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Related Concept Videos

Protein Diffusion in the Membrane01:24

Protein Diffusion in the Membrane

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Proteins show rotational as well as lateral diffusion across the membrane. The lateral diffusion of proteins was confirmed through the cell fusion experiment where mouse and human cells were fused, resulting in hybrid cells. When the human and mouse cells fused, the specific membrane proteins on human and mouse cells were marked with the red and green-fluorescent markers, respectively. Initially, the red and green fluorescence was located on the respective hemisphere of the cell. As time...
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Enzymes like flippase, floppase, and scramblase transfer phospholipids from one layer to another in the membrane, thereby affecting membrane asymmetry.
Flippase
Eukaryotic flippases are type-IV P-type ATPases or P4-ATPases belonging to P-type ATPase family proteins that are membrane-bound pumps involved in the ATP-mediated transport of ions and molecules across the membrane. Flippases flip specific phospholipids from the outer to the inner leaflet of a membrane. All P4-ATPases have one...
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Mechanisms of Membrane-bending01:15

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The living membranes are flexible due to their fluid mosaic nature; however, their bending into different shapes is an active process regulated by specific lipids and proteins. The membrane bending can be transient as seen in vesicles or stable for a long time as in microvilli. Cells regulate the size, location, and duration of the membrane curvature.
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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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Mutations01:39

Mutations

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Overview
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Insertion of Multi-pass Transmembrane Proteins in the RER01:29

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The rough ER membrane synthesizes, assembles, and embeds transmembrane proteins in diverse topologies. These proteins function as transporters or channels and can remain in the ER membrane or are sent to the Golgi complex, lysosome, and cell membrane.
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Related Experiment Video

Updated: Apr 16, 2026

Preparation of Synaptic Plasma Membrane and Postsynaptic Density Proteins Using a Discontinuous Sucrose Gradient
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Missense mutations on SynGAP C2 domain impair membrane diffusion.

Mattia Miotto1,2, Leonardo Bo'2, Giancarlo Ruocco1,2

  • 1Department of Physics, Sapienza University of Rome, Rome, Italy.

Protein Science : a Publication of the Protein Society
|April 15, 2026
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The SynGAP C2 domain binds lipid bilayers in two ways, influencing its signaling. Disease mutations disrupt this binding, altering SynGAP function in neurological disorders and cancer.

Keywords:
C2 domainVUS mutationsmissense mutationsneurodevelopmental disorderssynGAP

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Biophysics

Background:

  • SynGAP is a postsynaptic protein regulating synaptic plasticity and Ras/ERK signaling.
  • Its C2 domain may interact with membranes, affecting localization and function.
  • The precise membrane interaction mechanism and impact of mutations are unclear.

Purpose of the Study:

  • To elucidate how the SynGAP C2 domain associates with lipid bilayers.
  • To investigate the effects of disease-associated mutations on this membrane interaction.

Main Methods:

  • Extensive molecular dynamics simulations.
  • Structural analysis of SynGAP C2 domain-membrane interactions.

Main Results:

  • The SynGAP C2 domain binds lipid bilayers in two distinct orientations: top and side.
  • These binding modes exhibit different dynamics: faster diffusion (top) vs. stable contacts (side).
  • Pathogenic mutations disrupt these dynamics, reducing diffusivity and altering membrane avidity.

Conclusions:

  • SynGAP C2 domain employs a dual binding mechanism for membrane interaction.
  • Mutations perturb SynGAP's membrane association, potentially explaining its role in neuropathology and cancer.
  • This provides a framework for understanding how mutations impact SynGAP's diverse functions.