from a domain leading peer-reviewed journal.](https://doi.org/10.1016/j.jbc.2021.101077)