Feed

Cellular senescence is a state where cells permanently exit the cell cycle after a finite number of divisions, while maintaining metabolic activity. This phenomenon, initially described by Leonard Hayflick, plays a pivotal role in aging, contributing to the progressive decline in physiological function by promoting tissue dysfunction and restricting regenerative capacity. It is regulated by an array of factors, including DNA damage, telomere shortening, oxidative stress, mitochondrial dysfunction, and epigenetic modifications. Nesprins, a family of transmembrane proteins embedded in the nuclear envelope, are integral components of the LINC (Linker of Nucleoskeleton and Cytoskeleton) complex, which connects the nucleus to the cytoskeleton, thus preserving structural integrity and facilitating mechanotransduction. Lamin proteins, which form the nuclear lamina beneath the inner nuclear membrane, provide support to nuclear envelope architecture, organize chromatin, and modulate gene expression. Lamin proteins also interact with nesprins to collectively sustain nuclear mechanics and maintain morphological stability. Understanding the molecular mechanisms by which nesprins and lamins influence cellular senescence provides valuable insights into the biology of aging and may offer novel therapeutic avenues to address age-related diseases. This review examines the interactions between nesprin and lamin proteins and their potential contributions to cellular senescence.