RRC ID 76239
Author Mauro MS, Celma G, Zimyanin V, Magaj MM, Gibson KH, Redemann S, Bahmanyar S.
Title Ndc1 drives nuclear pore complex assembly independent of membrane biogenesis to promote nuclear formation and growth.
Journal Elife
Abstract The nuclear envelope (NE) assembles and grows from bilayer lipids produced at the endoplasmic reticulum (ER). How ER membrane incorporation coordinates with assembly of nuclear pore complexes (NPCs) to generate a functional NE is not well understood. Here, we use the stereotypical first division of the early C. elegans embryo to test the role of the membrane-associated nucleoporin Ndc1 in coupling NPC assembly to NE formation and growth. 3D-EM tomography of reforming and expanded NEs establishes that Ndc1 determines NPC density. Loss of ndc1 results in faster turnover of the outer scaffold nucleoporin Nup160 at the NE, providing an explanation for how Ndc1 controls NPC number. NE formation fails in the absence of both Ndc1 and the inner ring component Nup53, suggesting partially redundant roles in NPC assembly. Importantly, upregulation of membrane synthesis restored the slow rate of nuclear growth resulting from loss of ndc1 but not from loss of nup53. Thus, membrane biogenesis can be decoupled from Ndc1-mediated NPC assembly to promote nuclear growth. Together, our data suggest that Ndc1 functions in parallel with Nup53 and membrane biogenesis to control NPC density and nuclear size.
Volume 11
Published 2022-7-19
DOI 10.7554/eLife.75513
PII 75513
PMID 35852146
PMC PMC9296133
MeSH Animals Caenorhabditis elegans / genetics Caenorhabditis elegans / metabolism Cell Nucleus / metabolism Nuclear Envelope / metabolism Nuclear Pore* / metabolism Nuclear Pore Complex Proteins* / genetics Nuclear Pore Complex Proteins* / metabolism
C.elegans tm1845 tm2886 tm4369