Nuclear motility in glioma cells reveals a cell-line dependent role of various cytoskeletal components.

Nuclear migration is a general term for the movement of the nucleus towards a specific site in the cell. These movements are involved in a number of fundamental biological processes, such as fertilization, cell division, and embryonic development. Despite of its importance, the mechanism of nuclear migration is still poorly understood in mammalian cells.

The diverse functional LINCs of the nuclear envelope to the cytoskeleton and chromatin.

The nuclear envelope (NE) is connected to the different types of cytoskeletal elements by linker of nucleoskeleton and cytoskeleton (LINC) complexes. LINC complexes exist from yeast to humans, and have preserved their general architecture throughout evolution. They are composed of SUN and KASH domain proteins of the inner and the outer nuclear membrane, respectively.

Poring over pores: nuclear pore complex insertion into the nuclear envelope.

The nuclear boundary is formed by the nuclear envelope (NE), a double membrane system that establishes a selective barrier between the nucleoplasm and the cytoplasm. Its barrier characteristics are determined by nuclear pore complexes (NPCs); huge protein assemblies that guard nucleocytoplasmic compartmentalization. In this review, we discuss the biogenesis of NPCs during interphase of the cell cycle.

LINCing complex functions at the nuclear envelope: what the molecular architecture of the LINC complex can reveal about its function.

Linker of nucleoskeleton and cytoskeleton (LINC) complexes span the double membrane of the nuclear envelope (NE) and physically connect nuclear structures to cytoskeletal elements. LINC complexes are envisioned as force transducers in the NE, which facilitate processes like nuclear anchorage and migration, or chromosome movements. The complexes are built from members of two evolutionary conserved families of transmembrane (TM) proteins, the SUN (Sad1/UNC-84) domain proteins in the inner nuclear membrane (INM) and the KASH (Klarsicht/ANC-1/SYNE homology) domain proteins in the outer nuclear membrane (ONM).