Fiche publication
Date publication
mars 2026
Journal
Nature communications
Auteurs
Membres identifiés du Cancéropôle Est :
Dr RUFF Marc
,
Dr SUMARA Izabela
,
Dr KLAHOLZ Bruno
Tous les auteurs :
Lin J, Agote-Aran A, Liao Y, Cloarec M, Andronov L, Schoch RL, Ronchi P, Cochard V, Zhu R, Grandgirard E, Liu X, Lemée MV, Kleiss C, Golzio C, Ruff M, Chevreux G, Schwab Y, Klaholz BP, Sumara I
Lien Pubmed
Résumé
Nuclear pore complexes (NPCs) enable nucleocytoplasmic transport. While NPCs primarily localize to the nuclear envelope (NE), they also appear in cytoplasmic endoplasmic reticulum (ER) membranes called annulate lamellae (AL). Though discovered in the mid-20th century, AL's function and biogenesis remain unclear. Previously considered exclusive to embryonic and malignant cells, we find AL in somatic mammalian cells. Under normal conditions, AL store pre-assembled AL-NPCs that integrate into the NE, producing approximately one-third of newly formed nuclear pores and supporting nuclear expansion during G1. Upon pathological stimuli, AL transfer to the NE is impaired, leading to their cytoplasmic accumulation. RanBP2 (Nup358) is essential for AL biogenesis, with its phenylalanine-glycine repeats promoting AL-NPC scaffold oligomerization. ER-associated Climp63 (CKAP4) directs AL-NPCs to ER sheets and the NE. This AL-driven nuclear pore formation is complementary to the canonical routes, constituting a distinct NPC assembly pathway. Our work uncovers the biogenesis mechanism of AL and the nuclear function of this key cellular organelle.
Référence
Nat Commun. 2026 03 25;:
