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Updated: Jul 5, 2026

Retroviral Scanning: Mapping MLV Integration Sites to Define Cell-specific Regulatory Regions
Published on: May 28, 2017
Retromer.
Juan S Bonifacino1, James H Hurley
1Cell Biology and Metabolism Program, National Institute of Child Health and Human Development, Building 18T/Room 101, National Institutes of Health, Bethesda, MD 20892, USA. juan@helix.nih.gov
The retromer complex facilitates retrograde transport of cellular cargo. This essential process involves sorting nexins and cargo-recognition proteins, crucial for endosome-to-Golgi network trafficking.
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- The retromer is a protein complex vital for intracellular trafficking.
- It mediates the retrograde transport of transmembrane proteins from endosomes to the trans-Golgi network.
- Dysfunctional retromer is linked to various physiological and pathological conditions.
Purpose of the Study:
- To elucidate the composition and function of the retromer complex.
- To describe the structural domains of retromer subunits and their membrane-binding capabilities.
- To highlight the broad physiological and pathological relevance of retromer-mediated transport.
Main Methods:
- Biochemical analysis of protein complex composition.
- Structural studies of retromer subunits (SNX, Vps26, Vps29, Vps35).
- Investigation of membrane-binding properties involving PI(3)P and curved membranes.
Main Results:
- The retromer complex is a heteropentamer consisting of a sorting nexin dimer and a Vps26/Vps29/Vps35 trimer.
- Sorting nexin subunits possess PX and BAR domains for endosomal membrane association.
- Vps26, Vps29, and Vps35 subunits exhibit distinct protein folds (arrestin, phosphoesterase, alpha-solenoid).
Conclusions:
- The retromer complex is a critical mediator of retrograde transport.
- Its distinct subunit composition and domain organization facilitate endosomal cargo sorting.
- Understanding retromer function is essential for comprehending diverse cellular processes and diseases.
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