Related Experiment Video

Updated: Oct 11, 2026

Determination of Plasma Membrane Partitioning for Peripherally-associated Proteins
11:11

Determination of Plasma Membrane Partitioning for Peripherally-associated Proteins

Published on: June 15, 2018

ERM-Merlin and EBP50 protein families in plasma membrane organization and function

A Bretscher1, D Chambers, R Nguyen

  • 1Department of Molecular Biology and Genetics, Biotechnology Building, Cornell University, Ithaca, New York 14853, USA. apb5@cornell.edu

Annual Review of Cell and Developmental Biology
|October 14, 2000
PubMed

Insights

Ezrin-radixin-moesin (ERM) proteins and merlin link cell structures to the actin cytoskeleton. Their regulation involves intramolecular binding, phosphorylation, and interactions with membrane proteins, influencing cell functions.

Area of Science:

  • Cell biology
  • Molecular and structural biology

Background:

  • Ezrin-radixin-moesin (ERM) proteins are crucial for linking F-actin to membrane proteins in cell surface structures.
  • Merlin, encoded by the NF2 tumor suppressor gene, shares similarities with ERM proteins but lacks a C-terminal F-actin binding site.

Purpose of the Study:

  • To review the regulation and function of ERM proteins and merlin.
  • To discuss their interactions with membrane proteins and adaptor molecules.
  • To explore their roles in cellular processes.

Main Methods:

  • Review of existing literature on ERM proteins and merlin.
  • Discussion of protein structure, regulation, and function.
  • Analysis of protein-protein interactions.

Main Results:

  • ERM proteins and merlin are negatively regulated by intramolecular N- and C-terminal domain association.
  • Activation of ERM proteins involves C-terminal phosphorylation and PIP2.
  • These proteins interact with membrane proteins directly or indirectly via adaptor molecules like EBP50 and E3KARP.

Conclusions:

  • ERM proteins and merlin play significant roles in maintaining cortical structure, endocytic traffic, signal transduction, and growth control.
  • Understanding their regulation and interactions is key to comprehending cellular organization and function.

More Related Videos

Purification of the Sarco-Endoplasmic Reticulum Ca2+-ATPase from Rabbit Muscle08:37

Purification of the Sarco-Endoplasmic Reticulum Ca2+-ATPase from Rabbit Muscle

Published on: March 21, 2025

Determining Membrane Protein Topology Using Fluorescence Protease Protection (FPP)08:14

Determining Membrane Protein Topology Using Fluorescence Protease Protection (FPP)

Published on: April 20, 2015

Related Concept Videos

Assembly of the Lipid Bilayer in the ER01:28

Assembly of the Lipid Bilayer in the ER

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.
A large chunk of any biological membrane is composed of phospholipids. These lipids have a heterogeneous distribution across different subcellular organelles and even between...
Plasma Membrane in Bacteria and Archaea01:27

Plasma Membrane in Bacteria and Archaea

The plasma membrane is an essential cellular structure responsible for maintaining cellular integrity and regulating the selective transport of molecules. While bacteria and archaea share the fundamental function of plasma membranes, their structural and molecular differences reflect adaptations to distinct ecological and physiological challenges.Bacterial Plasma MembranesBacterial plasma membranes are predominantly composed of phospholipids with fatty acid chains ester-linked to a glycerol...
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...
Introduction to Membrane Proteins01:16

Introduction to Membrane Proteins

The cell membrane, or plasma membrane, is an ever-changing landscape. It is described as a fluid mosaic where various macromolecules are embedded in the phospholipid bilayer. Among the macromolecules are proteins. The protein content varies across cell types. For example, mitochondrial inner membranes contain ~76% protein content, while myelin contains ~18% protein content. Individual cells contain many types of membrane proteins—red blood cells contain over 50—and different cell types have...
Membrane Proteins01:30

Membrane Proteins

Plasma membranes have integral transmembrane proteins involved in facilitated transport. These proteins are collectively referred to as transport proteins, and they function as either channels for the material or as carriers themselves. Channel proteins have hydrophilic domains exposed to the intracellular and extracellular fluids and a hydrophilic channel through their core that provides a hydrated opening for solutes to pass through the membrane layers. Passage through the channel allows...
Membrane Proteins01:30

Membrane Proteins

Plasma membranes have integral transmembrane proteins involved in facilitated transport. These proteins are collectively referred to as transport proteins, and they function as either channels for the material or as carriers themselves. Channel proteins have hydrophilic domains exposed to the intracellular and extracellular fluids and a hydrophilic channel through their core that provides a hydrated opening for solutes to pass through the membrane layers. Passage through the channel allows...