Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Gene Ontology annotation based on curation of immunofluorescence data
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Automatic assignment of GO terms using logical inference, based on on inter-ontology links
Identification of a novel homolog of the Drosophila staufen protein in the chromosome 8q13-q21.1 region.
-
Initial identification of STAU2 encoding a 479 aa protein with three dsRBDs, showing 48.5% similarity to Drosophila Staufen and 59.9% to human STAU1.
"presence of three double-stranded RNA-binding domains...48.5% similarity to the Drosophila protein and a 59.9% similarity to the recently described mammalian homolog hStau"
Staufen2 isoforms localize to the somatodendritic domain of neurons and interact with different organelles.
-
STAU2 is brain-enriched, somatodendritic, aligned on microtubule tracts in dendrites. Three isoforms (62, 59, 52 kDa) have distinct subcellular fractionation patterns. Some isoforms associate with ribosomes. STAU2 does not colocalize with STAU1 particles.
"Stau2 is a double-stranded RNA-binding protein that is mainly expressed in the brain...Stau2 is found in the somatodendritic compartment of neurons...we also provide evidence for an interaction of some Stau2 isoforms with ribosomes"
The mammalian RNA-binding protein Staufen2 links nuclear and cytoplasmic RNA processing pathways in neurons.
-
STAU2 interacts with nuclear pore protein p62, export receptor Tap, and EJC proteins Y14-Mago. A pool of STAU2 is present in neuronal nuclei. This suggests STAU2 links nuclear RNA processing to cytoplasmic RNA granule formation.
"Staufen2 interacts with the nuclear pore protein p62, with the RNA export protein Tap and with the exon-exon junction complex (EJC) proteins Y14-Mago...A pool of Staufen2 is present in neuronal nuclei"
Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic RNPs.
-
STAU2 identified in an IGF2BP1-associated mRNP complex also containing DHX9, DDX3X, ELAVL1, HNRNPU, ILF3, PABPC1, PCBP2, PTBP2, STAU1, SYNCRIP, and YBX1 that controls c-myc mRNA stability.
"various RNA-binding proteins that associate with IGF2BP1 in an RNA-dependent fashion"
Defining the membrane proteome of NK cells.
Raftlin is involved in the nucleocapture complex to induce poly(I:C)-mediated TLR3 activation.
-
STAU2 pulled down on poly(I:C) affinity columns, demonstrating dsRNA binding activity.
"we isolated poly(I:C)-binding proteins from CD14-negative cell lysates by sequential affinity chromatography with poly(U)- and poly(I:C)-Sepharose"
Mapping a dynamic innate immunity protein interaction network regulating type I interferon production.
-
STAU2 interacts with EIF2AK2 (PKR) and DHX58 (LGP2) in the HI5 innate immunity interactome.
"Fifty-eight baits were associated with 260 interacting proteins forming a human innate immunity interactome for type I interferon (HI5) of 401 unique interactions"
Cell type-dependent gene regulation by Staufen2 in conjunction with Upf1.
-
STAU2 binds UPF1 directly in an RNA-independent manner. Tethering STAU2 to 3'-UTR has cell-type-dependent effects on mRNA regulation in conjunction with UPF1.
"Stau2 was found to bind directly to Upf1 in an RNA-independent manner in vitro"
Insights into RNA biology from an atlas of mammalian mRNA-binding proteins.
The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts.
Asymmetric segregation of the double-stranded RNA binding protein Staufen2 during mammalian neural stem cell divisions promotes lineage progression.
-
STAU2 segregates asymmetrically during mouse cortical progenitor divisions into the Tbr2+ neuroblast daughter. Knockdown stimulates differentiation. STAU2 cargo mRNAs include Trim32 and primary cilium-related mRNAs.
"the double-stranded RNA-binding protein Stau2 is distributed asymmetrically during progenitor divisions in the developing mouse cortex, preferentially segregating into the Tbr2(+) neuroblast daughter"
The mammalian TRIM-NHL protein TRIM71/LIN-41 is a repressor of mRNA function.
Staufen2 functions in Staufen1-mediated mRNA decay by binding to itself and its paralog and promoting UPF1 helicase but not ATPase activity.
-
STAU2 participates in SMD alongside STAU1. STAU2 binds ~10-fold more UPF1 than STAU1, promotes UPF1 helicase activity without enhancing ATP hydrolysis. STAU1 and STAU2 form homo- and heterodimers. SMD efficiency reflects cumulative STAU1+STAU2 abundance.
"Compared with STAU1, STAU2 binds ~10-fold more UPF1 and ~two- to fivefold more of those SBS-containing mRNAs that were tested, and it comparably promotes UPF1 helicase activity"
Staufen-mediated mRNA decay.
-
Review of SMD. Both STAU1 and STAU2 mediate SMD by binding SBS in 3'-UTRs and recruiting UPF1. SMD competes with NMD for UPF1, contributing to cellular differentiation.
"Recently, STAU2, a paralog of STAU1, has also been reported to mediate SMD...Both STAU1 and STAU2 interact directly with the ATP-dependent RNA helicase UPF1"
Staufen2 deficiency leads to impaired response to novelty in mice.
-
Stau2-deficient mice show reduced locomotor activity, altered novelty preference, failure to discriminate familiar vs new objects, and deficits in spatial context discrimination.
"Stau2GT mice displayed reduced locomotor activity in the open field and altered novelty preference in the NOR and NOL paradigms"
Live cell imaging reveals 3'-UTR dependent mRNA sorting to synapses.
-
STAU2 is required for 3'-UTR-dependent anterograde transport bias in dendrites. mRNA granules patrol dendrites and are dynamically recruited to active synapses. Neuronal activity regulates transport bias and synaptic mRNA recruitment.
"the Rgs4 3'-UTR causes an anterograde transport bias, which requires the Staufen2 protein...the 3'-UTR mediates dynamic, sustained mRNA recruitment to synapses"
Insights into the assembly and architecture of a Staufen-mediated mRNA decay (SMD)-competent mRNP.
-
UPF2 acts as an adaptor between Stau1 and UPF1 in SMD, stimulating UPF1 catalytic activity.
"UPF2 acts as an adaptor between Stau1 and UPF1, stimulates the catalytic activity of UPF1 and plays a central role in the formation of an SMD-competent mRNP"
NF45 and NF90 Regulate Mitotic Gene Expression by Competing with Staufen-Mediated mRNA Decay.
-
NF45-NF90 complex competes with SMD machinery for a common set of mitotic mRNAs. Depletion of SMD components rescues NF45-NF90 depletion phenotypes.
"depletion of SMD components increases the binding of mitotic mRNAs to the NF45-NF90 complex and rescues cells from mitotic defects"
Kinase Interaction Network Expands Functional and Disease Roles of Human Kinases.
Nsp2 has the potential to be a drug target revealed by global identification of SARS-CoV-2 Nsp2-interacting proteins.
-
STAU2 identified as a SARS-CoV-2 Nsp2-interacting protein by AP-MS/SILAC, confirmed by BLI assay.
"Bio-layer interferometry (BLI) assay confirmed the bindings between Nsp2- and 4-interacting proteins, i.e. STAU2 (Staufen2)"
Falcon deep research report on STAU2
-
STAU2 is a double-stranded RNA-binding protein that recognizes structured RNA,
binding secondary structures in 3'-UTRs including complex long-range RNA hairpins,
which provides a structural basis for selective mRNA association.
"STAU2 binds **secondary structures in 3′ UTRs**, including **complex long-range RNA hairpins**, which provide a structural basis for selective mRNA association and downstream regulation."
-
A retained intron in the 3'-UTR of Calm3 mRNA mediates its STAU2- and
activity-dependent localization to neuronal dendrites, directly linking a
structural RNA feature to STAU2-driven subcellular targeting.
"a retained intron in the 3′ UTR of Calm3 mRNA mediates its STAU2- and activity-dependent localization to neuronal dendrites, directly linking a structural RNA feature to STAU2-driven subcellular targeting."
-
STAU2 is enriched in brain and gonads, in contrast to the more ubiquitously
expressed STAU1, and within neurons localizes as RNP particles in the soma and
dendrites that traffic bidirectionally along microtubules.
"STAU2 is described as **enriched in brain and gonads**, in contrast to more ubiquitous STAU1, aligning with its prominent roles in neuronal RNA regulation."
-
Mammalian Staufen proteins contain 4-5 dsRBDs and a tubulin-binding domain (TBD)
between later dsRBDs, consistent with their role in cytoskeleton-linked mRNP transport.
"mammalian Staufen proteins as containing **4–5 dsRBDs** and a **tubulin-binding domain (TBD)** between later dsRBDs, consistent with their role in cytoskeleton-linked mRNP transport."
-
In Staufen-mediated mRNA decay, STAU2 can interact with itself and with STAU1 and
can promote UPF1 helicase activity but not ATPase activity.
"**STAU2 can interact with itself and with STAU1** and can promote **UPF1 helicase (but not ATPase) activity** in SMD-related regulation."
-
STAU2 contributes to mRNA stability beyond transport, with STAU2-deficient neurons
showing decreased levels of target transcripts.
"STAU2 contributes to **mRNA stability**, with **STAU2-deficient neurons showing decreased levels of target transcripts**, supporting a functional role beyond transport"
-
Quantitative target-identification syntheses report ~1,200 STAU2-associated mRNAs
by immunoprecipitation from rat brain and 356 neuronal mRNAs with 3'-UTRs bound by
STAU2 in a mouse brain study.
"~**1,200** STAU2-associated mRNA targets identified by immunoprecipitation from rat brain (mostly neurite-localized), and
- **356** neuronal mRNAs with **3′ UTRs bound by STAU2** reported in a mouse-brain study."
-
STAU2 localization is isoform-dependent: STAU2 isoforms can show isoform-specific
nucleolar accumulation and exportin-5-dependent export.
"**STAU2 isoforms** can show **isoform-specific nucleolar accumulation** and **exportin-5-dependent export**, indicating that STAU2 localization may depend on isoform context and nuclear–cytoplasmic trafficking regulation."