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BEACH domain proteins function as cargo-sorting adaptors in secretory and endocytic pathways
Serhiy Pankiv1,2,3, Anette Kathinka Dahl1,2,3, Aleksander Aas1
1Department of Molecular Medicine, Institute of Basic Medical Sciences, University of Oslo, Oslo, Norway.
The Journal of Cell Biology
|November 8, 2024
Summary
BEACH domain-containing proteins (BDCPs) are identified as novel coat proteins crucial for sorting transmembrane proteins (TMPs). These proteins play a key role in cellular transport pathways.
Area of Science:
- Cell Biology
- Molecular Biology
- Protein Trafficking
Background:
- Membrane trafficking is essential for cellular function.
- The sorting of transmembrane proteins (TMPs) is a complex process.
- The role of BEACH domain-containing proteins (BDCPs) in protein sorting was previously unknown.
Purpose of the Study:
- To identify novel proteins involved in transmembrane protein sorting.
- To elucidate the function of BEACH domain-containing proteins (BDCPs) in the secretory pathway.
- To understand the mechanism of TMP sorting in tubular-vesicular compartments.
Main Methods:
- Subcellular localization studies using colocalization with RAB and ARF small GTPases.
- Analysis of protein-protein interactions between BDCPs and TMPs.
- Functional assays in cells lacking BDCPs to assess TMP trafficking.
Main Results:
- BEACH domain-containing proteins (BDCPs) identified as novel membrane coat proteins.
- BDCPs are localized to dynamic tubular-vesicular compartments involved in endocytic recycling and post-Golgi secretion.
- BDCPs directly interact with transmembrane proteins and are required for their proper trafficking to the plasma membrane.
Conclusions:
- BDCPs function as key regulators of transmembrane protein sorting.
- Competitive binding of BDCPs and clathrin coat adaptors mediates TMP sorting in specific cellular compartments.
- This mechanism operates in pleomorphic tubular-vesicular compartments that lack a clathrin coat.
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