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Related Experiment Videos

AP-3: an adaptor-like protein complex with ubiquitous expression

E C Dell'Angelica1, H Ohno, C E Ooi

  • 1Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA.

The EMBO Journal
|March 3, 1997
PubMed
Summary

Researchers identified two human proteins, sigma3A and sigma3B, as components of a novel adaptor complex, AP-3. This ubiquitous complex recognizes tyrosine-based sorting signals, suggesting a key role in protein trafficking.

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Immunoprecipitation.

Current protocols in immunology·2008

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Protein Trafficking

Background:

  • Clathrin-associated adaptor complexes mediate protein sorting.
  • Sigma chains (sigma1, sigma2) are small subunits of these complexes.

Purpose of the Study:

  • Identify novel proteins homologous to sigma1 and sigma2.
  • Characterize the function and localization of these proteins and their associated complexes.

Main Methods:

  • Northern and Western blot analyses for gene and protein expression.
  • Complex immunoprecipitation to identify associated proteins.
  • Immunofluorescence microscopy for cellular localization.

Main Results:

  • Identified sigma3A and sigma3B proteins, homologous to known sigma chains.

Related Experiment Videos

  • sigma3A and sigma3B are part of a large complex, AP-3, with other subunits.
  • The AP-3 complex localizes to the Trans-Golgi Network (TGN) and peripheral structures containing transferrin receptor.
  • The p47A subunit interacts with the YQRL sorting signal from TGN38.

    • Conclusions:

    • sigma3A and sigma3B are components of a novel, ubiquitous adaptor-like complex, AP-3.
    • AP-3 is involved in recognizing tyrosine-based sorting signals.
    • This complex likely plays a significant role in intracellular protein trafficking.