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Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
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Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
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Updated: Aug 25, 2025

Membrane-SPINE: A Biochemical Tool to Identify Protein-protein Interactions of Membrane Proteins In Vivo
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Unmasking a two-faced protein.

Ivan Maslov1, Jelle Hendrix1

  • 1Dynamic Bioimaging Lab, Advanced Optical Microscopy Centre, Biomedical Research Institute, Hasselt University, Hasselt, Belgium.

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|October 19, 2022
PubMed
Summary
This summary is machine-generated.

Single-molecule fluorescence spectroscopy and molecular dynamics simulations reveal the structure and dynamics of the postsynaptic density-95 (PSD-95) protein, crucial for neural plasticity.

Keywords:
E. colimolecular biophysicsneurosciencepostsynaptic densityprotein dynamicssingle molecule fluorescencesingle-molecule FRETstructural biology

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Area of Science:

  • Structural biology
  • Neuroscience
  • Biophysics

Background:

  • Postsynaptic density-95 (PSD-95) is a key scaffolding protein in synaptic plasticity.
  • Understanding PSD-95's structure and dynamics is vital for comprehending neural function.

Discussion:

  • Combined use of single-molecule fluorescence spectroscopy and molecular dynamics simulations offers a powerful approach.
  • These methods provide high-resolution insights into protein behavior at the molecular level.

Key Insights:

  • Detailed structural and dynamic information of PSD-95 has been elucidated.
  • The study highlights the dynamic nature of PSD-95 in its native environment.

Outlook:

  • Further research can explore PSD-95's interactions with other synaptic proteins.
  • This work may pave the way for therapeutic strategies targeting neurological disorders.