Photoregulation of G protein Ras function using photoresponsive protein
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ID: 321857
2026
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Abstract
The small GTPase Ras functions as a molecular switch in intracellular signaling by cycling between GTP-bound active and GDP-bound inactive states. Here, we developed a photoregulated Ras (PR-Ras) by fusing the photoresponsive protein LOV2-Jα as a photoswitch to its N-terminus. PR-Ras retained intrinsic GTPase activity and reversible photoresponsiveness of LOV2-Jα, with no light-dependent changes in basal GTPase activity. In contrast, clear light-dependent regulation emerged in the presence of regulatory proteins, particularly the Ras-specific guanine nucleotide exchange factor (GEF) under limited GTPase activating protein conditions (GAP). Optimization of GAP concentration enabled visualization of GEF-dependent photocontrol across varying GEF levels. Importantly, disruption of the Ras-GEF allosteric interaction using a GEF mutant abolished light-dependent regulation. These findings demonstrate that PR-Ras photocontrol arises from modulation of regulatory interactions rather than intrinsic catalysis, suggesting that the Ras-GEF allosteric interaction contributes to this regulatory mechanism.
| Reference Key |
openalex_W7170101360
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|---|---|
| Authors | Stanley Tabi Besong, Ziyun Zhang, Fofou Yonta Tostani, Nobuyuki Nishibe, Shinsaku Maruta |
| Journal | bioscience biotechnology and biochemistry |
| Year | 2026 |
| DOI |
10.1093/bbb/zbag111
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| URL | |
| Keywords | Keywords not found |
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