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LZK cooperates with DLK to promote retinal ganglion cell death in response to axon injury.
REVIEW: Regulation of Beta-Cell Function and Mass by the Dual Leucine Zipper Kinase
miR-130a inhibited the JNK pathway by targeting MAP3K12, contributing to its anti-apoptotic effect and the maintenance of diabetic endothelial progenitor cell function.
Data suggest that specific pharmacological inhibition of dual leucine zipper kinase (DLK, MAP3K12) may have therapeutic potential in multiple indications of neuronal degeneration.
these findings indicate that DLK participates in cell proliferation and/or survival, at least in part, by modulating the expression of cell cycle regulatory proteins.
The results confirm the significance of apoptosis deregulation in CLL, and suggest a possible relationship between ZIPK expression and the clinical course of the disease.
the DLK-ERK signaling pathway may act as a regulator of the interaction that occurs between Hsp27 and the cytoskeleton during the formation of the cornified cell envelope, a process conferring to the skin its crucial barrier function
for the selective expression of ZPK gene, cell-specific negative regulatory element(s) which locate outside of the core promoter region repress the potent basic promoter activity
ZIPK is positively regulated by phosphorylation within its kinase domain and contains an inhibitory C-terminal domain that controls enzyme activity.
DLK is a signaling molecule implicated in the regulation of keratinocyte terminal differentiation and cornification
DAPK-ZIPK-L13a axis forms a unique regulatory module that first represses, then repermits inflammatory gene expression.
Src-dependent tyrosine phosphorylation recombinant human DLK was important for regulation of its activity. DLK may have a role in PDGF signaling.
These findings demonstrate that pathological activation of DLK is a conserved mechanism that regulates neurodegeneration.
These findings identify DLK as a central regulator of not only JNK but also PERK stress signaling in neurons, with both pathways contributing to neurodegeneration.
Results provide the first evidence that axon guidance genes are downstream targets of the dual leucine zipper kinase (DLK) signaling pathway, which through their regulation probably modulates neuronal cell development, structure and function.
the prevention of the nuclear localization of DLK as induced by prediabetic signals with consecutive suppression of beta-cell apoptosis might constitute a novel target in the therapy of diabetes mellitus
Data assesses DLK's role in axons of adult, injured CNS neurons in vivo and shows that DLK does not appear to have a critical function in axonal degeneration; function appears restricted to soma
This study provides compelling evidence for the pivotal roles of the ZPK/DLK and MKK4/MAP2K4-dependent mechanism in axotomy-induced motoneuron death in neonates
DLK-inducible knockouts displayed a modest increase in basal synaptic transmission but had an attenuation of the JNK/c-Jun stress response pathway activation and significantly reduced neuronal degeneration after kainic acid-induced seizures.
Abundance of DLK in turn controlled the levels of downstream JNK signaling and apoptosis.
DLK is required for RGC JNK activation and cell death in a rodent model of optic neuropathy
The cell intrinsic factors that determine whether a neuron regenerates or undergoes apoptosis in response to axonal injury are not well defined. DLK is an essential upstream mediator of both of these divergent outcomes in the same cell type.
These data demonstrate that DLK enhances regeneration by promoting a retrograde injury signal that is required for the activation of the neuronal proregenerative program.
The mixed lineage kinase dual leucine zipper kinase (DLK) selectively regulates the JNK-based stress response pathway to mediate axon degeneration and neuronal apoptosis without influencing other aspects of JNK signaling.
ZPK/DLK plays a critical role in naturally occurring programmed cell death of motoneurons.
This study indicated that the DLK-JNK pathway facilitates axon formation in neocortical neurons via stage-specific regulation of microtubule stability.
Hepatic progenitors from DLK+ hepatocytes were maintained in long-term culture.
This protein kinase is tightly associated with the microtubules of neurond in the embryonic nervous system.
Hsp70 contributes to the regulation of activated DLK by promoting its CHIP-dependent proteasomal degradation
These data suggest that DLK plays a significant role in the coordinated regulation of radial migration and axon projection by modulating JNK activity.
Activation of Map3k12 and induction of beta-cell apoptosis by the immunosuppressive drug cyclosporin A is reported.
This gene encodes a member of the serine/threonine protein kinase family. This kinase contains a leucine-zipper domain and is predominately expressed in neuronal cells. The phosphorylation state of this kinase in synaptic terminals was shown to be regulated by membrane depolarization via calcineurin. This kinase forms heterodimers with leucine zipper containing transcription factors, such as cAMP responsive element binding protein (CREB) and MYC, and thus may play a regulatory role in PKA or retinoic acid induced neuronal differentiation. Alternatively spliced transcript variants encoding different proteins have been described.
, dual leucine zipper bearing kinase
, dual leucine zipper kinase DLK
, leucine zipper protein kinase
, mixed lineage kinase
, protein kinase MUK
, Mitogen activated protein kinase 12 (Zipper (leucine) protein kinase)
, Zipper (leucine) protein kinase
, dual leucine zipper kinase
, leucine-zipper protein kinase
, mitogen-activated protein kinase kinase kinase 12
, mitogen activated protein kinase kinase kinase 12
, zipper (leucine) protein kinase
, mitogen activated protein kinase kinase kinase 12 type A
, mitogen activated protein kinase kinase kinase 12 type B
, mitogen-activated protein kinase kinase kinase 12 L homeolog