ArticleMolecular biology of the cell2021
Heh2/Man1 may be an evolutionarily conserved sensor of NPC assembly state.
Article in Molecular biology of the cell, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 18 citations in OpenAlex.
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- A quantitative ultrastructural timeline of nuclear autophagy reveals a role for dynamin-like protein 1 at the nuclear envelope.Nature cell biology · 2025Article
- Phase separation of initiation hubs on cargo is a trigger switch for selective autophagy.Nature cell biology · 2025Article
- A quantitative ultrastructural timeline of nuclear autophagy reveals a role for dynamin-like protein 1 at the nuclear envelope.bioRxiv : the preprint server for biology · 2024Article
- The dynamic nuclear envelope: resilience in health and dysfunction in disease.Current opinion in cell biology · 2023Review
- Quality control mechanisms that protect nuclear envelope identity and function.The Journal of cell biology · 2022Review
- Review
- Emerging Connections between Nuclear Pore Complex Homeostasis and ALS.International journal of molecular sciences · 2022Review
- The LEM-ESCRT toolkit: Repair and maintenance of the nucleus.Frontiers in cell and developmental biology · 2022Review
- Atg39 selectively captures inner nuclear membrane into lumenal vesicles for delivery to the autophagosome.The Journal of cell biology · 2021Article
- A short perinuclear amphipathic α-helix in Apq12 promotes nuclear pore complex biogenesis.Open biology · 2021Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Integral membrane proteins of the Lap2-emerin-MAN1 (LEM) family have emerged as important components of the inner nuclear membrane (INM) required for the functional and physical integrity of the nuclear envelope. However, like many INM proteins, there is limited understanding of the biochemical interaction networks that enable LEM protein function. Here, we show that Heh2/Man1 can interact with major scaffold components of the nuclear pore complex (NPC), specifically the inner ring complex (IRC), in evolutionarily distant yeasts. Although an N-terminal domain is required for Heh2 targeting to the INM, we demonstrate that more stable interactions with the NPC are mediated by a C-terminal winged helix (WH) domain, thus decoupling INM targeting and NPC binding. Inhibiting Heh2's interactions with the NPC by deletion of the Heh2 WH domain leads to NPC clustering. Interestingly, Heh2's association with NPCs can also be disrupted by knocking out several outer ring nucleoporins. Thus, Heh2's interaction with NPCs depends on the structural integrity of both major NPC scaffold complexes. We propose a model in which Heh2 acts as a sensor of NPC assembly state, which may be important for NPC quality control mechanisms and the segregation of NPCs during cell division.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.