Interplay between endoplasmic reticulum membrane contacts and actomyosin cytoskeleton

Zhang, Dan

doi:10.1002/cm.21623

Cited by 8 publications

(3 citation statements)

References 64 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…5 F ). Considering the interplay between cytoskeleton and the ER membrane ( 69 – 72 ), it is tempting to speculate that virus-induced vimentin cage not only provides physical space for viral RCs accumulation, but equally importantly, interacts with molecules involved in cellular transcription and translation process, and thus promotes the efficiency of virus replication from perspectives of both physical support and functional control.…”

Section: Discussionmentioning

confidence: 99%

Host cytoskeletal vimentin serves as a structural organizer and an RNA-binding protein regulator to facilitate Zika viral replication

Zhang

Zhao

et al. 2022

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

Emerging microbe infections, such as Zika virus (ZIKV), pose an increasing threat to human health. Investigations on ZIKV replication have revealed the construction of replication complexes (RCs), but the role of cytoskeleton in this process is largely unknown. Here, we investigated the function of cytoskeletal intermediate filament protein vimentin in the life cycle of ZIKV infection. Using advanced imaging techniques, we uncovered that vimentin filaments undergo drastic reorganization upon viral protein synthesis to form a perinuclear cage-like structure that embraces and concentrates RCs. Genetic removal of vimentin markedly disrupted the integrity of RCs and resulted in fragmented subcellular dispersion of viral proteins. This led to reduced viral genome replication, viral protein production, and release of infectious virions, without interrupting viral binding and entry. Furthermore, mass spectrometry and RNA-sequencing screens identified interactions and interplay between vimentin and hundreds of endoplasmic reticulum (ER)-resident RNA-binding proteins. Among them, the cytoplasmic-region of ribosome receptor binding protein 1, an ER transmembrane protein that directly binds viral RNA, interacted with and was regulated by vimentin, resulting in modulation of ZIKV replication. Together, the data in our work reveal a dual role for vimentin as a structural element for RC integrity and as an RNA-binding-regulating hub during ZIKV infection, thus unveiling a layer of interplay between Zika virus and host cell.

show abstract

Section: Discussionmentioning

confidence: 99%

Host cytoskeletal vimentin serves as a structural organizer and an RNA-binding protein regulator to facilitate Zika viral replication

Zhang

Zhao

et al. 2022

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

show abstract

“…Moreover, tight ER-PM junctions can impose steric effects on cortical events. Such physical roles have been mainly established for contractile ring assembly and for delimiting exocytic territory in the fission yeast Schizosaccharomyces pombe (S. pombe) [10][11][12] . Here, for the first time, we expand VAP-mediated ER-PM contact functions to pH homeostasis using S. pombe.…”

Section: Introductionmentioning

confidence: 99%

VAP-mediated membrane tethering mechanisms implicate ER-PM contact function in pH homeostasis

Hoh

See

et al. 2023

Preprint

Self Cite

View full text Add to dashboard Cite

VAMP-associated proteins (VAPs) are highly conserved endoplasmic reticulum (ER) resident proteins that establish ER contacts with multiple membrane compartments in many eukaryotes. However, VAP-mediated membrane tethering mechanisms remain ambiguous. Here, focusing on fission yeast ER-plasma membrane (PM) contact formation, using systematic interactome analyses and quantitative microscopy, we predict a non-protein-protein binding-based tethering mechanism of VAPs. We further demonstrate that VAP-anionic phospholipids interactions underlie ER-PM association and define the pH-responsive nature of VAP-tethered membrane contacts. Importantly, such conserved interactions, particularly with phosphatidylinositol 4-phosphate (PI4P) and phosphatidylinositol (PI), are defective in amyotrophic lateral sclerosis (ALS)-associated human VAPB mutant. Moreover, we identify a conserved FFAT-like motif locating at the autoinhibitory hotspot of the essential PM proton pump Pma1. This modulatory VAP-Pma1 interaction is crucial for pH homeostasis. We thus propose an ingenious strategy for maintaining intracellular pH by coupling Pma1 modulation with pH-biosensory ER-PM contacts via VAP-mediated interactions.

show abstract

“…Limited spacing at MCSs could obstruct space-demanding processes that involve large-sized protein assemblies (Zhang, 2020 ) or vesicles (Ng et al, 2018 ). It is conceivable that such physical roles would depend on the amount and plasticity of MCSs, and hence the disassembly and removal of MCS become an important step to finetune this barrier effect.…”

mentioning

confidence: 99%

Editorial: Coupling and Uncoupling: Dynamic Control of Membrane Contacts

Zhang

Saheki

et al. 2021

Front. Cell Dev. Biol.

Self Cite

View full text Add to dashboard Cite

Interplay between endoplasmic reticulum membrane contacts and actomyosin cytoskeleton

Cited by 8 publications

References 64 publications

Host cytoskeletal vimentin serves as a structural organizer and an RNA-binding protein regulator to facilitate Zika viral replication

Host cytoskeletal vimentin serves as a structural organizer and an RNA-binding protein regulator to facilitate Zika viral replication

VAP-mediated membrane tethering mechanisms implicate ER-PM contact function in pH homeostasis

Editorial: Coupling and Uncoupling: Dynamic Control of Membrane Contacts

Contact Info

Product

Resources

About