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Super-Resolution Microscopy of the Synaptonemal Complex Within the Caenorhabditis elegans Germline
Published on: September 13, 2022
Hybrid structural model of the complete human ESCRT-0 complex.
Xuefeng Ren1, Daniel P Kloer, Young C Kim
1Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Department of Health and Human Services, Bethesda, MD 20892, USA.
Structure (London, England : 1993)
|March 13, 2009
Summary
The study models the complete ESCRT-0 complex, revealing its structure and dynamic nature. This complex is crucial for sorting cell surface receptors for degradation, ensuring cellular homeostasis.
Area of Science:
- Cell Biology
- Structural Biology
- Biochemistry
Background:
- The Endosomal Sorting Complexes Required for Transport (ESCRT) machinery regulates multivesicular body formation and receptor sorting.
- The ESCRT-0 complex, composed of Hrs and STAM proteins, initiates the ESCRT pathway by recognizing ubiquitinated cargo.
- Understanding the structural organization of ESCRT-0 is vital for elucidating its role in receptor trafficking and degradation.
Purpose of the Study:
- To determine the complete structural model of the human ESCRT-0 complex.
- To investigate the dynamic and conformational properties of ESCRT-0.
- To correlate structural features with the functional role of ESCRT-0 in receptor sorting.
Main Methods:
- Crystal structure determination of the Hrs-STAM core complex at 2.3 Angstroms.
- Hydrodynamic measurements to determine the complex's size and stoichiometry.
- Monte Carlo simulations to model the dynamic ensemble of ESCRT-0 conformations.
Main Results:
- A 1:1 heterodimer structure for ESCRT-0 with a hydrodynamic radius of 7.9 nm.
- The crystal structure reveals domain-swapped GAT domains and an antiparallel coiled-coil.
- Simulations show a dynamic ensemble of conformations, highlighting functional versatility.
Conclusions:
- ESCRT-0 exhibits a unique structural organization combining ordered and disordered elements.
- The dynamic nature of ESCRT-0 facilitates versatile recognition of diverse ubiquitinated receptors.
- This structural insight provides a foundation for understanding ESCRT-mediated trafficking and cellular regulation.
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