Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 20, Issue 4, Pages 515-+Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.2528
Keywords
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Funding
- US National Institutes of Health (NIH) [NIH R01 GM074593]
- Ruth L. Kirschstein National Research Service Award (NRSA) [NIHF32 GM090479, NIH NCI T32 CA09363]
- Messersmith Graduate Student Fellowship
- NIH National Center for Research Resources (NCRR) [1S10 RR026501, 1S10 RR027241]
- NIH National Institute of Allergy and Infectious Diseases (NIAID) [P30 AI078498]
- University of Rochester School of Medicine and Dentistry
- National Science Foundation (NSF)
- NIH National Institute of General Medicine Sciences (NIGMS) through NSF award [DMR-0225180]
- NIH NCRR [RR-01646]
- Department of Energy Office of Biological and Environmental Research
- NIH National Center for Research Resources Biomedical Technology Program [P41RR001209]
- NIGMS
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Staufen1 (STAU1)-mediated mRNA decay (SMD) degrades mammalian-cell mRNAs that bind the double-stranded RNA (dsRNA)binding protein STAU1 in their 3' untranslated region. We report a new motif, which typifies STAU homologs from all vertebrate classes, that is responsible for human STAU1 (hSTAU1) homodimerization. Our crystal structure and mutagenesis analyses reveal that this motif, which we named the Staufen-swapping motif (SSM), and the dsRNA-binding domain 5 ('RBD'5) mediate protein dimerization: the two SSM alpha-helices of one molecule interact primarily through a hydrophobic patch with the two 'RBD'5 a-helices of a second molecule. 'RBD'5 adopts the canonical alpha-beta-beta-beta-alpha fold of a functional RBD, but it lacks residues and features required to bind duplex RNA. In cells, SSM-mediated hSTAU1 dimerization increases the efficiency of SMD by augmenting hSTAU1 binding to the ATP-dependent RNA helicase hUPF1. Dimerization regulates keratinocyte-mediated wound healing and many other cellular processes.
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