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Related Experiment Videos

The ENTH domain.

Pietro De Camilli1, Hong Chen, Joel Hyman

  • 1Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, CT 06510, USA. pietro.decamilli@yale.edu

FEBS Letters
|March 26, 2002
PubMed
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The epsin NH2-terminal homology (ENTH) domain is a key protein module involved in membrane interactions and endocytic adaptor functions. Its structure and regulation by phosphoinositides are crucial for cellular processes.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • The epsin NH2-terminal homology (ENTH) domain is a conserved protein module.
  • It is found in proteins that act as endocytic adaptors, interacting with clathrin coat components.
  • ENTH domains are structurally similar to VHS domains, defining families of membrane traffic adaptors.

Purpose of the Study:

  • To elucidate the structural and functional characteristics of the ENTH domain.
  • To understand the role of ENTH domain-containing proteins in cellular processes.
  • To explore the regulation of membrane interaction by phosphoinositides.

Main Methods:

  • Structural analysis of the ENTH domain.
  • Biochemical assays to study protein-membrane interactions.

Related Experiment Videos

  • Investigating the role of phosphoinositides in regulating ENTH domain function.

    • Main Results:

    • The ENTH domain is a superhelix of alpha-helices mediating membrane interactions.
    • ENTH domain proteins function as endocytic adaptors and are involved in signaling and actin regulation.
    • Membrane interaction of ENTH domains is modulated by phosphoinositides.

    Conclusions:

    • The ENTH domain is a critical module for membrane trafficking and cellular signaling.
    • Phosphoinositide regulation is essential for the function of ENTH domain-containing proteins.
    • ENTH and VHS domains represent important protein families involved in membrane dynamics.