Uip4p modulates nuclear pore complex function in Saccharomyces cerevisiae
Abstract
A double membrane bilayer perforated by nuclear pore complexes (NPCs) governs the shape of the nucleus, the prominent distinguishing organelle of a eukaryotic cell. Despite the absence of lamins in yeasts, the nuclear morphology is stably maintained and shape changes occur in a regulated fashion. In a quest to identify factors that contribute to regulation of nuclear shape and function in Saccharomyces cerevisiae, we used a fluorescence imaging based approach. Here we report the identification of a novel protein, Uip4p, that is required for regulation of nuclear morphology. Loss of Uip4 compromises NPC function and loss of nuclear envelope (NE) integrity. Our localisation studies show that Uip4 localizes to the NE and endoplasmic reticulum (ER) network. Furthermore, we demonstrate that the localization and expression of Uip4 is regulated during growth, which is crucial for NPC distribution.
02 /Specification & Classification
Click any tag to browse matching papers- Organism
- Assay
- Research Focus
- Approach
Reproducibility ledger
Nobody has reported trying to reproduce this paper yet. Did you replicate an experiment or run the code? Your report saves the next lab a week.
Sign in to file a reproducibility report.
Related papers
- Comprehensive Structure and Functional Adaptations of the Yeast Nuclear Pore Complex
- In cell architecture of the nuclear pore complex and snapshots of its turnover
M. Allegretti, C. E. Zimmerli, … M. Beck·NaturePeer-reviewed·Sep 2, 2020
- REEP4 is recruited to the inner nuclear membrane by ELYS and promotes nuclear pore complex formation
B. Golchoubian, A. Brunner, … A.-L. Schlaitz·bioRxiv·Sep 30, 2020
- Nuclear envelope-vacuole contacts mitigate nuclear pore complex assembly stress
- Quantitative analysis of nuclear pore complex organization in Schizosaccharomyces pombe
J. M. Varberg, J. Unruh, … S. Jaspersen·bioRxiv·Aug 11, 2021
- UBAP2L drives scaffold assembly of nuclear pore complexes at the intact nuclear envelope
Y. LIAO, L. Andronov, … I. Sumara·bioRxiv·Aug 21, 2023