Histone-lysine N-methyltransferase SETD3 (NP_115609.2) was identified as the actin-specific histidine N-methyltransferase, an enzyme catalyzing the extremely well-conserved methylation of H73 in β-actin.
Microtubules are nucleated by the centrosome of the primary cilium in the apical end-foot of neuroepithelial cells and inter-dependent microtubule and actin dynamics are required here to orchestrate delamination of newborn neurons.
A reconstituted system has been developed that self-organizes into dynamic actin cortices capable of spontaneous polarization, similar to the initial cortical polarization observed in cells during embryogenesis and development.
Eps8, a specific effector of oncogenic signaling, organizes the cortical actin cytoskeleton of cancer cells to promote mechanical properties that favor a newly identified mode of confined, adhesion-independent cell migration.
Pericytes surrounding capillaries in the retina contain α-smooth muscle actin, demonstrating that pericytes have the necessary molecular machinery to change capillary diameter during neurovascular coupling.
The numerous reports in support of action-value representation in the striatum are based on statistical analyses that are subject to two critical confounds and, thus, this long-held belief of striatal action-value representation should be retested using different experiments and analyses.
Structural research, supplemented by biochemical experiments and enzymatic assays, unravels the sequence-dependent molecular mechanism by which SETD3 recognizes β-actin and methylates His73 of β-actin.