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Characterization of a novel RP2-OSTF1 interaction and its implication for actin remodelling
Rodanthi Lyraki1, Mandy Lokaj2, Dinesh C Soares1
1MRC Human Genetics Unit, Institute of Genetics and Molecular Medicine, University of Edinburgh, Western General Hospital, Crewe Road, Edinburgh EH4 2XU, UK.
Journal of Cell Science
|January 24, 2018
Summary
Retinitis pigmentosa 2 (RP2) protein interacts with osteoclast-stimulating factor 1 (OSTF1), revealing a new role for RP2 in regulating cell motility. This discovery sheds light on X-linked retinal degeneration mechanisms.
Area of Science:
- Molecular Biology
- Cell Biology
- Genetics
Background:
- Retinitis pigmentosa 2 (RP2) is linked to X-linked retinal degeneration.
- RP2's N-terminus has GTPase-activating protein (GAP) activity towards ARL3, but the C-terminus function is unknown.
Purpose of the Study:
- To investigate the function of the RP2 C-terminus.
- To identify novel interaction partners of RP2.
- To elucidate the role of RP2 in cell motility.
Main Methods:
- Protein interaction studies using a structure-based approach.
- Analysis of RP2 mutations.
- In vitro cell motility assays.
Main Results:
- A novel interaction between RP2 and osteoclast-stimulating factor 1 (OSTF1) was identified.
- The binding site spans both RP2 domains and is distinct from the ARL3-binding site.
- RP2 positively regulates cell motility by recruiting OSTF1 and preventing its interaction with Myo1E.
Conclusions:
- The RP2 C-terminus interacts with OSTF1, a regulator of cell motility.
- This interaction is disrupted by pathogenic RP2 mutations.
- RP2 plays a crucial role in cell migration, independent of its GAP activity towards ARL3.
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