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Clathrin and adaptors

J Hirst1, M S Robinson

  • 1Department of Clinical Biochemistry, University of Cambridge, Addenbrooke's Hospital, Hills Road, Cambridge CB2 2QR, UK. jh228@cam.ac.uk

Biochimica Et Biophysica Acta
|August 26, 1998
PubMed
Summary
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Clathrin adaptors like AP-1 and AP-2 mediate vesicle formation for protein sorting. A new complex, AP-3, functions independently of clathrin in lysosomal protein transport.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Clathrin and adaptor proteins (APs) are crucial for forming clathrin-coated vesicles involved in intracellular trafficking.
  • AP-1 and AP-2 complexes associate with clathrin-coated vesicles budding from the trans-Golgi network (TGN) and plasma membrane, respectively.
  • These vesicles mediate the sorting of lysosomal enzymes and receptor-mediated endocytosis.

Purpose of the Study:

  • To elucidate the function of adaptor protein complexes in clathrin-mediated vesicle formation and protein sorting.
  • To investigate the role of a newly identified adaptor-related complex, AP-3, in cellular transport pathways.

Main Methods:

  • Analysis of clathrin and adaptor protein complex localization and function.
  • Investigation of vesicle budding dynamics at the TGN and plasma membrane.

Related Experiment Videos

  • Genetic studies to determine the role of AP-3 in protein sorting to lysosomes and related organelles.

    • Main Results:

    • AP-1 and AP-2 complexes are integral to clathrin-coated vesicle formation, driving membrane invagination and concentrating specific transmembrane proteins.
    • Clathrin-coated vesicles from the TGN sort lysosomal enzymes, while those from the plasma membrane handle receptor-mediated endocytosis.
    • AP-3 associates with TGN and peripheral membranes but not clathrin, and genetic data implicates it in sorting to lysosomes and lysosome-related organelles.

    Conclusions:

    • Clathrin-coated vesicles, utilizing AP-1 and AP-2, are essential for distinct protein sorting pathways.
    • The novel AP-3 complex represents a distinct pathway for protein sorting to lysosomes and related organelles, independent of clathrin.
    • Understanding these adaptor complexes provides insight into fundamental cellular transport mechanisms and disease-related protein mis-sorting.