Title : Staufen2 functions in Staufen1-mediated mRNA decay by binding to itself and its paralog and promoting UPF1 helicase but not ATPase activity.

Pub. Date : 2013 Jan 8

PMID : 23263869






5 Functional Relationships(s)
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Protein Name
Organism
1 STAU2, like STAU1, is a double-stranded RNA-binding protein that interacts directly with the ATP-dependent RNA helicase up-frameshift 1 (UPF1) to reduce the half-life of SMD targets that form an SBS by either intramolecular or intermolecular base-pairing. Adenosine Triphosphate UPF1 RNA helicase and ATPase Homo sapiens
2 STAU2, like STAU1, is a double-stranded RNA-binding protein that interacts directly with the ATP-dependent RNA helicase up-frameshift 1 (UPF1) to reduce the half-life of SMD targets that form an SBS by either intramolecular or intermolecular base-pairing. Adenosine Triphosphate UPF1 RNA helicase and ATPase Homo sapiens
3 STAU1- or STAU2-mediated augmentation of UPF1 helicase activity is not accompanied by enhanced ATP hydrolysis but does depend on ATP binding and a basal level of UPF1 ATPase activity. Adenosine Triphosphate UPF1 RNA helicase and ATPase Homo sapiens
4 STAU1- or STAU2-mediated augmentation of UPF1 helicase activity is not accompanied by enhanced ATP hydrolysis but does depend on ATP binding and a basal level of UPF1 ATPase activity. Adenosine Triphosphate UPF1 RNA helicase and ATPase Homo sapiens
5 We propose that STAU paralogs contribute to SMD by "greasing the wheels" of RNA-bound UPF1 so as to enhance its unwinding capacity per molecule of ATP hydrolyzed. Adenosine Triphosphate UPF1 RNA helicase and ATPase Homo sapiens