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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 (show NEU2 Proteins) determines the direction of MT-based pigment granule movement.
Microtubule-associated protein 4 (MAP4) controls the dynein-dependent transport of BTN3A1 (show BTN3A1 Proteins) in response to nucleic acid stimulation, thereby identifying MAP4 as an upstream regulator of BTN3A1 (show BTN3A1 Proteins). Thus, the depletion of either MAP4 or BTN3A1 (show BTN3A1 Proteins) 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 (show SNUPN Proteins) significantly associated with systolic blood pressure.
We demonstrated that the MAP4 (Ser696 and Ser787) phosphorylation increased concomitantly with the p38/MAPK (show MAPK14 Proteins) pathway activation by the LPS (show IRF6 Proteins) and TNF-alpha (show TNF Proteins) 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 (show SEPT2 Proteins).
there are two possible mechanisms triggered by MAP4: stabilization of MT networks; DYNLT1 (show DYNLT1 Proteins) modulation, which is connected with VDAC1 (show VDAC1 Proteins), and inhibition of hypoxia-induced mitochondrial permeabilization
DNAL1 (show DNAL1 Proteins) and MAP4 may exert their functions in the HIV life cycle at reverse transcription, prior to nuclear translocation.
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