Intermediate filaments
- The diverse roles and dynamic rearrangement of vimentin during viral infection
Summary: A review on the versatile regulations of vimentin in the key steps during the infection of various viruses, including binding, entry, trafficking, replication, assembly, and egress.
- Disease-associated keratin mutations reduce traction forces and compromise adhesion and collective migration
Summary: An epidermolysis bullosa simplex-associated keratin mutation causes defects in mechanotransduction. Keratin networks regulate traction force generation through a Rho signaling pathway upstream of cell–ECM adhesion formation and organized cell migration.
- SNAP29 mediates the assembly of histidine-induced CTP synthase filaments in proximity to the cytokeratin network
Summary: Nutrition starvation stress induces a spatiotemporal interaction of SNAP29 with the cytokeratin network, which mediates the assembly of CTP synthase filaments along the cytokeratin network to modulate enzymatic activity.
- Scaling up single-cell mechanics to multicellular tissues – the role of the intermediate filament–desmosome network
Summary: A review of the roles of intermediate filaments and desmosomes in mechanobiology, highlighting their integration with other cytoskeletal and adhesive systems.
- A rim-and-spoke hypothesis to explain the biomechanical roles for cytoplasmic intermediate filament networks
Summary: The cytoplasmic intermediate filament comprises a rim and spoke arrangement supporting the plasma membrane and connecting to the nucleus, to deliver their mechanosensory functions.
- A mutation in keratin 18 that causes caspase-digestion resistance protects homozygous transgenic mice from hepatic apoptosis and injury
Summary: K18 that is resistant to caspase digestion helps to maintain keratin filament organization and delays apoptosis, thereby protecting liver from injury.
- Desmin and αB-crystallin interplay in the maintenance of mitochondrial homeostasis and cardiomyocyte survival
Highlighted Article: Both desmin and its partner chaperone αB-crystallin associate with mitochondria–sarcoplasmic-reticulum contact sites (MAMs), stabilizing MICOS super-complexes, and thus contributing to proper mitochondrial cristae structure–function.