Deubiquitinase USP19 enhances phenylalanine hydroxylase protein stability and its enzymatic activity View Full Text


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Article Info

DATE

2022-04-21

AUTHORS

Neha Sarodaya, Apoorvi Tyagi, Hyun-Jin Kim, Jencia Carminha Colaco, Ju-Seop Kang, Woo Jin Kim, Kye-Seong Kim, Suresh Ramakrishna

ABSTRACT

Phenylalanine hydroxylase (PAH) is the key enzyme in phenylalanine metabolism, deficiency of which is associated with the most common metabolic phenotype of phenylketonuria (PKU) and hyperphenylalaninemia (HPA). A bulk of PKU disease-associated missense mutations in the PAH gene have been studied, and the consequence of each PAH variant vary immensely. Prior research established that PKU-associated variants possess defects in protein folding with reduced cellular stability leading to rapid degradation. However, recent evidence revealed that PAH tetramers exist as a mixture of resting state and activated state whose transition depends upon the phenylalanine concentration and certain PAH variants that fail to modulate the structural equilibrium are associated with PKU disease. Collectively, these findings framed our understanding of the complex genotype–phenotype correlation in PKU. In the current study, we substantiate a link between PAH protein stability and its degradation by the ubiquitin-mediated proteasomal degradation system. Here, we provide an evidence that PAH protein undergoes ubiquitination and proteasomal degradation, which can be reversed by deubiquitinating enzymes (DUBs). We identified USP19 as a novel DUB that regulates PAH protein stability. We found that ectopic expression of USP19 increased PAH protein level, whereas depletion of USP19 promoted PAH protein degradation. Our study indicates that USP19 interacts with PAH and prevents polyubiquitination of PAH subsequently extending the half-life of PAH protein. Finally, the increase in the level of PAH protein by the deubiquitinating activity of USP19 resulted in enhanced metabolic function of PAH. In summary, our study identifies the role of USP19 in regulating PAH protein stability and promotes its metabolic activity.Graphical abstractGraphical highlights1. E3 ligase Cdh1 promotes PAH protein degradation leading to insufficient cellular amount of PAH causing PKU.2. A balance between E3 ligase and DUB is important to regulate the proteostasis of PAH.3. USP19 deubiquitinates and stabilizes PAH further protecting it from rapid degradation.4. USP19 increases the enzymatic activity of PAH, thus maintaining normal Phe levels. More... »

PAGES

1-16

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s10565-022-09719-z

DOI

http://dx.doi.org/10.1007/s10565-022-09719-z

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1147289275

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/35449354


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