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The peripheral lamina is the only bona fide nucleoskeleton described to date. Several other cytoskeletal proteins (e.g., actins and myosins) are also found in nuclei, but their roles in the nucleoskeleton have not been identified.
Amyloids consist of a β-sheet motif that repeats almost indefinitely. This and other unique properties bestow on these aggregates many biological activities (e.g., template assistance, membrane binding, and infectivity).
Several non-Smad signaling pathways (e.g., MAPK) can be activated by TGF-β family ligands. Advances in understanding the mechanisms of activation and cellular responses to these pathways have recently been made.
Intriguing insights into the assembly, composition, and function of the central microtubules and associated proteins in motile cilia have recently been made. For example, katanin—a protein that severs microtubules—has been implicated in their assembly.
In yeast, prion propagation is controlled by the same Hsp104/70/40 chaperone machinery that is involved in protection against proteotoxic stress. Similar mechanisms may be present in higher eukaryotes.
The ciliary gate is the region at the base of the cilium that separates it from the rest of the cell. The gate consists of transition fibers and a transition zone that regulate proteins entering and exiting the cilium.
Direct contact between muscle precursor cells or between muscle and nonmuscle precursor cells initiates signaling pathways that are critical during steps of skeletal muscle development (e.g., myoblast differentiation and fusion).
Methods for precisely engineering genomes and for producing organ structures from composite cells and matrices have rapidly advanced, allowing the rational engineering of more effective transplantation solutions.
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