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

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...

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Bibliographic Details
Published in:Cells (Basel, Switzerland) Switzerland), 2024-02, Vol.13 (4), p.333
Main Authors: Köster, Kyra-Alexandra, Dethlefs, Marten, Duque Escobar, Jorge, Oetjen, Elke
Format: Article
Language:English
Subjects:
Amyotrophic lateral sclerosis
Apoptosis
Biological control systems
Cancer
Cell research
Chemotherapy
Clinical trials
Cytotoxicity
Dephosphorylation
Diabetes
Diabetes mellitus
Disease
Drug dosages
dual leucine zipper kinase
Edema
Genomes
Glaucoma
Homology
Kinases
Leucine zipper proteins
Leucine Zippers
Localization
MAP kinase
MAP Kinase Kinase Kinases - metabolism
Mutation
Neurodegeneration
Neurodegenerative diseases
Optic nerve
Palmitoylation
Pathology
Patients
Peripheral neuropathy
Phosphorylation
Phosphotransferases
Physiological aspects
Prenatal development
proteasomal degradation
Proteasomes
Protein interaction
Protein-serine/threonine kinase
Protein-Tyrosine Kinases - metabolism
Proteins
protein–protein interaction
Serine - metabolism
Spinal cord
Stroke
Threonine - metabolism
Traumatic brain injury
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Summary: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.
ISSN:2073-4409
2073-4409
DOI:10.3390/cells13040333