MARK4 antibody
- Known as:
- MARK4 (anti-)
- Catalog number:
- orb101859
- Product Quantity:
- EUR
- Category:
- -
- Supplier:
- Biorbyt biorb
- Gene target:
- MARK4 antibody
Related genes to: MARK4 antibody
- Gene:
- MARK4 NIH gene
- Name:
- microtubule affinity regulating kinase 4
- Previous symbol:
- MARKL1
- Synonyms:
- Nbla00650, FLJ90097, KIAA1860, PAR-1D
- Chromosome:
- 19q13.32
- Locus Type:
- gene with protein product
- Date approved:
- 2000-09-25
- Date modifiied:
- 2016-02-10
Related products to: MARK4 antibody
Related articles to: MARK4 antibody
- Overactivation of Microtubule affinity regulating kinase 4 (MARK4) is believed to contribute to Alzheimer's disease pathogenesis. MARK4 promotes the accumulation of the microtubule-binding protein tau, thereby enhancing tau-induced neurodegeneration. However, the underlying mechanisms by which MARK4 enhances tau accumulation are not fully understood. T-cell intracellular antigen 1 (TIA1), a critical regulator of stress granule (SG) formation, has been suggested to initiate tau abnormality. Here, we report that MARK4 and TIA1 synergistically induce stress granule (SG) formation. MARK4 is localized in SGs with TIA1 in mammalian cultured cells and primary neurons. MARK4 suppresses TIA1 dimerization and enhances SG formation under oxidative stress. Co-expression of MARK4 and TIA1 promotes tau accumulation, and knockdown of a fly ortholog of TIA1 suppressed tau toxicity in a Drosophila model. These results identify MARK4 as a novel regulator of SG formation and suggest a mechanistic link between oxidative stress and tau pathology. - Source: PubMed
Publication date: 2026/09/04
Nakajima ShoWatanabe KotoneSultanakhmetov GrigoriiFukuchi AoiIto KeiyaShimizu SawakoSaito TaroAsada AkikoAndo Kanae - Brain neurons rely predominantly on glucose as an energy source and express glucose transporter 3 (GLUT3) as their principal glucose transporter. Unlike GLUT4, which undergoes insulin-stimulated membrane translocation in peripheral tissues, GLUT3 mediates largely constitutive and relatively insulin-independent glucose uptake in neurons. Although GLUT3 is essential for neuronal functions, its regulatory mechanisms are not fully understood. Microtubule affinity-regulating kinase 4 (MARK4), a member of the AMP-activated protein kinase-related kinase family, has been implicated in Alzheimer's disease and metabolic regulation in peripheral tissues. Here, we show that MARK4 knockdown in primary neurons reduces GLUT3 surface expression and consequently decreases glucose uptake. While MARK4 knockdown did not alter the intracellular distribution of GLUT3 or mitochondria, it reduced mitochondrial abundance. We further found that MARK4 activity is negatively regulated by the insulin/IGF-1-GSK3β signaling axis in primary neurons. Despite these acute metabolic effects in cultured neurons, Mark4-null mice exhibited no overt morphological abnormalities in the brain. Together, these findings identify MARK4 as a regulator of neuronal glucose uptake by modulating GLUT3 surface expression and suggest that MARK4 functions as a modulatory rather than essential component of neuronal metabolic homeostasis. - Source: PubMed
Publication date: 2026/08/19
Limlingan Sophia Jobien MKrishnankutty AmbikaAsada AkikoAndo KanaeSaito Taro - Thoracic aortic dissection (TAD) is a severe vascular disorder characterized by structural damage, where macrophage-driven inflammation and NLRP3 inflammasome activation play pivotal roles. While the broad anti-inflammatory properties of Theaflavin (TF) are known, its precise structural targets within the TAD cascade remain incompletely understood. We hypothesized that TF protects against TAD by competitively disrupting the MARK4-NLRP3 interaction, thereby suppressing macrophage pyroptosis and inflammasome assembly. - Source: PubMed
Publication date: 2026/06/30
Chen XingXu ShuyingGu TianhaoQian JintaoZhang JunhaoDeng YongWang ZhihuaWang JiahuiTang XinglongKong ChuiyuZhou Qing - Human neural organoids (NOs) provide a powerful platform for investigating synaptic development and dysfunction during early neurodevelopment. However, methodologies for isolating functional synaptic structures from these models remain limited. Here, we present a differential centrifugation protocol enabling the enrichment of growth cone particles (GCPs) and immature synaptosomes from air-liquid interface cerebral organoids (ALI-COs) at distinct developmental stages (Day 90 and 150). Notably, the method avoids density gradients, requires minimal starting material while maintaining reproducibility across human and murine tissues. Quantitative proteomic profiling revealed significant enrichment of growth cone markers (e.g., GAP43) and classical synaptosomal proteins (e.g., PCLO, BSN, SYN1). Transmission electron microscopy (TEM) confirmed the presence of membrane-enclosed GCPs with fibrous content and mitochondria in Day 90 isolates, and immature synaptosomes containing synaptic vesicles on day 150. Functional viability of both types of synaptic structures was demonstrated through KCl-induced depolarization, which triggered phosphorylation changes in growth cone proteins (GAP43, MARCKS, MARCKSL1), cytoskeletal regulators (DCLK1, SHTN1, MARK4, MAP1B) and protein kinases (CAMK2G, PRKCE) in Day 90 GCPs, as well as classical synaptic vesicle cycle proteins (SYN1, DNM1, RPH3A) at Day 150. Overall, this study establishes a centrifugation-based protocol for isolating growth cones and immature synapses from human organoids, capturing key stages of synaptic development and enabling scalable, patient-compatible models to study synaptic function and dysfunction in neurodevelopmental and neurodegenerative disorders. - Source: PubMed
Øhlenschlæger Marie SCriscuolo LucreziaJensen PiaLloyd-Davies Sánchez Daniel JSutcliffe MagdalenaBhosale SantoshBogetofte HelleTahir MuhammadJakobsen Lene APihl MariaBrewer JonathanSchwämmle VeitPoulsen Frantz RFreude KristineLancaster Madeline ARobinson Phillip JLarsen Martin R - Microglia dynamically remodel their cytoskeleton to surveil the brain, respond to injury, and shape synaptic connectivity. While actin drives rapid process motility and phagocytic cup formation, emerging evidence indicates that microtubules are critical regulators of microglial morphology, trafficking, and inflammatory signaling. In homeostatic microglia, microtubules are nucleated at Golgi outposts, supporting ramified architectures and low inflammatory tone. Upon activation, microglia undergo a switch to a centrosome-nucleated, radial microtubule array, driven in part by cyclin-dependent kinase 1 (Cdk1) and associated with polarized cytokine release, NLRP3 inflammasome engagement, and altered phagocytic behavior. We discuss how key regulators of this transition-including Cdk1, centrosomal γ-tubulin recruitment, Golgi-derived microtubule nucleation, and the kinase MARK4 may constitute druggable nodes to tune microglial reactivity in neuro-degenerative diseases. Finally, we outline experimental priorities for translating microglial microtubules into therapeutic targets. - Source: PubMed
Publication date: 2026/04/20
Sanchini CaterinaRosito MariaBartolini FrancescaDi Angelantonio Silvia