One Ring to Rule them All? Structural and Functional Diversity in the Nuclear Pore Complex. Issue 7 (July 2021)

• Record Type: Journal Article
• Authors: Fernandez-Martinez, Javier; Rout, Michael P.
• Is Part Of: Trends in biochemical sciences. Volume 46:Issue 7(2021)
• Page Start: 595
• Page End: 607
• Publication Date: 2021-07
• Subjects: nuclear pore complex -- nucleoporin -- structure -- NPC -- nuclear transport -- gene regulation; Biochemistry -- Periodicals; 572
• DOI: 10.1016/j.tibs.2021.01.003
• Languages: English
• ISSNs: 0968-0004

Abstract

Abstract : The nuclear pore complex (NPC) is the massive protein assembly that regulates the transport of macromolecules between the nucleus and the cytoplasm. Recent breakthroughs have provided major insights into the structure of the NPC in different eukaryotes, revealing a previously unsuspected diversity of NPC architectures. In parallel, the NPC has been shown to be a key player in regulating essential nuclear processes such as chromatin organization, gene expression, and DNA repair. However, our knowledge of the NPC structure has not been able to address the molecular mechanisms underlying its regulatory roles. We discuss potential explanations, including the coexistence of alternative NPC architectures with specific functional roles. Highlights: The NPC is a large protein assembly that regulates macromolecular transport between the nucleus and the cytoplasm, and acts as a regulatory platform for many other essential nuclear processes. NPC structural characterization has been challenging, but recent technical and methodological advances are advancing our understanding of NPC architecture. Structural analyses of the NPC in different organisms revealed that, although there is a common bauplan, a significant degree of variability is observed in the peripheral modules that build these NPCs. The multiple regulatory roles shown for the NPC suggest an even greater degree of NPC architectural diversity that has not yet been unveiled.