TY - JOUR
T1 - Regulation of innate immunity through RNA structure and the protein kinase PKR
AU - Nallagatla, Subba Rao
AU - Toroney, Rebecca
AU - Bevilacqua, Philip C.
N1 - Funding Information:
We thank Pete Beal, Jim Cole, Rick Russell, and Scott Showalter for helpful comments on the manuscript, and National Institutes of Health grant R01-58709 for support.
PY - 2011/2
Y1 - 2011/2
N2 - Molecular recognition of RNA structure is key to innate immunity. The protein kinase PKR differentiates self from non-self by recognition of molecular patterns in RNA. Certain biological RNAs induce autophosphorylation of PKR, activating it to phosphorylate eukaryotic initiation factor 2α (eIF2α), which leads to inhibition of translation. Additional biological RNAs inhibit PKR, while still others have no effect. The aim of this article is to develop a cohesive framework for understanding and predicting PKR function in the context of diverse RNA structure. We present effects of recently characterized viral and cellular RNAs on regulation of PKR, as well as siRNAs. A central conclusion is that assembly of accessible long double-stranded RNA (dsRNA) elements within biological RNAs plays a key role in regulation of PKR kinase. Strategies for forming such elements include RNA dimerization, formation of symmetrical helical defects, A-form dsRNA mimicry, and coaxial stacking of helices.
AB - Molecular recognition of RNA structure is key to innate immunity. The protein kinase PKR differentiates self from non-self by recognition of molecular patterns in RNA. Certain biological RNAs induce autophosphorylation of PKR, activating it to phosphorylate eukaryotic initiation factor 2α (eIF2α), which leads to inhibition of translation. Additional biological RNAs inhibit PKR, while still others have no effect. The aim of this article is to develop a cohesive framework for understanding and predicting PKR function in the context of diverse RNA structure. We present effects of recently characterized viral and cellular RNAs on regulation of PKR, as well as siRNAs. A central conclusion is that assembly of accessible long double-stranded RNA (dsRNA) elements within biological RNAs plays a key role in regulation of PKR kinase. Strategies for forming such elements include RNA dimerization, formation of symmetrical helical defects, A-form dsRNA mimicry, and coaxial stacking of helices.
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U2 - 10.1016/j.sbi.2010.11.003
DO - 10.1016/j.sbi.2010.11.003
M3 - Review article
C2 - 21145228
AN - SCOPUS:79551687500
SN - 0959-440X
VL - 21
SP - 119
EP - 127
JO - Current Opinion in Structural Biology
JF - Current Opinion in Structural Biology
IS - 1
ER -