The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
The target is the fruit-fly gene Uaf1, also called CG9062—not the human gene WDR48, although the proteins are homologs. The supplied UniProt accession Q1LZ08 identifies a WD-repeat protein in the WDR48 family; a species-specific experimental study independently identifies fly Uaf1/CG9062 as the UAF1/WDR48 component of a complex with fly Usp46 and Wdr20. The WD40-repeat annotation is consistent with its experimentally supported role as a protein-interaction and regulatory subunit. (spencer2023theusp46deubiquitylase pages 2-4, spencer2023theusp46deubiquitylase pages 1-2)
Best-supported primary function: Uaf1 is a noncatalytic cofactor of the Usp46–Uaf1–Wdr20 deubiquitylase complex that sustains the abundance of Arrow, the fly Wingless/Wnt coreceptor corresponding to vertebrate LRP5/6. By limiting Arrow ubiquitylation and turnover, the complex increases the receptor available at the cell surface and strengthens the response to Wingless. Usp46—not Uaf1—provides deubiquitylase catalysis; Uaf1 and Wdr20 regulate the enzyme and help maintain its abundance. Accordingly, there is no separate reaction or catalytic substrate specificity to assign to Uaf1 itself. Arrow is the experimentally supported substrate of the complex, whereas its exact ubiquitin-chain linkage preference on fly Arrow has not been established by the cited work. (spencer2023theusp46deubiquitylase pages 9-10, spencer2023theusp46deubiquitylase pages 7-9, spencer2023theusp46deubiquitylase pages 1-2, villamil2013thewd40repeatproteincontaining pages 7-9)
The following evidence summary separates experiments on the fly protein from mechanistic corroboration in other organisms.
| Finding | Assay and biological system | Interpretation | Evidence confidence and citations |
|---|---|---|---|
| Uaf1 loss lowers Wingless output without lowering ligand production | Posterior-compartment RNAi and independent CRISPR sgRNAs targeting different coding regions of Uaf1/CG9062 reduced the Wingless target Senseless (Sens) in Drosophila wing discs. wingless (wg) expression at the dorsal–ventral boundary was retained. | Uaf1 is required in Wingless-responsive cells for signal reception or downstream transduction, rather than for Wingless-ligand production. | High—direct fly genetics with independent perturbations and spatial controls. (spencer2023theusp46deubiquitylase pages 2-4, spencer2023theusp46deubiquitylase pages 1-2) |
| Uaf1 maintains the amplitude and range of intestinal Wingless signaling | Uaf1-null mosaic clones in the adult Drosophila posterior midgut showed cell-autonomous loss or reduction of fz3-GFP and nkd-lacZ, especially farther from the midgut–hindgut Wingless source. | Uaf1 enables cells to respond across the Wingless morphogen gradient; loss preferentially compromises lower-signal, source-distant responses. | High—direct fly null-clone and reporter evidence. (spencer2023theusp46deubiquitylase pages 4-7, spencer2023theusp46deubiquitylase pages 4-4) |
| Uaf1 maintains Arrow receptor abundance in vivo | Adult posterior-midgut Uaf1-null clones showed cell-autonomous reduction of membrane-associated and cytoplasmic Arrow, the fly LRP5/6 ortholog. Decreased Arrow was significant at p < 0.0001; the Armadillo comparison associated with Uaf1 loss was p = 0.043. | Uaf1 acts at or upstream of the Wingless receptor level by sustaining Arrow abundance, with consequent effects on β-catenin/Armadillo signaling. These measurements localize Arrow and Arm—not Uaf1 itself. | High—direct fly mosaic imaging with statistical support and independent null alleles. (spencer2023theusp46deubiquitylase pages 12-13, spencer2023theusp46deubiquitylase pages 9-10) |
| Uaf1 participates in an Arrow-associated Usp46 complex | In Drosophila S2R+ cells, tagged complex components co-immunoprecipitated with FLAG-Arrow. RNAi against Uaf1 reduced steady-state Arrow (p = 0.0008); Usp46- and Wdr20-directed RNAi produced concordant effects. | Uaf1 functions with catalytic Usp46 and Wdr20 in an Arrow-associated deubiquitylase complex. Co-immunoprecipitation does not prove direct Uaf1–Arrow contact. | High for complex association and Arrow dependence; moderate for direct physical contact. (spencer2023theusp46deubiquitylase pages 9-10, spencer2023theusp46deubiquitylase pages 7-9, spencer2023theusp46deubiquitylase pages 10-11) |
| Uaf1 helps stabilize the catalytic Usp46 subunit | In Drosophila cells or tissues, Uaf1 depletion reduced Usp46 protein, whereas Uaf1 overexpression increased it; Wdr20 had the stronger stabilizing effect. | In addition to supporting catalysis, Uaf1 contributes to Usp46 protein abundance and therefore the capacity of the complex. | Moderate-to-high—direct perturbation evidence, but no precise Uaf1-specific effect size was available. (spencer2023theusp46deubiquitylase pages 7-9) |
| Primary molecular role: noncatalytic WD40 regulator of Arrow deubiquitylation | Fly genetics and biochemistry place Uaf1 with Usp46–Wdr20; the complex reduces Arrow ubiquitylation and turnover and increases cell-surface receptor abundance. Homologous-complex studies show UAF1/WDR48 and WDR20 stimulate USP-family catalysis allosterically rather than acting as proteases. | Q1LZ08 is best annotated as a WD40 scaffold/allosteric cofactor, not an enzyme. Usp46 is the catalytic deubiquitylase; Arrow is the experimentally supported receptor substrate of the complex. | High for complex-level fly function; homolog-based for detailed allosteric mechanism. (spencer2023theusp46deubiquitylase pages 9-10, spencer2023theusp46deubiquitylase pages 1-2, hodul2017functionofthe pages 2-3, villamil2013thewd40repeatproteincontaining pages 7-9, li2021molecularmechanismsof pages 12-15) |
| Conserved LRP6 mechanism in other species | Other-species evidence: in human cells, Xenopus, zebrafish and intestinal organoids, USP46–UAF1/WDR48–WDR20 promoted Wnt/β-catenin signaling. Wnt increased complex association with cell-surface LRP6; USP46/UAF1 perturbation reduced LRP6 or pathway output, and the complex opposed RNF43/ZNRF3-mediated LRP6 ubiquitylation. | This strongly corroborates conservation of the fly Uaf1–Arrow mechanism, but it is not direct evidence for Q1LZ08 localization. | High for conservation, but indirect for fly Q1LZ08. (ng2023theusp46complex pages 5-6, ng2023theusp46complex pages 1-2, ng2023theusp46complex pages 2-3, ng2023theusp46complex pages 3-5) |
| USP1–UAF1 DNA-repair functions remain an inference for fly Uaf1 | Mammalian evidence only: USP1–UAF1 deubiquitylates FANCD2/FANCI and PCNA in Fanconi-anemia and translesion-synthesis pathways; mammalian UAF1 DNA binding supports DNA-dependent FANCD2 deubiquitylation. No direct fly Uaf1–Usp1 interaction, FANCD2/PCNA assay, DNA-repair phenotype or nuclear localization was established in the retrieved fly evidence. | A DNA-repair function for Q1LZ08 is evolutionarily plausible but must remain inferred, not asserted as its demonstrated primary fly function. | High for mammalian mechanism; insufficient for direct transfer to fly Q1LZ08. (villamil2013thewd40repeatproteincontaining pages 6-7, cukras2016theusp1uaf1complex pages 7-9, liang2019dnarequirementin pages 1-2, villamil2013thewd40repeatproteincontaining pages 1-3) |
Table: Evidence-tier summary for Drosophila melanogaster Uaf1/CG9062 (UniProt Q1LZ08), separating direct fly findings from cross-species corroboration and mammalian-only inference.
The most informative fly study is Spencer and colleagues, published October 2023. Tagged Usp46-complex components associated with tagged Arrow in Drosophila S2R+ cells. Depleting any of Usp46, Uaf1 or Wdr20 lowered steady-state Arrow; for Uaf1 RNAi, the reported comparison was p = 0.0008, compared with p = 0.00006 for Usp46 and p = 0.000078 for Wdr20. These significance values establish evidence for an effect but are not measurements of its magnitude. Uaf1 depletion also reduced Usp46 protein, whereas Uaf1 overexpression increased it; Wdr20 had a stronger effect on Usp46 abundance. These results support both a regulatory-complex role and a contribution to stability of its catalytic partner. Co-immunoprecipitation establishes complex association, not necessarily direct contact between isolated Uaf1 and Arrow. (spencer2023theusp46deubiquitylase pages 9-10, spencer2023theusp46deubiquitylase pages 7-9, spencer2023theusp46deubiquitylase pages 10-11)
At the complex level, experiments found reduced Arrow ubiquitylation and increased cell-surface Arrow when Usp46-complex activity was increased. Conversely, Uaf1-null clones in the adult posterior midgut had less membrane-associated and cytoplasmic Arrow than adjacent wild-type cells. The Arrow-reduction comparisons for the tested complex-component mutants were reported as p < 0.0001; an Armadillo comparison for Uaf1 mutants was reported as p = 0.043. These observations place the functional defect at least partly at the receptor-abundance step, upstream of the signaling pool of Armadillo/β-catenin. They do not establish that Uaf1 alone catalyzes Arrow deubiquitylation. The identity of the opposing fly Arrow ubiquitin ligase was not established in this study. (spencer2023theusp46deubiquitylase pages 7-9, spencer2023theusp46deubiquitylase pages 12-13, spencer2023theusp46deubiquitylase pages 11-12)
This molecular role is supported by independent in vivo pathway readouts. RNAi against fly Uaf1, and independent CRISPR guides targeting different portions of its coding sequence, reduced the Wingless target Senseless in the posterior wing-disc compartment. Wingless-ligand expression at the dorsal–ventral boundary was not reduced, arguing against impaired ligand production as the explanation. In the posterior midgut, Uaf1-null mosaic clones reduced the fz3-GFP and nkd-lacZ Wingless-response reporters cell-autonomously; fz3-GFP could be almost absent in clones approximately 8–20 cells from the midgut–hindgut boundary, with a less pronounced effect nearer the Wingless source. The reporter comparisons included 91 Uaf1 mutant clones in one quantified experiment. This spatial pattern supports the authors’ interpretation that the complex maintains the amplitude and range of responses to a Wingless gradient. An Axin epistasis experiment with Usp46, rather than specifically Uaf1, further places complex action upstream of the β-catenin destruction machinery. (spencer2023theusp46deubiquitylase pages 4-7, spencer2023theusp46deubiquitylase pages 2-4, spencer2023theusp46deubiquitylase pages 4-4)
A physiological consequence is disturbed Wingless-dependent intestinal homeostasis: Uaf1-mutant midgut clones increased enteroblasts and were associated with more neighboring stem/progenitor cells and mitoses. This is relevant as an outcome of impaired receptor-level signaling, rather than evidence that Uaf1’s primary molecular activity is cell-cycle control. (spencer2023theusp46deubiquitylase pages 4-4)
The demonstrated functional setting is inside Wingless-responsive fly cells, including developing wing-disc cells, cultured S2R+ cells and adult posterior-midgut epithelium. The complex regulates a receptor whose functional pool is at the plasma membrane; its effects on membrane-associated Arrow, and the complex’s association with Arrow, are consistent with action on receptor trafficking or stability. They do not directly locate Uaf1 itself at the plasma membrane. The available fly evidence does not establish a definitive Uaf1-specific cytoplasmic, endosomal or nuclear distribution by localization imaging or fractionation. Similarly, changes in membrane Arrow and cytoplasmic Armadillo must not be presented as measurements of Uaf1 localization. The most precise defensible annotation is an intracellular regulatory protein acting in a pathway controlling cell-surface Arrow, with its exact subcellular site of action unresolved. (spencer2023theusp46deubiquitylase pages 7-9, spencer2023theusp46deubiquitylase pages 12-13, spencer2023theusp46deubiquitylase pages 1-2)
Uaf1’s WD40-repeat architecture fits a binding/regulatory function, not a USP-family catalytic domain. Mechanistic work on homologous complexes describes UAF1/WDR48 and WDR20 as allosteric activators of USP12/USP46: they enhance catalytic turnover without a corresponding increase in substrate-binding affinity. Structural analyses of the homologous USP12 complex describe UAF1 binding away from the catalytic cleft and transmitting conformational changes toward the ubiquitin-binding/catalytic region. This explains how a WD-repeat cofactor could potentiate a protease, but the detailed structural mechanism is inferred for Q1LZ08, not directly resolved in fly Uaf1. (hodul2017functionofthe pages 2-3, villamil2013thewd40repeatproteincontaining pages 7-9, li2021molecularmechanismsof pages 12-15)
A companion October 2023 study found a concordant mechanism in human cells, with developmental support from Xenopus and zebrafish: human USP46–UAF1–WDR20 promoted Wnt/β-catenin signaling, Wnt stimulation increased association with LRP6, and the complex opposed LRP6 ubiquitylation associated with RNF43 and ZNRF3. Experiments also found reduced Wnt-dependent intestinal-organoid viability after USP46/UAF1 perturbation. This is strong evidence that receptor protection is evolutionarily conserved, but human organoid, ligase and localization results should not be attributed as direct experiments on fly Q1LZ08. The human study proposed that removing ubiquitin chains may facilitate assembly of receptor signaling complexes; that more detailed proposal remains distinct from the directly measured fly Uaf1 phenotypes. (ng2023theusp46complex pages 5-6, ng2023theusp46complex pages 1-2, ng2023theusp46complex pages 6-8, ng2023theusp46complex pages 2-3)
The historical name “USP1-associated factor 1” does not establish that fly Uaf1’s principal demonstrated pathway is USP1-mediated DNA repair. In mammals, USP1–UAF1 deubiquitylates FANCD2/FANCI in the Fanconi-anemia pathway and PCNA in DNA-damage tolerance; reconstituted experiments also show a role for UAF1 DNA binding in FANCD2 deubiquitylation. These are well-supported mammalian functions, but the literature examined here does not demonstrate a fly Uaf1–Usp1 interaction, a fly Uaf1-dependent FANCD2/PCNA reaction, a fly Uaf1-specific DNA-repair phenotype or nuclear localization. Such functions are plausible hypotheses from homology, not established annotations for Q1LZ08. (villamil2013thewd40repeatproteincontaining pages 6-7, liang2019dnarequirementin pages 1-2, cukras2016theusp1uaf1complex pages 1-5)
Likewise, a 2012 study genetically implicated the distinct fly protein CG7023, a USP12/USP46-related deubiquitylase, in negative regulation of Notch; its direct USP12–UAF1 biochemical Notch assays used mammalian proteins. It did not test fly Uaf1/CG9062 as the Notch regulator. In the 2023 fly wing-disc study, Uaf1 depletion did not reduce wingless expression, a readout dependent on Notch at the dorsal–ventral boundary, arguing against a general Notch defect in that setting. These observations do not exclude untested context-specific Uaf1 functions. (moretti2012theubiquitinspecificprotease pages 5-6, moretti2012theubiquitinspecificprotease pages 11-12, spencer2023theusp46deubiquitylase pages 1-2)
Annotation recommendation: describe Q1LZ08 as a WD40-repeat-containing, nonenzymatic Usp46-complex cofactor that promotes Wingless/Wnt receptor Arrow stability and signal reception in D. melanogaster. Record Arrow deubiquitylation as an activity of the Usp46–Uaf1–Wdr20 complex, rather than of Uaf1 alone; mark precise Uaf1 subcellular localization, a particular Arrow ubiquitin-linkage preference, and proposed USP1/DNA-repair roles as unresolved or inferred. (spencer2023theusp46deubiquitylase pages 9-10, spencer2023theusp46deubiquitylase pages 12-13, spencer2023theusp46deubiquitylase pages 1-2, liang2019dnarequirementin pages 1-2)
References
(spencer2023theusp46deubiquitylase pages 2-4): Zachary T. Spencer, Victoria H. Ng, Hassina Benchabane, Ghalia Saad Siddiqui, Deepesh Duwadi, Ben Maines, Jamal M. Bryant, Anna Schwarzkopf, Kai Yuan, Sara N. Kassel, Anant Mishra, Ashley Pimentel, Andres M. Lebensohn, Rajat Rohatgi, Scott A. Gerber, David J. Robbins, Ethan Lee, and Yashi Ahmed. The usp46 deubiquitylase complex increases wingless/wnt signaling strength by stabilizing arrow/lrp6. Nature Communications, Oct 2023. URL: https://doi.org/10.1038/s41467-023-41843-0, doi:10.1038/s41467-023-41843-0. This article has 11 citations and is from a highest quality peer-reviewed journal.
(spencer2023theusp46deubiquitylase pages 1-2): Zachary T. Spencer, Victoria H. Ng, Hassina Benchabane, Ghalia Saad Siddiqui, Deepesh Duwadi, Ben Maines, Jamal M. Bryant, Anna Schwarzkopf, Kai Yuan, Sara N. Kassel, Anant Mishra, Ashley Pimentel, Andres M. Lebensohn, Rajat Rohatgi, Scott A. Gerber, David J. Robbins, Ethan Lee, and Yashi Ahmed. The usp46 deubiquitylase complex increases wingless/wnt signaling strength by stabilizing arrow/lrp6. Nature Communications, Oct 2023. URL: https://doi.org/10.1038/s41467-023-41843-0, doi:10.1038/s41467-023-41843-0. This article has 11 citations and is from a highest quality peer-reviewed journal.
(spencer2023theusp46deubiquitylase pages 9-10): Zachary T. Spencer, Victoria H. Ng, Hassina Benchabane, Ghalia Saad Siddiqui, Deepesh Duwadi, Ben Maines, Jamal M. Bryant, Anna Schwarzkopf, Kai Yuan, Sara N. Kassel, Anant Mishra, Ashley Pimentel, Andres M. Lebensohn, Rajat Rohatgi, Scott A. Gerber, David J. Robbins, Ethan Lee, and Yashi Ahmed. The usp46 deubiquitylase complex increases wingless/wnt signaling strength by stabilizing arrow/lrp6. Nature Communications, Oct 2023. URL: https://doi.org/10.1038/s41467-023-41843-0, doi:10.1038/s41467-023-41843-0. This article has 11 citations and is from a highest quality peer-reviewed journal.
(spencer2023theusp46deubiquitylase pages 7-9): Zachary T. Spencer, Victoria H. Ng, Hassina Benchabane, Ghalia Saad Siddiqui, Deepesh Duwadi, Ben Maines, Jamal M. Bryant, Anna Schwarzkopf, Kai Yuan, Sara N. Kassel, Anant Mishra, Ashley Pimentel, Andres M. Lebensohn, Rajat Rohatgi, Scott A. Gerber, David J. Robbins, Ethan Lee, and Yashi Ahmed. The usp46 deubiquitylase complex increases wingless/wnt signaling strength by stabilizing arrow/lrp6. Nature Communications, Oct 2023. URL: https://doi.org/10.1038/s41467-023-41843-0, doi:10.1038/s41467-023-41843-0. This article has 11 citations and is from a highest quality peer-reviewed journal.
(villamil2013thewd40repeatproteincontaining pages 7-9): Mark A. Villamil, Qin Liang, and Zhihao Zhuang. The wd40-repeat protein-containing deubiquitinase complex: catalysis, regulation, and potential for therapeutic intervention. Cell Biochemistry and Biophysics, 67:111-126, Jun 2013. URL: https://doi.org/10.1007/s12013-013-9637-1, doi:10.1007/s12013-013-9637-1. This article has 51 citations and is from a peer-reviewed journal.
(spencer2023theusp46deubiquitylase pages 4-7): Zachary T. Spencer, Victoria H. Ng, Hassina Benchabane, Ghalia Saad Siddiqui, Deepesh Duwadi, Ben Maines, Jamal M. Bryant, Anna Schwarzkopf, Kai Yuan, Sara N. Kassel, Anant Mishra, Ashley Pimentel, Andres M. Lebensohn, Rajat Rohatgi, Scott A. Gerber, David J. Robbins, Ethan Lee, and Yashi Ahmed. The usp46 deubiquitylase complex increases wingless/wnt signaling strength by stabilizing arrow/lrp6. Nature Communications, Oct 2023. URL: https://doi.org/10.1038/s41467-023-41843-0, doi:10.1038/s41467-023-41843-0. This article has 11 citations and is from a highest quality peer-reviewed journal.
(spencer2023theusp46deubiquitylase pages 4-4): Zachary T. Spencer, Victoria H. Ng, Hassina Benchabane, Ghalia Saad Siddiqui, Deepesh Duwadi, Ben Maines, Jamal M. Bryant, Anna Schwarzkopf, Kai Yuan, Sara N. Kassel, Anant Mishra, Ashley Pimentel, Andres M. Lebensohn, Rajat Rohatgi, Scott A. Gerber, David J. Robbins, Ethan Lee, and Yashi Ahmed. The usp46 deubiquitylase complex increases wingless/wnt signaling strength by stabilizing arrow/lrp6. Nature Communications, Oct 2023. URL: https://doi.org/10.1038/s41467-023-41843-0, doi:10.1038/s41467-023-41843-0. This article has 11 citations and is from a highest quality peer-reviewed journal.
(spencer2023theusp46deubiquitylase pages 12-13): Zachary T. Spencer, Victoria H. Ng, Hassina Benchabane, Ghalia Saad Siddiqui, Deepesh Duwadi, Ben Maines, Jamal M. Bryant, Anna Schwarzkopf, Kai Yuan, Sara N. Kassel, Anant Mishra, Ashley Pimentel, Andres M. Lebensohn, Rajat Rohatgi, Scott A. Gerber, David J. Robbins, Ethan Lee, and Yashi Ahmed. The usp46 deubiquitylase complex increases wingless/wnt signaling strength by stabilizing arrow/lrp6. Nature Communications, Oct 2023. URL: https://doi.org/10.1038/s41467-023-41843-0, doi:10.1038/s41467-023-41843-0. This article has 11 citations and is from a highest quality peer-reviewed journal.
(spencer2023theusp46deubiquitylase pages 10-11): Zachary T. Spencer, Victoria H. Ng, Hassina Benchabane, Ghalia Saad Siddiqui, Deepesh Duwadi, Ben Maines, Jamal M. Bryant, Anna Schwarzkopf, Kai Yuan, Sara N. Kassel, Anant Mishra, Ashley Pimentel, Andres M. Lebensohn, Rajat Rohatgi, Scott A. Gerber, David J. Robbins, Ethan Lee, and Yashi Ahmed. The usp46 deubiquitylase complex increases wingless/wnt signaling strength by stabilizing arrow/lrp6. Nature Communications, Oct 2023. URL: https://doi.org/10.1038/s41467-023-41843-0, doi:10.1038/s41467-023-41843-0. This article has 11 citations and is from a highest quality peer-reviewed journal.
(hodul2017functionofthe pages 2-3): Molly Hodul, Caroline L. Dahlberg, and Peter Juo. Function of the deubiquitinating enzyme usp46 in the nervous system and its regulation by wd40-repeat proteins. Frontiers in Synaptic Neuroscience, Dec 2017. URL: https://doi.org/10.3389/fnsyn.2017.00016, doi:10.3389/fnsyn.2017.00016. This article has 17 citations.
(li2021molecularmechanismsof pages 12-15): Ying Li and David Reverter. Molecular mechanisms of dubs regulation in signaling and disease. International Journal of Molecular Sciences, 22:986, Jan 2021. URL: https://doi.org/10.3390/ijms22030986, doi:10.3390/ijms22030986. This article has 121 citations.
(ng2023theusp46complex pages 5-6): Victoria H. Ng, Zachary Spencer, Leif R. Neitzel, Anmada Nayak, Matthew A. Loberg, Chen Shen, Sara N. Kassel, Heather K. Kroh, Zhenyi An, Christin C. Anthony, Jamal M. Bryant, Amanda Lawson, Lily Goldsmith, Hassina Benchabane, Amanda G. Hansen, Jingjing Li, Starina D’Souza, Andres M. Lebensohn, Rajat Rohatgi, William A. Weiss, Vivian L. Weiss, Charles Williams, Charles C. Hong, David J. Robbins, Yashi Ahmed, and Ethan Lee. The usp46 complex deubiquitylates lrp6 to promote wnt/β-catenin signaling. Nature Communications, Oct 2023. URL: https://doi.org/10.1038/s41467-023-41836-z, doi:10.1038/s41467-023-41836-z. This article has 29 citations and is from a highest quality peer-reviewed journal.
(ng2023theusp46complex pages 1-2): Victoria H. Ng, Zachary Spencer, Leif R. Neitzel, Anmada Nayak, Matthew A. Loberg, Chen Shen, Sara N. Kassel, Heather K. Kroh, Zhenyi An, Christin C. Anthony, Jamal M. Bryant, Amanda Lawson, Lily Goldsmith, Hassina Benchabane, Amanda G. Hansen, Jingjing Li, Starina D’Souza, Andres M. Lebensohn, Rajat Rohatgi, William A. Weiss, Vivian L. Weiss, Charles Williams, Charles C. Hong, David J. Robbins, Yashi Ahmed, and Ethan Lee. The usp46 complex deubiquitylates lrp6 to promote wnt/β-catenin signaling. Nature Communications, Oct 2023. URL: https://doi.org/10.1038/s41467-023-41836-z, doi:10.1038/s41467-023-41836-z. This article has 29 citations and is from a highest quality peer-reviewed journal.
(ng2023theusp46complex pages 2-3): Victoria H. Ng, Zachary Spencer, Leif R. Neitzel, Anmada Nayak, Matthew A. Loberg, Chen Shen, Sara N. Kassel, Heather K. Kroh, Zhenyi An, Christin C. Anthony, Jamal M. Bryant, Amanda Lawson, Lily Goldsmith, Hassina Benchabane, Amanda G. Hansen, Jingjing Li, Starina D’Souza, Andres M. Lebensohn, Rajat Rohatgi, William A. Weiss, Vivian L. Weiss, Charles Williams, Charles C. Hong, David J. Robbins, Yashi Ahmed, and Ethan Lee. The usp46 complex deubiquitylates lrp6 to promote wnt/β-catenin signaling. Nature Communications, Oct 2023. URL: https://doi.org/10.1038/s41467-023-41836-z, doi:10.1038/s41467-023-41836-z. This article has 29 citations and is from a highest quality peer-reviewed journal.
(ng2023theusp46complex pages 3-5): Victoria H. Ng, Zachary Spencer, Leif R. Neitzel, Anmada Nayak, Matthew A. Loberg, Chen Shen, Sara N. Kassel, Heather K. Kroh, Zhenyi An, Christin C. Anthony, Jamal M. Bryant, Amanda Lawson, Lily Goldsmith, Hassina Benchabane, Amanda G. Hansen, Jingjing Li, Starina D’Souza, Andres M. Lebensohn, Rajat Rohatgi, William A. Weiss, Vivian L. Weiss, Charles Williams, Charles C. Hong, David J. Robbins, Yashi Ahmed, and Ethan Lee. The usp46 complex deubiquitylates lrp6 to promote wnt/β-catenin signaling. Nature Communications, Oct 2023. URL: https://doi.org/10.1038/s41467-023-41836-z, doi:10.1038/s41467-023-41836-z. This article has 29 citations and is from a highest quality peer-reviewed journal.
(villamil2013thewd40repeatproteincontaining pages 6-7): Mark A. Villamil, Qin Liang, and Zhihao Zhuang. The wd40-repeat protein-containing deubiquitinase complex: catalysis, regulation, and potential for therapeutic intervention. Cell Biochemistry and Biophysics, 67:111-126, Jun 2013. URL: https://doi.org/10.1007/s12013-013-9637-1, doi:10.1007/s12013-013-9637-1. This article has 51 citations and is from a peer-reviewed journal.
(cukras2016theusp1uaf1complex pages 7-9): Scott Cukras, Euiho Lee, Emily Palumbo, Pamela Benavidez, George-Lucian Moldovan, and Younghoon Kee. The usp1-uaf1 complex interacts with rad51ap1 to promote homologous recombination repair. Cell Cycle, 15:2636-2646, Aug 2016. URL: https://doi.org/10.1080/15384101.2016.1209613, doi:10.1080/15384101.2016.1209613. This article has 48 citations and is from a peer-reviewed journal.
(liang2019dnarequirementin pages 1-2): Fengshan Liang, Adam S. Miller, Simonne Longerich, Caroline Tang, David Maranon, Elizabeth A. Williamson, Robert Hromas, Claudia Wiese, Gary M. Kupfer, and Patrick Sung. Dna requirement in fancd2 deubiquitination by usp1-uaf1-rad51ap1 in the fanconi anemia dna damage response. Nature Communications, Jun 2019. URL: https://doi.org/10.1038/s41467-019-10408-5, doi:10.1038/s41467-019-10408-5. This article has 74 citations and is from a highest quality peer-reviewed journal.
(villamil2013thewd40repeatproteincontaining pages 1-3): Mark A. Villamil, Qin Liang, and Zhihao Zhuang. The wd40-repeat protein-containing deubiquitinase complex: catalysis, regulation, and potential for therapeutic intervention. Cell Biochemistry and Biophysics, 67:111-126, Jun 2013. URL: https://doi.org/10.1007/s12013-013-9637-1, doi:10.1007/s12013-013-9637-1. This article has 51 citations and is from a peer-reviewed journal.
(spencer2023theusp46deubiquitylase pages 11-12): Zachary T. Spencer, Victoria H. Ng, Hassina Benchabane, Ghalia Saad Siddiqui, Deepesh Duwadi, Ben Maines, Jamal M. Bryant, Anna Schwarzkopf, Kai Yuan, Sara N. Kassel, Anant Mishra, Ashley Pimentel, Andres M. Lebensohn, Rajat Rohatgi, Scott A. Gerber, David J. Robbins, Ethan Lee, and Yashi Ahmed. The usp46 deubiquitylase complex increases wingless/wnt signaling strength by stabilizing arrow/lrp6. Nature Communications, Oct 2023. URL: https://doi.org/10.1038/s41467-023-41843-0, doi:10.1038/s41467-023-41843-0. This article has 11 citations and is from a highest quality peer-reviewed journal.
(ng2023theusp46complex pages 6-8): Victoria H. Ng, Zachary Spencer, Leif R. Neitzel, Anmada Nayak, Matthew A. Loberg, Chen Shen, Sara N. Kassel, Heather K. Kroh, Zhenyi An, Christin C. Anthony, Jamal M. Bryant, Amanda Lawson, Lily Goldsmith, Hassina Benchabane, Amanda G. Hansen, Jingjing Li, Starina D’Souza, Andres M. Lebensohn, Rajat Rohatgi, William A. Weiss, Vivian L. Weiss, Charles Williams, Charles C. Hong, David J. Robbins, Yashi Ahmed, and Ethan Lee. The usp46 complex deubiquitylates lrp6 to promote wnt/β-catenin signaling. Nature Communications, Oct 2023. URL: https://doi.org/10.1038/s41467-023-41836-z, doi:10.1038/s41467-023-41836-z. This article has 29 citations and is from a highest quality peer-reviewed journal.
(cukras2016theusp1uaf1complex pages 1-5): Scott Cukras, Euiho Lee, Emily Palumbo, Pamela Benavidez, George-Lucian Moldovan, and Younghoon Kee. The usp1-uaf1 complex interacts with rad51ap1 to promote homologous recombination repair. Cell Cycle, 15:2636-2646, Aug 2016. URL: https://doi.org/10.1080/15384101.2016.1209613, doi:10.1080/15384101.2016.1209613. This article has 48 citations and is from a peer-reviewed journal.
(moretti2012theubiquitinspecificprotease pages 5-6): Julien Moretti, Patricia Chastagner, Chih-Chao Liang, Martin A. Cohn, Alain Israël, and Christel Brou. The ubiquitin-specific protease 12 (usp12) is a negative regulator of notch signaling acting on notch receptor trafficking toward degradation. Journal of Biological Chemistry, 287:29429-29441, Aug 2012. URL: https://doi.org/10.1074/jbc.m112.366807, doi:10.1074/jbc.m112.366807. This article has 73 citations and is from a domain leading peer-reviewed journal.
(moretti2012theubiquitinspecificprotease pages 11-12): Julien Moretti, Patricia Chastagner, Chih-Chao Liang, Martin A. Cohn, Alain Israël, and Christel Brou. The ubiquitin-specific protease 12 (usp12) is a negative regulator of notch signaling acting on notch receptor trafficking toward degradation. Journal of Biological Chemistry, 287:29429-29441, Aug 2012. URL: https://doi.org/10.1074/jbc.m112.366807, doi:10.1074/jbc.m112.366807. This article has 73 citations and is from a domain leading peer-reviewed journal.