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Related Concept Videos

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Biological membranes are more than just a barrier separating cell cytoplasm from the outside environment. They are highly dynamic and help maintain the integrity and physiological stability of the cells as well as membrane-bound organelles. Membranes also play vital roles in cell-to-cell and intracellular communication.
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Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
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The ER, Golgi apparatus, endosomes, and lysosomes work in tandem to modify, sort, and package proteins and lipids. An integrated membrane trafficking network facilitates the back and forth shuttling of molecules within different organelles in the same cell or across the cell membrane.
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GPI-anchoring is a post-translational, reversible protein modification that is ubiquitous in eukaryotes. Such proteins are primarily present on the exoplasmic leaflet of the plasma membrane.
GPI-anchor structure
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Related Experiment Video

Updated: Jun 17, 2025

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

Kar Ling Hoh1, Baicong Mu1, Tingyi See2

  • 1Temasek Life Sciences Laboratory, 1 Research Link, National University of Singapore, Singapore 117604, Singapore; Department of Biological Sciences, National University of Singapore, 14 Science Drive 4, Singapore 117543, Singapore.

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|August 7, 2024
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Summary

Vesicle-associated membrane proteins (VAPs) mediate endoplasmic reticulum-plasma membrane contacts through interactions with anionic phospholipids, crucial for pH homeostasis. Defects in these interactions are linked to amyotrophic lateral sclerosis.

Keywords:
CP: Cell biology

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Area of Science:

  • Cell Biology
  • Membrane Trafficking
  • Molecular Interactions

Background:

  • Vesicle-associated membrane proteins (VAPs) are conserved ER proteins that mediate membrane contact sites.
  • Mechanisms of VAP-mediated membrane tethering are not fully understood.
  • ER-plasma membrane (PM) contacts are vital for cellular functions.

Purpose of the Study:

  • To elucidate the mechanism of ER-PM contact formation mediated by VAPs in fission yeast.
  • To investigate the role of VAP-phospholipid interactions in ER-PM tethering.
  • To explore the functional significance of VAP-Pma1 interactions in pH homeostasis.

Main Methods:

  • Systematic interactome analyses.
  • Quantitative microscopy.
  • Biochemical assays to study VAP-phospholipid and VAP-Pma1 interactions.

Main Results:

  • ER-PM coupling is predicted to be independent of direct VAP-protein binding.
  • VAP interactions with anionic phospholipids underlie ER-PM association and are pH-responsive.
  • Amyotrophic lateral sclerosis-associated VAPB mutants show defective phospholipid interactions.
  • A conserved motif in Pma1 interacts with VAP, crucial for pH homeostasis.

Conclusions:

  • VAP-mediated ER-PM contacts are regulated by VAP-anionic phospholipid interactions.
  • These interactions are conserved and functionally relevant, with implications for neurodegenerative diseases.
  • VAP-Pma1 interaction provides a mechanism for pH sensing and regulation at the ER-PM interface.