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Related Concept Videos

Conserved Binding Sites01:49

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
Conserved Binding Sites01:49

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
Fibronectins Connect Cells with ECM01:25

Fibronectins Connect Cells with ECM

Fibronectin is an adhesive glycoprotein present in the extracellular matrix of embryogenic and adult tissue. These molecules primarily aid in regulating cell motility and attachment. A fibronectin molecule is composed of two identical polypeptide chains attached to each other by a pair of disulfide bonds at the C-terminal.
Both proteoglycans and collagen are attached to fibronectin proteins, which, in turn, are attached to integrin proteins. These integrin proteins interact with transmembrane...
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
Fibrous Proteins00:55

Fibrous Proteins

Fibrous proteins are either long and narrow proteins or assemble to form long and thin structures. They contain repetitive units and usually consist of either alpha helices or beta sheets and, in rare cases, a mix of both. The amino acids in the primary structure often consist of repeating amino acid sequences. The role of fibrous proteins is primarily structural. Many are located in the extracellular matrix and are present in connective tissues to impart strength and joint mobility. They are...
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...

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Functional Site-Directed Fluorometry in Native Cells to Study Skeletal Muscle Excitability
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A functional FERM domain binding motif in neurofascin.

Frank J Gunn-Moore1, Maria Hill, Fleur Davey

  • 1Bute Medical Building, School of Biology, University of St. Andrews, St. Andrews, KY16 9TS, UK. fjg1@st-and.ac.uk

Molecular and Cellular Neurosciences
|October 19, 2006
PubMed
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Neurofascin, a cell adhesion receptor, directly binds to ezrin, a protein linking cell membranes to the cytoskeleton. This interaction differs between neurofascin and L1, with Nfasc155 and ezrin co-localizing in specific nerve cells.

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Area of Science:

  • Neuroscience
  • Cell Biology
  • Molecular Biology

Background:

  • The L1 family of transmembrane cell adhesion receptors (L1, neuron-glial-related cell adhesion molecule, neurofascin) are crucial for nervous system development.
  • These receptors bind to ankyrin, a cytoskeletal protein, via their cytoplasmic tails.
  • Ezrin, a cytoplasmic protein, links plasma membrane proteins to the cytoskeleton and interacts with L1.

Purpose of the Study:

  • To investigate the interaction between neurofascin and ezrin.
  • To elucidate the mechanism of interaction between L1/neurofascin and ezrin.
  • To determine the cellular localization of neurofascin and ezrin interaction.

Main Methods:

  • Co-immunoprecipitation assays to detect protein-protein interactions.
  • Analysis of interaction mechanisms between L1, neurofascin, and ezrin.
  • Immunofluorescence microscopy to visualize co-localization of Nfasc155 and ezrin in transfected cells and primary tissues.

Main Results:

  • Neurofascin directly interacts with ezrin, in addition to L1.
  • The interaction mechanisms of L1 with ezrin differ from those of neurofascin with ezrin.
  • The neurofascin isoform Nfasc155 co-localizes with ezrin in HEK293 cells and in Schwann cells at the node of Ranvier.

Conclusions:

  • Neurofascin, like L1, binds to ezrin, suggesting a role for ezrin in mediating L1 family receptor-cytoskeleton interactions.
  • Distinct mechanisms govern the interaction of L1 and neurofascin with ezrin.
  • The co-localization of Nfasc155 and ezrin at the node of Ranvier highlights their functional association in myelinated nerve fibers.