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The linker of nucleoskeleton and cytoskeleton ( LINC ) complex is a multifunctional protein complex that is involved in various processes at the nuclear envelope, including nuclear migration, mechanotransduction, chromatin tethering and  DNA  damage response. We recently showed that a nuclear envelope protein, Sad1 and  UNC 84 domain protein 1 ( SUN 1), a component of the  LINC  complex, has a critical function in cell migration. Although ionizing radiation activates cell migration and invasion in vivo and in vitro, the underlying molecular mechanism remains unknown. Here, we examined the involvement of the  LINC  complex in radiation‐enhanced cell migration and invasion. A sublethal dose of X‐ray radiation promoted human breast cancer  MDA ‐ MB ‐231 cell migration and invasion, whereas carbon ion beam radiation suppressed these processes in a dose‐dependent manner. Depletion of  SUN 1 and  SUN 2 significantly suppressed X‐ray‐enhanced cell migration and invasion. Moreover, depletion or overexpression of each  SUN 1 splicing variant revealed that  SUN 1_888 containing 888 amino acids of  SUN 1 but not  SUN 1_916 was required for X‐ray‐enhanced migration and invasion. In addition, the results suggested that X‐ray irradiation affected the expression level of  SUN 1 splicing variants and a SUN protein binding partner, nesprins. Taken together, our findings supported that the  LINC  complex contributed to photon‐enhanced cell migration and invasion.

X‐ray‐enhanced cancer cell migration requires the linker of nucleoskeleton and cytoskeleton complex