The tau proteins (or τ proteins, after the Greek letter with that name) are a group of six highly soluble protein isoforms produced by alternative splicing from the gene MAPT (microtubule-associated protein tau). They have roles primarily in maintaining the stability of microtubules in axons and are abundant in the neurons of the central nervous system (CNS). They are less common elsewhere but are also expressed at very low levels in CNS astrocytes and oligodendrocytes. Tau proteins are found more often in neurons than in non-neuronal cells in humans. One of tau's main functions is to modulate the stability of axonal microtubules. Other nervous system microtubule-associated proteins (MAPs) may perform similar functions, as suggested by tau knockout mice that did not show abnormalities in brain development – possibly because of compensation in tau deficiency by other MAPs. Abundant filamentous inclusions of tau are characteristic of more than 20 neurodegenerative diseases that are collectively termed tauopathies. Electron cryo-microscopy (cryo-EM) structures of tau amyloid filaments from human brain revealed that distinct tau folds characterise many different diseases. Here you can see how a specific fragment of Tau protein (aminoacids 297-394) is able to form stable aggregates and microstructures, as determined by cryoEM (PDB code: 7QJX)
#molecularart ... #immolecular ... #tau ... #filament ... #assembly ... #fragment ... #neurodegeneration ... #neuron ... #Alzheimer ... #cryoem
Structure of Tau filaments rendered with @proteinimaging and depicted with @corelphotopaint
#molecularart ... #immolecular ... #tau ... #filament ... #assembly ... #fragment ... #neurodegeneration ... #neuron ... #Alzheimer ... #cryoem
Structure of Tau filaments rendered with @proteinimaging and depicted with @corelphotopaint
