UBAP2L ensures homeostasis of nuclear pore complexes at the intact nuclear envelope.
Fiche publication
Date publication
juillet 2024
Journal
The Journal of cell biology
Auteurs
Membres identifiés du Cancéropôle Est :
Pr RIVELINE Daniel, Dr SUMARA Izabela, Dr KLAHOLZ Bruno, Dr PANGOU Evanthia
Tous les auteurs :
Liao Y, Andronov L, Liu X, Lin J, Guerber L, Lu L, Agote-Arán A, Pangou E, Ran L, Kleiss C, Qu M, Schmucker S, Cirillo L, Zhang Z, Riveline D, Gotta M, Klaholz BP, Sumara I
Lien Pubmed
Résumé
Assembly of macromolecular complexes at correct cellular sites is crucial for cell function. Nuclear pore complexes (NPCs) are large cylindrical assemblies with eightfold rotational symmetry, built through hierarchical binding of nucleoporins (Nups) forming distinct subcomplexes. Here, we uncover a role of ubiquitin-associated protein 2-like (UBAP2L) in the assembly and stability of properly organized and functional NPCs at the intact nuclear envelope (NE) in human cells. UBAP2L localizes to the nuclear pores and facilitates the formation of the Y-complex, an essential scaffold component of the NPC, and its localization to the NE. UBAP2L promotes the interaction of the Y-complex with POM121 and Nup153, the critical upstream factors in a well-defined sequential order of Nups assembly onto NE during interphase. Timely localization of the cytoplasmic Nup transport factor fragile X-related protein 1 (FXR1) to the NE and its interaction with the Y-complex are likewise dependent on UBAP2L. Thus, this NPC biogenesis mechanism integrates the cytoplasmic and the nuclear NPC assembly signals and ensures efficient nuclear transport, adaptation to nutrient stress, and cellular proliferative capacity, highlighting the importance of NPC homeostasis at the intact NE.
Mots clés
Humans, Nuclear Pore Complex Proteins, metabolism, Nuclear Pore, metabolism, Homeostasis, Nuclear Envelope, metabolism, HeLa Cells, Active Transport, Cell Nucleus, Membrane Glycoproteins
Référence
J Cell Biol. 2024 07 1;223(7):