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Regulation of the Activity of the Dual Leucine Zipper Kinase by Distinct Mechanisms

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Regulation of the Activity of the Dual Leucine Zipper Kinase by Distinct Mechanisms. / Köster, Kyra-Alexandra; Dethlefs, Marten; Duque Escobar, Jorge; Oetjen, Elke.

In: CELLS-BASEL, Vol. 13, No. 4, 333, 11.02.2024.

Research output: SCORING: Contribution to journal › SCORING: Review article › Research

Harvard

Köster, K-A, Dethlefs, M, Duque Escobar, J & Oetjen, E 2024, 'Regulation of the Activity of the Dual Leucine Zipper Kinase by Distinct Mechanisms', CELLS-BASEL, vol. 13, no. 4, 333. https://doi.org/10.3390/cells13040333

APA

Köster, K-A., Dethlefs, M., Duque Escobar, J., & Oetjen, E. (2024). Regulation of the Activity of the Dual Leucine Zipper Kinase by Distinct Mechanisms. CELLS-BASEL, 13(4), [333]. https://doi.org/10.3390/cells13040333

Vancouver

Köster K-A, Dethlefs M, Duque Escobar J, Oetjen E. Regulation of the Activity of the Dual Leucine Zipper Kinase by Distinct Mechanisms. CELLS-BASEL. 2024 Feb 11;13(4). 333. https://doi.org/10.3390/cells13040333

Bibtex

@article{03b2eff9acd247cea0c6092b3cf4012c,
title = "Regulation of the Activity of the Dual Leucine Zipper Kinase by Distinct Mechanisms",
abstract = "The dual leucine zipper kinase (DLK) alias mitogen-activated protein 3 kinase 12 (MAP3K12) has gained much attention in recent years. DLK belongs to the mixed lineage kinases, characterized by homology to serine/threonine and tyrosine kinase, but exerts serine/threonine kinase activity. DLK has been implicated in many diseases, including several neurodegenerative diseases, glaucoma, and diabetes mellitus. As a MAP3K, it is generally assumed that DLK becomes phosphorylated and activated by upstream signals and phosphorylates and activates itself, the downstream serine/threonine MAP2K, and, ultimately, MAPK. In addition, other mechanisms such as protein-protein interactions, proteasomal degradation, dephosphorylation by various phosphatases, palmitoylation, and subcellular localization have been shown to be involved in the regulation of DLK activity or its fine-tuning. In the present review, the diverse mechanisms regulating DLK activity will be summarized to provide better insights into DLK action and, possibly, new targets to modulate DLK function.",
keywords = "Leucine Zippers, MAP Kinase Kinase Kinases/metabolism, Phosphorylation, Protein-Tyrosine Kinases/metabolism, Serine/metabolism, Threonine/metabolism",
author = "Kyra-Alexandra K{\"o}ster and Marten Dethlefs and {Duque Escobar}, Jorge and Elke Oetjen",
year = "2024",
month = feb,
day = "11",
doi = "10.3390/cells13040333",
language = "English",
volume = "13",
journal = "CELLS-BASEL",
issn = "2073-4409",
publisher = "MDPI Multidisciplinary Digital Publishing Institute",
number = "4",

}

RIS

TY - JOUR

T1 - Regulation of the Activity of the Dual Leucine Zipper Kinase by Distinct Mechanisms

AU - Köster, Kyra-Alexandra

AU - Dethlefs, Marten

AU - Duque Escobar, Jorge

AU - Oetjen, Elke

PY - 2024/2/11

Y1 - 2024/2/11

N2 - The dual leucine zipper kinase (DLK) alias mitogen-activated protein 3 kinase 12 (MAP3K12) has gained much attention in recent years. DLK belongs to the mixed lineage kinases, characterized by homology to serine/threonine and tyrosine kinase, but exerts serine/threonine kinase activity. DLK has been implicated in many diseases, including several neurodegenerative diseases, glaucoma, and diabetes mellitus. As a MAP3K, it is generally assumed that DLK becomes phosphorylated and activated by upstream signals and phosphorylates and activates itself, the downstream serine/threonine MAP2K, and, ultimately, MAPK. In addition, other mechanisms such as protein-protein interactions, proteasomal degradation, dephosphorylation by various phosphatases, palmitoylation, and subcellular localization have been shown to be involved in the regulation of DLK activity or its fine-tuning. In the present review, the diverse mechanisms regulating DLK activity will be summarized to provide better insights into DLK action and, possibly, new targets to modulate DLK function.

AB - The dual leucine zipper kinase (DLK) alias mitogen-activated protein 3 kinase 12 (MAP3K12) has gained much attention in recent years. DLK belongs to the mixed lineage kinases, characterized by homology to serine/threonine and tyrosine kinase, but exerts serine/threonine kinase activity. DLK has been implicated in many diseases, including several neurodegenerative diseases, glaucoma, and diabetes mellitus. As a MAP3K, it is generally assumed that DLK becomes phosphorylated and activated by upstream signals and phosphorylates and activates itself, the downstream serine/threonine MAP2K, and, ultimately, MAPK. In addition, other mechanisms such as protein-protein interactions, proteasomal degradation, dephosphorylation by various phosphatases, palmitoylation, and subcellular localization have been shown to be involved in the regulation of DLK activity or its fine-tuning. In the present review, the diverse mechanisms regulating DLK activity will be summarized to provide better insights into DLK action and, possibly, new targets to modulate DLK function.

KW - Leucine Zippers

KW - MAP Kinase Kinase Kinases/metabolism

KW - Phosphorylation

KW - Protein-Tyrosine Kinases/metabolism

KW - Serine/metabolism

KW - Threonine/metabolism

U2 - 10.3390/cells13040333

DO - 10.3390/cells13040333

M3 - SCORING: Review article

C2 - 38391946

VL - 13

JO - CELLS-BASEL

JF - CELLS-BASEL

SN - 2073-4409

IS - 4

M1 - 333

ER -