About NUP / Nucleoporin:
NUP Mechanism and Interactions
Nucleoporins (NUP) are the regulators when it comes to the moving of macromolecules through the nuclear envelope through interaction with karyopherins molecules. Karyopherins will bind to their contents. It will also mingle with the FG-repeats that some nucleoporins contain. Until they can diffuse through nuclear pores, Karyopherins and their contents repeatedly move between the FG-repeats and then through the nuclear pore complex. Karyopherins can either transport protein into the nucleus out of the nucleus. Then, driven by the G protein (Ran), which is so tiny that it can diffuse through nuclear pores down, Karyopherins release their contents.
Nucleoporins (NUP) are fragments of the nuclear pore complex. It regulates the movement of macromolecules across the nuclear envelope. Due to their molecular weights, they got their names from. The protein RANBD (RAN), NTD (N-terminal domain), and CTD (C-terminal domain) is bound to a domain contained in them.
●For the Nuclear protein import, maintenance of nuclear architecture, and mRNA export, NUP1P (a yeast nucleoprotein) is required.
●Bidirectional transport of importin a requires NUP2P (a yeast nucleoprotein)
●mRNA export requires NUP Gle1 (a human and yeast nucleoprotein)
NUP is the cumulative name for the 30 different nuclear proteins which are included in the eightfold symmetrical structure of the nuclear pore complexes (NPC). The NPS is an eight-sided ring that crosses the nuclear envelope. Another eight scaffold sub-complexes consist of the eight-sided ring. Some proteins that line the pore are interlayered with two structural layers of COPII-like coating. There are three layers (cytoplasm, nucleoplasm, and inner pore) of the ring complex, which can be found from the cytoplasm to the nucleoplasm.