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The authors propose a model for the regulation of microtubule (MT)-based transport of pigment granules in melanophores in which reversible binding of XMAP4 to MTs determines the direction of MT-based pigment granule movement.
The strongest bond of MAP4 was found around the intertubulin-dimer interface such that MAP4 coexists on the microtubule with kinesin-1 bound to the intratubulin-dimer interface as well.
Further experiments revealed that MAP4 regulates microtubule dynamics and promotes epidermal cell migration through Tctex-1. MAP4 and Tctex-1 play important roles in regulating the migration of epidermal cells under hypoxia.
Results suggest that Syk, MAP4, and calpain-1 expression are correlated with each other and these proteins may be involved in early stages of tumour spread.
Expression level of MAP4 mRNA and protein in lung adenocarcinoma tissues were significantly higher than those in noncancerous tissues. MAP4 expression significantly correlated with tumor progression.
Microtubule-associated protein 4 (MAP4) controls the dynein-dependent transport of BTN3A1 in response to nucleic acid stimulation, thereby identifying MAP4 as an upstream regulator of BTN3A1. Thus, the depletion of either MAP4 or BTN3A1 impairs cytosolic DNA- or RNA-mediated type I IFN responses.
an intratumoral injection of MAP4-small interfering RNA (siRNA) remarkably inhibited the growth of the tumors that formed by the MAP4-expressing ESCC cells in nude mice, and a combination of MAP4-siRNA and Bevacizumab significantly enhanced the inhibition effect. Our data suggest that MAP4 is probably a useful prognostic biomarker and a potential therapeutic target for the disease.
MAP4 acts as a checkpoint molecule that balances positive and negative hallmarks of T cell activation.
Results show that marker rs218966 in gene PHF14 and rs9836027 in MAP4 significantly associated with hypertension; additionally, rare variants in SNUPN significantly associated with systolic blood pressure.
We demonstrated that the MAP4 (Ser696 and Ser787) phosphorylation increased concomitantly with the p38/MAPK pathway activation by the LPS and TNF-alpha stimulation of HPMECs, which induced MT disassembly followed by hyperpermeability.
Results demonstrated that MAP4 mutations contribute to the clinical spectrum of centrosomal defects and confirmed the complex role of a centrosomal protein in centrosomal, ciliary, and Golgi regulation associated with severe short stature.
Data show that cAMP/alpha isoform of the catalytic subunit of human PKA (PKAc-alpha) signaling can disrupt microtubule (MT) cytoskeleton by the phosphorylation of microtubule-Associated Protein 4 (MAP4).
MAP4, which is a binding partner of SEPT2.
there are two possible mechanisms triggered by MAP4: stabilization of MT networks; DYNLT1 modulation, which is connected with VDAC1, and inhibition of hypoxia-induced mitochondrial permeabilization
DNAL1 and MAP4 may exert their functions in the HIV life cycle at reverse transcription, prior to nuclear translocation.
Data show that the tau-related protein MAP4 and the microtubule rescue factor CLASP1 are essential for maintaining spindle position and the correct cell-division axis.
Results suggest that structural features of the PJ domain of MAP4 may contribute to the formation of a radial array of microtubules in proliferating cells.
demonstrate that ectopic MAP4 promotes outgrowth of extended MTs during beta1-integrin-induced cell spreading
activity of MAP4 is downregulated by reduced free tubulin concentrations
adenovirus 2 E1B-55K protein blocks p53 as a transcriptional repressor protein of the survivin and the MAP4 promoters
MAP4 microtubule decoration interferes with beta-adrenergic receptor recycling and that this may be one mechanism for beta-adrenergic receptor downregulation in heart failure.
data reveal for the first time that MAP4 drives pathological cardiac remodeling through its phosphorylation. These findings bear the therapeutic potential to ameliorate pathological cardiac remodeling by attenuating MAP4 phosphorylation.
A novel isoform of MAP4 organizes the paraxial microtubule array required for muscle cell differentiation.
This study suggested that The results suggest that MAP4 play roles in some neuron-specific events, such as the dynamic cytoskeletal reorganization and regulation of the microtubule-dependent long-range transport.
Basis for MAP4 dephosphorylation-related microtubule network densification in pressure overload cardiac hypertrophy.
Data indicate that MAP4 binding alters the properties of the actin filaments.
the role of the MAP4 isoforms is to regulate the surface charge of microtubules
A neural cell-specific variant of MAP4 was identified; an ultrastructural study was also made.
The protein encoded by this gene is a major non-neuronal microtubule-associated protein. This protein contains a domain similar to the microtubule-binding domains of neuronal microtubule-associated protein (MAP2) and microtubule-associated protein tau (MAPT/TAU). This protein promotes microtubule assembly, and has been shown to counteract destabilization of interphase microtubule catastrophe promotion. Cyclin B was found to interact with this protein, which targets cell division cycle 2 (CDC2) kinase to microtubules. The phosphorylation of this protein affects microtubule properties and cell cycle progression. Multiple transcript variants encoding different isoforms have been found for this gene.
microtubule-associated protein 4
, MAP 4
, microtubule associated protein 4
, microtubule-associated protein U