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Insights from the protein interaction Universe of the multifunctional “Goldilocks” kinase DYRK1A

Human Dual specificity tyrosine (Y)-Regulated Kinase 1A (DYRK1A) is encoded by a dosage-dependent gene located in the Down syndrome critical region of human chromosome 21. The known substrates of DYRK1A include proteins involved in transcription, cell cycle control, DNA repair and other processes. H...

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Autores principales: Ananthapadmanabhan, Varsha, Shows, Kathryn H., Dickinson, Amanda J., Litovchick, Larisa
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10600473/
https://www.ncbi.nlm.nih.gov/pubmed/37900285
http://dx.doi.org/10.3389/fcell.2023.1277537
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author Ananthapadmanabhan, Varsha
Shows, Kathryn H.
Dickinson, Amanda J.
Litovchick, Larisa
author_facet Ananthapadmanabhan, Varsha
Shows, Kathryn H.
Dickinson, Amanda J.
Litovchick, Larisa
author_sort Ananthapadmanabhan, Varsha
collection PubMed
description Human Dual specificity tyrosine (Y)-Regulated Kinase 1A (DYRK1A) is encoded by a dosage-dependent gene located in the Down syndrome critical region of human chromosome 21. The known substrates of DYRK1A include proteins involved in transcription, cell cycle control, DNA repair and other processes. However, the function and regulation of this kinase is not fully understood, and the current knowledge does not fully explain the dosage-dependent function of this kinase. Several recent proteomic studies identified DYRK1A interacting proteins in several human cell lines. Interestingly, several of known protein substrates of DYRK1A were undetectable in these studies, likely due to a transient nature of the kinase-substrate interaction. It is possible that the stronger-binding DYRK1A interacting proteins, many of which are poorly characterized, are involved in regulatory functions by recruiting DYRK1A to the specific subcellular compartments or distinct signaling pathways. Better understanding of these DYRK1A-interacting proteins could help to decode the cellular processes regulated by this important protein kinase during embryonic development and in the adult organism. Here, we review the current knowledge of the biochemical and functional characterization of the DYRK1A protein-protein interaction network and discuss its involvement in human disease.
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spelling pubmed-106004732023-10-27 Insights from the protein interaction Universe of the multifunctional “Goldilocks” kinase DYRK1A Ananthapadmanabhan, Varsha Shows, Kathryn H. Dickinson, Amanda J. Litovchick, Larisa Front Cell Dev Biol Cell and Developmental Biology Human Dual specificity tyrosine (Y)-Regulated Kinase 1A (DYRK1A) is encoded by a dosage-dependent gene located in the Down syndrome critical region of human chromosome 21. The known substrates of DYRK1A include proteins involved in transcription, cell cycle control, DNA repair and other processes. However, the function and regulation of this kinase is not fully understood, and the current knowledge does not fully explain the dosage-dependent function of this kinase. Several recent proteomic studies identified DYRK1A interacting proteins in several human cell lines. Interestingly, several of known protein substrates of DYRK1A were undetectable in these studies, likely due to a transient nature of the kinase-substrate interaction. It is possible that the stronger-binding DYRK1A interacting proteins, many of which are poorly characterized, are involved in regulatory functions by recruiting DYRK1A to the specific subcellular compartments or distinct signaling pathways. Better understanding of these DYRK1A-interacting proteins could help to decode the cellular processes regulated by this important protein kinase during embryonic development and in the adult organism. Here, we review the current knowledge of the biochemical and functional characterization of the DYRK1A protein-protein interaction network and discuss its involvement in human disease. Frontiers Media S.A. 2023-10-12 /pmc/articles/PMC10600473/ /pubmed/37900285 http://dx.doi.org/10.3389/fcell.2023.1277537 Text en Copyright © 2023 Ananthapadmanabhan, Shows, Dickinson and Litovchick. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Cell and Developmental Biology
Ananthapadmanabhan, Varsha
Shows, Kathryn H.
Dickinson, Amanda J.
Litovchick, Larisa
Insights from the protein interaction Universe of the multifunctional “Goldilocks” kinase DYRK1A
title Insights from the protein interaction Universe of the multifunctional “Goldilocks” kinase DYRK1A
title_full Insights from the protein interaction Universe of the multifunctional “Goldilocks” kinase DYRK1A
title_fullStr Insights from the protein interaction Universe of the multifunctional “Goldilocks” kinase DYRK1A
title_full_unstemmed Insights from the protein interaction Universe of the multifunctional “Goldilocks” kinase DYRK1A
title_short Insights from the protein interaction Universe of the multifunctional “Goldilocks” kinase DYRK1A
title_sort insights from the protein interaction universe of the multifunctional “goldilocks” kinase dyrk1a
topic Cell and Developmental Biology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10600473/
https://www.ncbi.nlm.nih.gov/pubmed/37900285
http://dx.doi.org/10.3389/fcell.2023.1277537
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