NUP35 is a nucleoporin component of the nuclear pore complex (NPC) that functions in both structural organization and selective nuclear transport. Structurally, NUP35 exists at approximately 16 copies per NPC and localizes to distinct layers within the nuclear pore scaffold 1. It plays a critical role in postmitotic NPC reassembly by facilitating ordered assembly of channel-forming FG-nucleoporins during mitosis 2. Beyond structural roles, NUP35 mediates mRNA-specific nuclear export—particularly regulating cardiomyocyte NHE1 mRNA export through its N-terminal domain, thereby controlling intracellular pH homeostasis and cellular resistance to ischemic stress 3. NUP35 also supports nuclear entry of large macromolecular cargo, including HIV-1 capsids, through direct FG-motif interactions 4. Additionally, NUP35 participates in Ran-dependent mechanisms controlling nuclear envelope protein dynamics via peripheral nuclear pore channels 5. In disease contexts, NUP35 expression correlates with other nucleoporins and is implicated in cancer biology as part of nuclear envelope protein networks 6. However, NUP35 does not directly regulate transcription or 3D genome organization, distinguishing it from other core nucleoporins 7. Its involvement in pore membrane curvature suggests structural importance in maintaining NPC integrity 8.