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Related Concept Videos

Mechanisms of Membrane Domain Formation00:59

Mechanisms of Membrane Domain Formation

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.
Another mechanism for membrane domain formation involves membrane proteins interacting with cytoskeletal...
Membrane Domains01:18

Membrane Domains

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
The membrane comprises a group of distinct proteins responsible for carrying out a cell's specific function. For example, the plasma membrane of the human sperm, or a single germ cell, contains a unique set of proteins in the anterior...
Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as G-protein-linked receptors (GPCRs) and...
Structural Protein Function01:56

Structural Protein Function

Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity.  In bones and teeth, it mineralizes to form...
What are Membranes?01:24

What are Membranes?

A cell's plasma membrane demarcates the cell's borders and determines the nature of its interaction with the environment. Cells exclude certain substances, take in others, and excrete some others in controlled quantities. The plasma membrane must be flexible to allow certain cells, such as red and white blood cells, to change their shape while passing through narrow capillaries. These are the more obvious plasma membrane functions. In addition, the plasma membrane's surface carries markers that...
What are Membranes?01:24

What are Membranes?

A cell's plasma membrane demarcates the cell's borders and determines the nature of its interaction with the environment. Cells exclude certain substances, take in others, and excrete some others in controlled quantities. The plasma membrane must be flexible to allow certain cells, such as red and white blood cells, to change their shape while passing through narrow capillaries. These are the more obvious plasma membrane functions. In addition, the plasma membrane's surface carries markers that...

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Related Experiment Video

Updated: May 16, 2026

Using Unfixed, Frozen Tissues to Study Natural Mucin Distribution
11:39

Using Unfixed, Frozen Tissues to Study Natural Mucin Distribution

Published on: September 21, 2012

Membrane-bound mucin modular domains: from structure to function.

Nicolas Jonckheere1, Nicolas Skrypek, Frédéric Frénois

  • 1Inserm, UMR837, Jean Pierre Aubert Research Center, Team #5 Mucins, Epithelial Differentiation and Carcinogenesis, 1 Rue Polonovski, 59045 Lille Cedex, France. nicolas.jonckheere@inserm.fr

Biochimie
|November 27, 2012
PubMed
Summary

Mucins are large O-glycoproteins with modular domains involved in cell signaling. This review details membrane-bound mucin structures and functions, highlighting therapeutic potential.

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Mucin Agarose Gel Electrophoresis: Western Blotting for High-molecular-weight Glycoproteins
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Mucin Agarose Gel Electrophoresis: Western Blotting for High-molecular-weight Glycoproteins

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Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
12:05

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies

Published on: March 6, 2013

Related Experiment Videos

Last Updated: May 16, 2026

Using Unfixed, Frozen Tissues to Study Natural Mucin Distribution
11:39

Using Unfixed, Frozen Tissues to Study Natural Mucin Distribution

Published on: September 21, 2012

Mucin Agarose Gel Electrophoresis: Western Blotting for High-molecular-weight Glycoproteins
09:24

Mucin Agarose Gel Electrophoresis: Western Blotting for High-molecular-weight Glycoproteins

Published on: June 14, 2016

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
12:05

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies

Published on: March 6, 2013

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Glycobiology

Background:

  • Mucins are large O-glycoproteins with a core peptide (apomucin) and extensive oligosaccharide chains.
  • Membrane-bound mucins possess modular structures including Pro/Thr/Ser-rich (PTS), EGF-like, and SEA domains.
  • These domains mediate crucial roles in cell signaling and cell-environment interactions.

Purpose of the Study:

  • To review the structural and functional characteristics of membrane-bound mucin domains.
  • To present 3D structures of Epidermal Growth Factor (EGF)-like and SEA domains.
  • To discuss the implications of mucin domain function and alternative splicing in biological contexts.

Main Methods:

  • Structural analysis of EGF-like and SEA domains.
  • Review of literature on mucin domain functions.
  • Discussion of evolutionary conservation and splice event consequences.

Main Results:

  • Detailed 3D structures of EGF and SEA domains are presented.
  • Functional insights into evolutionary conserved domains of membrane-bound mucins are described.
  • The impact of splice events on mucin structure and function is discussed.

Conclusions:

  • Membrane-bound mucins, through their modular domains, are key players in cellular communication.
  • Understanding these domains offers avenues for novel therapeutic strategies.
  • Alternative splicing significantly influences mucin biology and function.