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The AP-3 complex: a coat of many colours
G Odorizzi1, C R Cowles, S D Emr
1Division of Cellular and Molecular Medicine, University of California, San Diego, La Jolla 92093-0668, USA.
Trends in Cell Biology
|August 26, 1998
Summary
The AP-3 adaptor protein complex plays a key role in intracellular transport. Mutations in AP-3 subunits are linked to specific genetic disorders in yeast, flies, and mice, revealing its conserved function.
Area of Science:
- Cell Biology
- Molecular Biology
- Genetics
Background:
- Adaptor protein complexes (AP) mediate protein sorting and trafficking.
- AP-3 is a recently identified complex involved in Golgi-derived vesicle transport.
- Its precise function in multicellular organisms was previously unclear.
Purpose of the Study:
- To review current knowledge of the AP-3 complex.
- To discuss AP-3's function in multicellular organisms.
- To highlight the significance of AP-3 mutations in various species.
Main Methods:
- Literature review of existing studies on AP-3.
- Analysis of genetic data from yeast, Drosophila, and mice.
- Comparison of AP-3 subunit mutations with known classical mutations.
Main Results:
- AP-3 mediates cargo-selective transport from the Golgi to the lysosome/vacuole.
- Mutations in AP-3 subunits in yeast indicate a role in an alternative trafficking pathway.
- Homologous mutations in Drosophila and mice confirm AP-3's conserved function in these organisms.
Conclusions:
- The AP-3 complex is crucial for lysosomal/vacuolar trafficking.
- Its function is conserved across different species, from yeast to mammals.
- Understanding AP-3 is vital for deciphering lysosomal storage disorders and related pathologies.