Publications by authors named "Akshay Rathish"
The linker of the nucleoskeleton and cytoskeleton (LINC) complex is formed by the conserved interactions between Sad-1 and UNC-84 (SUN) and Klarsicht, ANC-1, SYNE homology (KASH) domain proteins, providing a physical coupling between the nucleoskeleton and cytoskeleton that mediates the transfer of physical forces across the nuclear envelope. The LINC complex can perform distinct cellular functions by pairing various KASH domain proteins with the same SUN domain protein. For example, in , SUN protein UNC-84 binds to two KASH proteins UNC-83 and ANC-1 to mediate nuclear migration and anchorage, respectively.
View Article and Find Full Text PDFMechanical stresses directly regulate the function of several proteins of the integrin-mediated focal adhesion complex as they experience intra- and extracellular forces. Kindlin is a largely overlooked member of the focal adhesion complex whose roles in cellular mechanotransduction are only recently being identified. Recent crystallographic experiments have revealed that kindlins can form dimers that bind simultaneously to two integrins, providing a mechanistic explanation of how kindlins may promote integrin activation and clustering.
View Article and Find Full Text PDFArticle Synopsis
- Linkers of the nucleoskeleton and cytoskeleton connect the nuclear envelope to the cytoskeleton through SUN and KASH protein families, facilitating the transmission of mechanical signals.
- Recent structural studies indicate that the SUN protein SUN2 forms a trimer to interact effectively with KASH, but it can exist as an autoinhibited monomer.
- Computational modeling and molecular dynamics simulations of SUN2 reveal that interactions between specific regions (CC1 and CC2) may trigger the transition from a monomer to a trimer, highlighting the role of a specific residue (E452) in this process, which is linked to muscular dystrophy variants.