Publication details
Staufen-swapping motif is crucial for Staufen dimerization, structure, and Staufen-mediated mRNA decay
| Authors | |
|---|---|
| Year of publication | 2026 |
| Type | Peer-reviewed scientific article |
| Magazine / Source | PROTEIN SCIENCE |
| MU Faculty or unit | |
| Citation | |
| web | https://onlinelibrary.wiley.com/doi/10.1002/pro.70669 |
| Doi | https://doi.org/10.1002/pro.70669 |
| Keywords | RNA-binding protein; DSRNA |
| Description | Human Staufen1 (hStau1, UniProt O95793.2) is a double-strand RNA(dsRNA) binding protein that modulates gene expression via mRNA-dependent mechanisms such as Staufen-mediated mRNA decay (SMD).This modular protein is dynamic and binds to both messanger RNA (mRNA)targets and proteins. The Staufen-swapping motif (SSM) domain is reportedto play a key role in hStau1 dimerization. Our data confirm that SSM dele-tion decreases hStau1 dimerization. This protein shows higher protein disor-der in the absence of SSM. Thus, SSM plays not only a key role in hStau1dimerization but also modulates its tertiary structure. Surprisingly, increaseddisorder upon SSM deletion does not affect affinity for mRNA targets or pro-tein/RNA stoichiometry but SMD efficiency since SMD targets are upregu-lated upon SSM deletion. In conclusion, hStau1 dimerization via SSMaffects the overall structure and dynamics of the protein required for efficientregulation of gene expression via SMD. |
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