ABSTRACT
As mechanoreceptors, cells can sense and transmit mechanical forces exerted on their surfaces, meanwhile adjust their own mechanical properties to maintain stability. The mechanical force is transferred from cell surface or cytoplasm to the nucleus depending on the complete cytoskeletal system. This cytoskeletal system consists of cytoplasmic skeleton and nuclear skeleton, and these two parts are connected mechanically by the LINC complex (linker of nucleoskeleton and cytoskeleton complex), which plays an important role in cellular mechanotransduction. This review discusses the basic structure of mechanical transmission part in LINC complex and the changes in the nuclear morphology, the location of transcription factor, and the spatial conformation of chromatin induced by mechanotransduction, so as to lay a foundation for further exploring the role of LINC complex in cell mechanotransduction and gene expression.
ABSTRACT
Objective To investigate the interaction of human testis sperm-associated antigen 4 like(SPAG4L) protein containing Sad,UNC-84(SUN) domain with nuclear envelop spectrin repeat proteins 3 (Nesprin-3) containing Klarsicht,ANC-1 and Syne homology (KASH) domain.Methods SPAC-4L protein domains were analyzed with the bioinformatics method.After the SPAG4L plasmid was transfected into Ntera-2 cells,the subcellular localization of SPAG4L was observed.The interaction of SPAG4L with Nesprin-3 was determined by immunofluorescence,co-immunoprecipitation(co-IP) and bimolecular fluorescence complementation (BiFC) technology,respectively.Results Bioinformatics analysis results showed that there was a transmembrane structure in SPAG4L protein.Subcellular localization results demonstrated that SPAG4L protein located in the nuclear membrane and cytoplasm.Immunofluorescence,Co-IP,and BiFC results showed that there was an interaction between SPAG4L and Nesprin-3,and that a LINC(linkers of the nucleoskeleton to the cytoskeletan) complex was formed.Conclusion SPAG4L may interact with Nesprin-3 to form a LINC complex,which is important for understanding the function of SPAG4L protein in spermatogenesis.