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An ACAP1 coat complex acting in endocytic recycling
1Division of Rheumatology, Immunology, and Allergy, Brigham and Women's Hospital, Boston, MA, USA; Department of Medicine, Harvard Medical School, Boston, MA, USA.
Methods in Cell Biology
|September 12, 2015
Summary
Coat proteins sort cellular cargo. Researchers identified ACAP1 (adenosine diphosphate ribosylation factor GTPase-activating proteins with Coiled-coil, Ankryin repeat and PH domains 1) as a key coat complex in endocytic recycling pathways.
Area of Science:
- Cell Biology
- Molecular Biology
- Protein Trafficking
Background:
- Coat proteins are essential for intracellular transport pathways.
- The role of coat proteins in endocytic recycling pathways remained unclear for many years.
- Recent studies have identified multiple coat complexes involved in recycling pathways.
Purpose of the Study:
- To clarify the role of coat proteins in endocytic recycling.
- To characterize the function of ACAP1 (adenosine diphosphate ribosylation factor GTPase-activating proteins with Coiled-coil, Ankryin repeat and PH domains 1) in cargo sorting.
- To describe methods for studying ACAP1's role in recycling endosomes.
Main Methods:
- Identification of coat complexes in recycling pathways.
- Studies focusing on ACAP1's function.
- Characterization of ACAP1's role at the recycling endosome.
Main Results:
- Multiple coat complexes have been identified in recycling pathways.
- ACAP1 acts in the sorting of cargoes at the recycling endosome.
- ACAP1 facilitates the return of cargoes to the plasma membrane.
Conclusions:
- The role of coat proteins in endocytic recycling is now clarified.
- ACAP1 is a key coat complex involved in endocytic recycling.
- ACAP1 mediates cargo sorting for return to the plasma membrane.
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