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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
Abstract:
The ezrin-radixin-moesin (ERM) family of proteins have emerged as key regulatory molecules in linking F-actin to specific membrane proteins, especially in cell surface structures. Merlin, the product of the NF2 tumor suppressor gene, has sequence similarity to ERM proteins and binds to some of the same membrane proteins, but lacks a C-terminal F-actin binding site. In this review we discuss how ERM proteins and merlin are negatively regulated by an intramolecular association between their N- and C-terminal domains. Activation of at least ERM proteins can be accomplished by C-terminal phosphorylation in the presence of PIP2. We also discuss membrane proteins to which ERM and merlin bind, including those making an indirect linkage through the PDZ-containing adaptor molecules EBP50 and E3KARP. Finally, the function of these proteins in cortical structure, endocytic traffic, signal transduction, and growth control is discussed.
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.