Related Experiment Video
Updated: Mar 12, 2026

Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins
Published on: August 9, 2019
Structural Basis for Selective Interaction between the ESCRT Regulator HD-PTP and UBAP1
Deepankar Gahloth1, Colin Levy1, Graham Heaven2
1School of Biological Sciences, Faculty of Biology, Medicine and Health, University of Manchester, Manchester M13 9PT, UK.
The tumor suppressor HD-PTP regulates receptor degradation via ESCRT pathways. Structural studies reveal its unique coiled-coil domain interaction with UBAP1, offering insights for cancer therapies.
Area of Science:
- Cell Biology
- Structural Biology
- Cancer Research
Background:
- Endosomal sorting complexes required for transport (ESCRTs) are crucial for protein degradation.
- Dysregulation of ESCRT pathways is implicated in cancer progression.
- HD-PTP phosphatase controls ESCRT-mediated receptor sorting.
Purpose of the Study:
- To structurally characterize the interaction between HD-PTP and UBAP1.
- To elucidate the molecular mechanisms regulating ESCRT pathways.
- To identify potential targets for anticancer therapies.
Main Methods:
- X-ray crystallography
- Double electron-electron resonance (DEER) spectroscopy
Main Results:
- Determined the structure of the HD-PTP coiled-coil domain complexed with UBAP1.
- Revealed an unexpected open and rigid conformation of the HD-PTP coiled-coil domain.
- Identified key molecular interactions between HD-PTP and UBAP1.
Conclusions:
- The HD-PTP:UBAP1 structure provides a molecular basis for their functional cooperation.
- Findings offer insights into ESCRT pathway regulation in cancer.
- The study may inform the development of novel anticancer strategies.
Related Concept Videos
Regulation of the Unfolded Protein Response
The Unfolded Protein Response
Tail-anchoring of Proteins in the ER Membrane
Covalently Linked Protein Regulators
These groups modify specific amino acids in a protein....
Directing Proteins to the Rough Endoplasmic Reticulum
Coat Assembly and GTPases
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...

