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Expression, Purification, and Liposome Binding of Budding Yeast SNX-BAR Heterodimers
Published on: December 6, 2019
SNX27 mediates PDZ-directed sorting from endosomes to the plasma membrane
Benjamin E L Lauffer1, Cristina Melero, Paul Temkin
1Program in Pharmaceutical Sciences and Pharmacogenomics, University of California-San Francisco, San Francisco, CA 94158, USA.
The Journal of Cell Biology
|August 25, 2010
Summary
Sorting nexin 27 (SNX27) protein is crucial for recycling the beta(2)-adrenoreceptor (beta(2)AR) from endosomes. SNX27
Area of Science:
- Cell biology
- Molecular biology
- Membrane trafficking
Background:
- Postsynaptic density 95/discs large/zonus occludens-1 (PDZ) domain-interacting motifs are known for protein scaffolding.
- These motifs are hypothesized to direct transmembrane cargo sorting from endosomes to the plasma membrane.
Purpose of the Study:
- To identify the trans-acting PDZ protein involved in endosomal sorting.
- To investigate the role of sorting nexin 27 (SNX27) in PDZ-directed receptor recycling.
Main Methods:
- Investigated SNX27's role in beta(2)-adrenoreceptor (beta(2)AR) recycling from early endosomes.
- Assessed SNX27's function at endogenous levels.
- Examined the requirement of SNX27's PDZ and Phox homology (PX) domains in recycling.
Main Results:
- SNX27 is essential for efficient PDZ-directed recycling of beta(2)AR.
- SNX27 mediates this sorting at endogenous expression levels.
- SNX27's PDZ domain recognizes the beta(2)AR tail, and its PX domain binds to the endosome membrane.
Conclusions:
- SNX27 plays a distinct role in the PDZ-directed recycling of signaling receptors.
- This finding expands the understanding of cargo-specific molecular sorting in the endosomal recycling pathway.
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