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Related Concept Videos

Lipids as Anchors01:32

Lipids as Anchors

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In the plasma membrane, the lipids forming the bilayer can also act as an anchor to tether proteins to the membrane. The three main types of lipid anchors found in eukaryotes are – prenyl groups, fatty acyl groups, and glycosylphosphatidylinositol or GPI groups. Prenyl and fatty acyl groups act as anchors on the cytosolic surface of the membrane, whereas GPI anchors proteins on the extracellular side.
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Assembly of the Lipid Bilayer in the ER01:28

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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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Membrane Domains01:18

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The membrane domains concentrate specific lipids and proteins at one place within the membrane, which helps in cell signaling, adhesion, and other critical cellular processes. These domains can differ in size, composition, function, and lifespan.
Protein Domains
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Membrane fluidity is explained by the fluid mosaic model of the cell membrane, which describes the plasma membrane structure as a mosaic of components—including phospholipids, cholesterol, proteins, and carbohydrates—that gives the membrane a fluid character.
Mosaic nature of the membrane
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Membrane Lipids01:32

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Lipids are an essential component of all biological membranes. The average lipid content in mammalian membranes is 50%, though it can be as low as 20% in the inner mitochondrial membrane or as high as 80% in the myelin sheath present around the nerve cells.
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Mechanisms of Membrane Domain Formation00:59

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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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Related Experiment Video

Updated: Sep 20, 2025

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Structural insights into lipid membrane binding by human ferlins.

Constantin Cretu1,2,3, Aleksandar Chernev4, Csaba Zoltán Kibédi Szabó5

  • 1Institute for Auditory Neuroscience and InnerEarLab, University Medical Center Göttingen, Göttingen, Germany. constantin.cretu@med.uni-goettingen.de.

The EMBO Journal
|May 28, 2025
PubMed
Summary

Ferlin proteins, crucial for Ca2+-dependent vesicle fusion and linked to human diseases, adopt compact, ring-like structures upon binding membranes. This structural insight advances understanding of their membrane interactions and disease mechanisms.

Keywords:
C2 DomainCa2+ Sensing and SignallingCryo-EMFerlinsMembrane Fusion

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Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
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Fluorescence-Based Measurements of Phosphatidylserine/Phosphatidylinositol 4-Phosphate Exchange Between Membranes
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Area of Science:

  • Membrane biology
  • Protein structure and function
  • Molecular medicine

Background:

  • Ferlins are essential multi-C2 domain proteins involved in Ca2+-dependent vesicle fusion.
  • Despite their disease relevance, the mechanism of ferlin-lipid membrane interaction remains unclear.

Purpose of the Study:

  • To elucidate the near-complete structures of human myoferlin and dysferlin in Ca2+- and lipid-bound states.
  • To understand the mechanistic basis of ferlin-mediated membrane remodeling and fusion.

Main Methods:

  • Near-complete cryo-electron microscopy (cryo-EM) structure determination of human myoferlin and dysferlin.
  • Biophysical probing of ferlin domain interfaces.

Main Results:

  • Ferlins form compact, ring-like structures upon binding to lipid membranes.
  • The C2C-C2D region forms a rigid arch, while C2B, C2F, and C2G domains undergo Ca2+-dependent conformational changes to close the ring.
  • This Ca2+-triggered ring closure facilitates tight interaction with the target membrane.

Conclusions:

  • The study reveals the general structural principles of human ferlins, characterized by a dynamic ring-like architecture.
  • This provides a mechanistic framework for ferlin-lipid interactions and Ca2+-dependent membrane fusion.
  • The findings offer insights into ferlin-related cellular functions and human disease mechanisms.