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Association of the AP-3 adaptor complex with clathrin
E C Dell'Angelica1, J Klumperman, W Stoorvogel
1Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA.
Science (New York, N.Y.)
|May 9, 1998
Summary
The adaptor-related protein complex AP-3 (AP-3) interacts with clathrin, a key protein in cellular transport. This interaction suggests AP-3
Area of Science:
- Cell biology
- Molecular and cell biology
- Protein sorting and trafficking
Background:
- Adaptor-related protein complex AP-3 (AP-3) mediates signal-dependent protein sorting to endosomal-lysosomal organelles.
- AP-3 has been hypothesized to function as part of a nonclathrin coat structure.
Purpose of the Study:
- To investigate the potential interaction between AP-3 and clathrin.
- To elucidate the role of AP-3 in clathrin-mediated protein sorting.
Main Methods:
- In vitro binding assays were performed to assess the association between AP-3 and clathrin.
- Immunofluorescence and immunoelectron microscopy were used to examine the colocalization of AP-3 and clathrin within cells.
Main Results:
- In vitro assays demonstrated that mammalian AP-3 binds to clathrin.
- The beta3 subunit's appendage domain of AP-3 interacts with the amino-terminal domain of clathrin heavy chain.
- A conserved clathrin-binding motif was identified within the beta3 appendage domain.
- AP-3 and clathrin were observed to colocalize in cellular compartments.
Conclusions:
- The findings support the association of AP-3 with clathrin.
- AP-3's role in protein sorting may be dependent on its interaction with clathrin.
- This interaction suggests a potential role for AP-3 in clathrin-mediated transport pathways.