Nuclear pore complexes (NPCs) are the gateways that regulate the nucleo-cytoplasmic exchange across the nuclear envelope. This complex is composed of different layers/ subcomplexes which contribute to its barrier function. The central transport channel (CTC) is made up of three key nucleoporins Nup62, Nup58 and Nup54 which is connected to scaffold layer of NPCs via Nup93, which acts as a linker. Multiple studies in the past few years have contributed in establishing the fact that the NPCs are diverse among various species. Our recent study suggests the evolutionary divergence among various nucleoporins including three CTC Nups. In this analysis, we have studied the complex formation and compositional variations from various species. It was observed that diverse stoichiometric CTC complexes exist at biochemical level. Such evolutionary conservation of dynamicity of CTC Nups is expected to modulate task specific transport functions.
Further, we have identified the crucial domain of mammalian Nup93 also, which is sufficient enough for anchoring the central channel complex to the scaffold. We show that entire CTC.93 complex is also very dynamic across various species.