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Related Experiment Videos

ENTH/ANTH proteins and clathrin-mediated membrane budding.

Valerie Legendre-Guillemin1, Sylwia Wasiak, Natasha K Hussain

  • 1Department of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal, Quebec H3A 2B4, Canada.

Journal of Cell Science
|December 6, 2003
PubMed
Summary

The epsin N-terminal homology (ENTH) and AP180 N-terminal homology (ANTH) domains are crucial for clathrin-mediated endocytosis. These domains facilitate clathrin coat formation and membrane curvature, essential for vesicle budding.

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Basic Science and Pathogenesis.

Alzheimer's & dementia : the journal of the Alzheimer's Association·2025

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • The epsin N-terminal homology (ENTH) domain is a conserved module in proteins involved in clathrin-mediated endocytosis.
  • Structural studies reveal a distinct yet similar module, the AP180 N-terminal homology (ANTH) domain, in some proteins previously classified as ENTH-containing.

Purpose of the Study:

  • To elucidate the structural and functional relationship between ENTH and ANTH domains.
  • To understand the role of E/ANTH domains in clathrin-mediated membrane budding and vesicle formation.

Main Methods:

  • Structural analyses of protein domains.
  • Ligand-binding studies to assess interactions with phospholipids and proteins.

Main Results:

Related Experiment Videos

  • ENTH and ANTH domains (collectively E/ANTH) bind inositol phospholipids and proteins.
  • E/ANTH domains are critical for nucleating and forming clathrin coats on membranes.
  • ENTH domains contribute to membrane curvature via lipid remodeling during vesicle formation.
  • E/ANTH-bearing proteins function with adaptor protein-1 and GGA adaptors at the trans-Golgi network.

Conclusions:

  • E/ANTH domains are key regulators of clathrin-mediated endocytosis and membrane remodeling.
  • These domains play a universal role in the machinery for clathrin-mediated membrane budding, particularly at the trans-Golgi network.