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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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 literature reviewed here matches the UniProt entry Q96K19 for Homo sapiens RNF170, described experimentally as an ER membrane, RING-type E3 ubiquitin ligase that regulates ER-associated degradation (ERAD) of activated inositol 1,4,5-trisphosphate receptors (IP3Rs) and is genetically linked to hereditary spastic paraplegia (HSP). (lu2011rnf170proteinan pages 4-5, wagner2019biallelicvariantsin pages 6-7)
RNF170 is a RING-HC E3 ubiquitin ligase: it promotes transfer of ubiquitin from an E2 enzyme to a substrate protein, typically creating polyubiquitin chains that control substrate fate (often proteasomal degradation). In vitro, immunopurified RNF170 catalyzes ubiquitin conjugation in the presence of E1 (UBE1), E2 (UbcH5b), and ubiquitin, producing a high-molecular-weight ubiquitin “smear,” consistent with intrinsic ligase activity. (lu2011rnf170proteinan pages 4-5, lu2011rnf170proteinan pages 3-4)
A key mechanistic validation is that mutating zinc-coordinating residues in the RING domain (Cys101/His103) abolishes ligase activity, establishing the catalytic dependence on the RING motif. (lu2011rnf170proteinan pages 3-4)
Activated IP3Rs undergo rapid down-regulation via the ubiquitin–proteasome pathway, a form of ERAD-like quality control applied to an activated signaling channel. RNF170 has been described as (at the time of foundational studies) the only E3 ligase directly demonstrated to mediate IP3R ubiquitination in this context, with recruitment to activated IP3Rs preceding robust polyubiquitination and downstream processing. (lu2011rnf170proteinan pages 5-6, lu2011rnf170proteinan pages 3-4)
ERLIN1/2 are ER membrane SPFH-family proteins that assemble into large oligomeric scaffolds in cholesterol-enriched ER nanodomains. These scaffolds act as platforms to recruit factors including RNF170, and (per 2024 work) can bridge RNF170 to other clients such as TMUB1-L, connecting ubiquitin machinery to ER lipid organization and secretory function. (veronese2024erlin12scaffoldsbridge pages 1-2, veronese2024erlin12scaffoldsbridge pages 12-12)
RNF170 is an integral ER membrane protein, with topology predictions and biochemical fractionation placing the N-terminus in the ER lumen and the RING domain/C-terminus in the cytosol, consistent with ubiquitination of cytosolic lysines on substrates such as IP3Rs. (lu2011rnf170proteinan pages 3-4, lu2011rnf170proteinan pages 4-5)
Foundational mechanistic work demonstrated that RNF170 rapidly associates with activated IP3R1, and depletion of RNF170 reduces stimulus-induced IP3R1 polyubiquitination and slows receptor down-regulation. (lu2011rnf170proteinan pages 4-5, lu2011rnf170proteinan pages 3-4)
Quantitatively, RNF170 knockdown reduced agonist-induced IP3R1 polyubiquitination to 57 ± 7% of control and inhibited IP3R1 down-regulation by ~50%, while also increasing basal IP3R1 levels. (lu2011rnf170proteinan pages 4-5, lu2011rnf170proteinan media b065ce9e)
Mechanistically, RNF170 recruitment to activated IP3Rs occurs via constitutive association with ERLIN1/2, which are required for efficient RNF170–IP3R coupling. (lu2011rnf170proteinan pages 8-9, lu2011rnf170proteinan pages 5-6)
A separate, well-developed mechanistic line of evidence (in murine systems) identifies RNF170 as a negative regulator of innate immunity through direct targeting of TLR3. RNF170 binds the TLR3 TIR domain and catalyzes K48-linked polyubiquitination at TLR3 Lys766, promoting proteasomal degradation; this requires intact RNF170 RING residues (C101/H103) and is blocked by proteasome inhibition (MG132), supported by CHX chase assays and in vivo phenotyping in Rnf170−/− mice. (song2020e3ubiquitinligase pages 6-7, song2020e3ubiquitinligase pages 7-9)
Because this primary study is performed in murine cells and mice, extension to human physiology should be made cautiously, although the TLR3 K766 site is noted as conserved between mouse and human in the primary study. (song2020e3ubiquitinligase pages 7-9)
RNF170 is reported to be constitutively associated with the ERLIN1/2 complex, which recruits RNF170 to activated IP3Rs to drive ubiquitination and proteasomal processing. (lu2011rnf170proteinan pages 8-9, lu2011rnf170proteinan pages 5-6)
Proteomics of ER-resident E3 ligase complexes has independently recovered RNF170 with high-confidence interactors including ERLIN1, ERLIN2, and ITPR3, supporting the recurring architecture of this module in ERAD/proteostasis networks. (lari2016resolutionofproteotoxic pages 111-115)
A major 2024 development is the proposal that ERLIN1/2 scaffolds bind a conserved luminal N-terminal motif present in RNF170 and the long isoform of TMUB1 (TMUB1-L), bridging these proteins in cholesterol-rich ER nanodomains. AlphaFold-Multimer modeling supports interaction interfaces between the conserved motifs and adjacent ERLIN subunits. (veronese2024erlin12scaffoldsbridge pages 4-6, veronese2024erlin12scaffoldsbridge pages 12-12)
Functionally, ERLIN loss (DKO) leads to increased cholesterol esterification and lipid droplet accumulation, ER tubule collapse, Golgi fragmentation, and impaired secretory trafficking, with rescue by ERLIN re-expression or pharmacologic inhibition of cholesterol esterification (SOAT1 inhibitor avasimibe). (veronese2024erlin12scaffoldsbridge pages 10-12, veronese2024erlin12scaffoldsbridge pages 12-12)
By controlling stimulus-dependent degradation of activated IP3Rs, RNF170 is positioned as a regulator of ER Ca2+ release signaling dynamics, linking receptor activation state to ERAD engagement. (wagner2019biallelicvariantsin pages 6-7, lu2011rnf170proteinan pages 5-6)
In patient-derived or engineered RNF170-deficient models, increased basal IP3R levels (cell-type-specific isoforms) and failure of stimulus-dependent IP3R reduction support the concept that RNF170 constrains IP3R abundance and signaling. (wagner2019biallelicvariantsin pages 6-7)
RNF170-mediated proteasomal removal of TLR3 reduces downstream IRF3/NF-κB/STAT1-linked transcriptional activity and cytokine production in TLR3 pathways, positioning RNF170 as a negative regulator of TLR3-dependent antiviral inflammation in murine models. (song2020e3ubiquitinligase pages 6-7, song2020e3ubiquitinligase pages 7-9)
2024 reviews summarize RNF170 in this role primarily by citing the 2020 primary study, without adding additional mechanistic detail in the excerpted sections. (wang2024hostfactorsmodulate pages 13-14, li2024thernabindingproteins pages 12-13)
A key primary genetics study provides evidence that biallelic RNF170 variants are a cause of autosomal recessive HSP, supported by functional validation across patient fibroblasts, neuronal cells, and zebrafish assays. (wagner2019biallelicvariantsin pages 6-7)
Mechanistically, patient-derived fibroblasts fail to show physiological stimulus-dependent degradation of IP3R-3, and RNF170 knockout neuronal SH-SY5Y cells show elevated basal IP3R-1 with rescue by re-expression of wild-type RNF170. (wagner2019biallelicvariantsin pages 6-7)
Quantitatively, this study reports zebrafish developmental phenotypes and statistical testing (e.g., embryo length and eye size differences with adjusted P < 0.0001) supporting functional impairment of tested patient variants relative to RNF170wt. (wagner2019biallelicvariantsin pages 6-7)
Open Targets disease–target evidence links RNF170 to hereditary spastic paraplegia and complex hereditary spastic paraplegia, with literature evidence pointing to PubMed ID 31636353 / PMC6803694. (OpenTargets Search: hereditary spastic paraplegia,spastic paraplegia,sensory ataxia,spinocerebellar ataxia,neuroaxonal dystrophy-RNF170)
A 2024 Trends in Neurosciences review emphasizes ER structure and protein quality-control pathways as central mechanisms in inherited neuropathies, HSP, and ataxias, and explicitly notes RNF170 as an E3 ligase associated with recessive HSP and inherited peripheral neuropathy. (vondel2024overarchingpathomechanismsin pages 5-8)
Consistent pathway-context evidence from 2024 human genetics (ERLIN1 series) supports the broader ERLIN1/2–RNF170–IP3R ERAD module as disease-relevant: in a cohort of 13 individuals with biallelic ERLIN1 variants (SPG62), the authors describe ERLIN1/2 as recruiting RNF170 to degrade activated IP3R1 and provide cohort-level statistics (e.g., mean onset 1.8 years; corpus callosum anomalies 5/13; founder splice variant in 6 individuals). Although ERLIN1 is not RNF170, these data reinforce the clinical relevance of the RNF170-centered module. (cogan2024biallelicvariantsin pages 1-6, cogan2024biallelicvariantsin pages 12-16)
Veronese et al. (Life Science Alliance; May 2024) propose that ERLIN scaffolds directly bind cholesterol and restrain cholesterol esterification, thereby maintaining ER cholesterol accessibility for ER→Golgi transport; the ERLIN scaffolds concurrently organize RNF170 and TMUB1-L via conserved luminal motifs. Loss of ERLINs increases cholesterol esterification (including CE 18:1), enlarges lipid droplets, fragments Golgi, and disrupts secretory trafficking and migration phenotypes; SOAT1 inhibition by avasimibe rescues multiple phenotypes. (veronese2024erlin12scaffoldsbridge pages 10-12, veronese2024erlin12scaffoldsbridge pages 12-12)
Quantitative details reported include proteomics showing a trend toward increased SOAT1 abundance (log2FC 0.40; q=0.07) and phenotyping with N=3 biological replicates and large cell counts (≥130 cells for lipid droplet size; ≥340 for Golgi fragmentation) analyzed by ANOVA with Tukey post hoc tests. (veronese2024erlin12scaffoldsbridge pages 12-12, veronese2024erlin12scaffoldsbridge pages 10-12)
Cogan et al. (Human Genetics; Oct 2024) frame ERLIN1/2 as ERAD organizers that associate with RNF170 to target activated IP3Rs, and expand genotype–phenotype characterization in ERLIN-related HSP. This strengthens the view (also consistent with RNF170 HSP genetics) that motor neurons are unusually sensitive to disruption of this ERAD-linked calcium signaling module. (cogan2024biallelicvariantsin pages 1-6, cogan2024biallelicvariantsin pages 12-16)
RNF170 is now a disease gene supported by primary genetics and functional validation for HSP, supporting its inclusion in neurogenetic diagnostic panels for spastic paraplegia/ataxia phenotypes and for variant interpretation workflows. (wagner2019biallelicvariantsin pages 6-7, vondel2024overarchingpathomechanismsin pages 5-8)
The RNF170-centered mechanism suggests two translationally relevant intervention layers:
1) IP3R signaling / ER Ca2+ homeostasis: human genetics and functional data prioritize the IP3R degradation/signaling axis as a candidate therapeutic pathway in HSP. (wagner2019biallelicvariantsin pages 6-7)
2) ER cholesterol esterification / secretory pathway: 2024 mechanistic work identifies cholesterol esterification control as a modifiable node in ERLIN-module dysfunction, with SOAT1 inhibition (avasimibe) rescuing cell phenotypes (lipid droplet size, Golgi morphology, and gene-expression readouts). This is not a direct RNF170-targeting therapy, but it provides a mechanism-based proof-of-concept for pharmacologic modulation of ERLIN–RNF170-associated ER nanodomain functions. (veronese2024erlin12scaffoldsbridge pages 10-12, veronese2024erlin12scaffoldsbridge pages 12-12)
A 2024 expert review in Trends in Neurosciences highlights ER structure and protein quality-control pathways (UPS/autophagy) as overarching mechanisms in inherited neuropathies, HSP, and ataxias, and includes RNF170 among implicated E3 ligases, supporting a convergent “ER homeostasis / QC” framing for RNF170-related disease mechanisms. (vondel2024overarchingpathomechanismsin pages 5-8)
Genetics-focused 2024 work on ERLIN1 (SPG62) similarly emphasizes that the ERLIN1/2–RNF170 module is expected to impair IP3R1 turnover and Ca2+ signaling, providing additional disease-mechanism coherence at the pathway level. (cogan2024biallelicvariantsin pages 12-16)
The following table consolidates the most evidence-supported statements for functional annotation.
| Category | Summary |
|---|---|
| Identity/domains | - Human RNF170 corresponds to UniProt Q96K19, a RING-type E3 ubiquitin ligase studied as an ER-membrane regulator of protein turnover and signaling. - Foundational work defines RNF170 as a 257 aa RING-HC protein with catalytic dependence on Cys101/His103; this matches the UniProt RING-domain annotation and ER-associated function. (lu2011rnf170proteinan pages 4-5, lu2011rnf170proteinan pages 3-4) |
| Localization/topology | - RNF170 is an integral endoplasmic reticulum (ER) membrane protein. - Topology predictions and biochemical fractionation place its N-terminus in the ER lumen and its RING domain/C-terminus in the cytosol, positioning the catalytic machinery to ubiquitinate cytosolic receptor lysines. - RNF170 localizes in ERLIN-positive cholesterol-rich ER nanodomains. (lu2011rnf170proteinan pages 4-5, lu2011rnf170proteinan pages 3-4, veronese2024erlin12scaffoldsbridge pages 1-2) |
| Core enzymatic activity | - RNF170 catalyzes E3 ubiquitin transfer in vitro using UBE1 + UbcH5b and ubiquitin, generating a high-molecular-weight ubiquitin smear typical of ligase activity. - Catalysis is lost with RING mutant C101S/H103A, confirming dependence on the RING domain. - Functionally, RNF170 promotes proteasome-directed ER-associated degradation (ERAD) of selected membrane/signaling proteins. (lu2011rnf170proteinan pages 4-5, lu2011rnf170proteinan pages 3-4, song2020e3ubiquitinligase pages 6-7) |
| Key substrates | - Best-supported human substrate class: activated IP3 receptors (IP3Rs), especially IP3R1/IP3R3, which undergo RNF170-dependent ubiquitination and degradation after stimulation. - In murine innate immunity studies, RNF170 also targets TLR3, catalyzing K48-linked polyubiquitination at K766 to drive proteasomal degradation. - TLR3 regulation is strongly supported experimentally, but species context should be noted because the primary paper is in murine cells/mice. (wagner2019biallelicvariantsin pages 6-7, lu2011rnf170proteinan pages 4-5, song2020e3ubiquitinligase pages 6-7, song2020e3ubiquitinligase pages 1-2, song2020e3ubiquitinligase pages 7-9) |
| Key interactors/complex | - RNF170 is constitutively associated with the ERLIN1/2 complex, which recruits it to activated IP3Rs. - It is also found in complexes containing p97/VCP-associated ERAD machinery and, in 2024 work, TMUB1-L bridged by ERLIN scaffolds. - Proteomics and co-IP studies repeatedly enrich ERLIN1, ERLIN2, ITPR3, TMUB1, TMEM259 with RNF170-centered complexes. (lu2011rnf170proteinan pages 8-9, lari2016resolutionofproteotoxic pages 111-115, veronese2024erlin12scaffoldsbridge pages 1-2, veronese2024erlin12scaffoldsbridge pages 12-12) |
| Pathways | - RNF170 acts in ERAD/proteostasis, especially stimulus-coupled degradation of activated IP3Rs. - Through IP3R turnover, RNF170 regulates ER Ca2+ release signaling and is therefore connected to neurodegeneration-relevant calcium homeostasis pathways. - Separate immune work places RNF170 in TLR3 innate immune signaling as a negative regulator limiting IRF3/NF-kB/STAT1 outputs by degrading TLR3. (wagner2019biallelicvariantsin pages 6-7, lu2011rnf170proteinan pages 5-6, song2020e3ubiquitinligase pages 6-7, vondel2024overarchingpathomechanismsin pages 5-8) |
| Disease associations | - Biallelic loss-of-function RNF170 variants cause autosomal recessive hereditary spastic paraplegia (HSP), with Open Targets evidence mapped to hereditary/complex HSP. - Earlier literature also linked a dominant sensory ataxia phenotype to RNF170 mutation, and mouse knockout models show age-dependent gait abnormalities. - Expert 2024 synthesis places RNF170 within an ER homeostasis/quality-control disease module shared across HSP, ataxia, and related neurodegenerative disorders. (wagner2019biallelicvariantsin pages 6-7, lu2011rnf170proteinan pages 8-9, OpenTargets Search: hereditary spastic paraplegia,spastic paraplegia,sensory ataxia,spinocerebellar ataxia,neuroaxonal dystrophy-RNF170, vondel2024overarchingpathomechanismsin pages 5-8) |
| Recent 2024 developments | - Veronese et al. 2024 propose that ERLIN1/2 ring-like scaffolds bind a conserved luminal motif in RNF170 and TMUB1-L, organizing them in cholesterol-rich ER nanodomains. - This work expands RNF170 biology beyond IP3R degradation by linking the ERLIN–RNF170 module to cholesterol esterification control, Golgi morphology, and secretory pathway regulation. - 2024 disease reviews and genetics papers further emphasize the ERLIN1/2–RNF170–IP3R axis as a recurrent neurogenetic mechanism in spastic paraplegia/ataxia. (veronese2024erlin12scaffoldsbridge pages 12-12, veronese2024erlin12scaffoldsbridge pages 4-6, veronese2024erlin12scaffoldsbridge pages 10-12, cogan2024biallelicvariantsin pages 1-6, vondel2024overarchingpathomechanismsin pages 5-8) |
| Quantitative data points | - RNF170 knockdown reduced agonist-induced IP3R1 polyubiquitination to 57 ± 7% of control, inhibited IP3R1 down-regulation by roughly ~50%, and increased basal IP3R1 by ~27 ± 11%. (lu2011rnf170proteinan pages 4-5) - In RNF170-deficient models, IP3R3 rose by about ~4-fold in patient fibroblasts and IP3R1 by ~1.8-fold in RNF170-knockout SH-SY5Y cells. (gehweiler2024rnf170anoveldisease pages 68-72) - 2024 ERLIN-loss proteomics/lipidomics reported SOAT1 log2FC = 0.40, q = 0.07 and phenotyping with N = 3 biological replicates, including ≥130 cells for lipid-droplet size and ≥340 cells for Golgi fragmentation. (veronese2024erlin12scaffoldsbridge pages 12-12, veronese2024erlin12scaffoldsbridge pages 10-12) |
Table: This table condenses the key verified facts about human RNF170 (UniProt Q96K19), including its identity, ER localization, E3 ligase function, substrates, complexes, disease relevance, and notable 2024 advances. It is useful as a quick-reference annotation scaffold anchored to specific evidence contexts.
A figure supporting RNF170’s quantitative effect on IP3R1 ubiquitination and down-regulation is available from Lu et al. 2011 (Figure 5A-B). (lu2011rnf170proteinan media b065ce9e)
References
(lu2011rnf170proteinan pages 4-5): Justine P. Lu, Yuan Wang, Danielle A. Sliter, Margaret M.P. Pearce, and Richard J.H. Wojcikiewicz. Rnf170 protein, an endoplasmic reticulum membrane ubiquitin ligase, mediates inositol 1,4,5-trisphosphate receptor ubiquitination and degradation. Journal of Biological Chemistry, 286:24426-24433, Jul 2011. URL: https://doi.org/10.1074/jbc.m111.251983, doi:10.1074/jbc.m111.251983. This article has 134 citations and is from a domain leading peer-reviewed journal.
(wagner2019biallelicvariantsin pages 6-7): Matias Wagner, Daniel P. S. Osborn, Ina Gehweiler, Maike Nagel, Ulrike Ulmer, Somayeh Bakhtiari, Rim Amouri, Reza Boostani, Faycal Hentati, Maryam M. Hockley, Benedikt Hölbling, Thomas Schwarzmayr, Ehsan Ghayoor Karimiani, Christoph Kernstock, Reza Maroofian, Wolfgang Müller-Felber, Ege Ozkan, Sergio Padilla-Lopez, Selina Reich, Jennifer Reichbauer, Hossein Darvish, Neda Shahmohammadibeni, Abbas Tafakhori, Katharina Vill, Stephan Zuchner, Michael C. Kruer, Juliane Winkelmann, Yalda Jamshidi, and Rebecca Schüle. Bi-allelic variants in rnf170 are associated with hereditary spastic paraplegia. Nature Communications, Oct 2019. URL: https://doi.org/10.1038/s41467-019-12620-9, doi:10.1038/s41467-019-12620-9. This article has 62 citations and is from a highest quality peer-reviewed journal.
(lu2011rnf170proteinan pages 3-4): Justine P. Lu, Yuan Wang, Danielle A. Sliter, Margaret M.P. Pearce, and Richard J.H. Wojcikiewicz. Rnf170 protein, an endoplasmic reticulum membrane ubiquitin ligase, mediates inositol 1,4,5-trisphosphate receptor ubiquitination and degradation. Journal of Biological Chemistry, 286:24426-24433, Jul 2011. URL: https://doi.org/10.1074/jbc.m111.251983, doi:10.1074/jbc.m111.251983. This article has 134 citations and is from a domain leading peer-reviewed journal.
(lu2011rnf170proteinan pages 5-6): Justine P. Lu, Yuan Wang, Danielle A. Sliter, Margaret M.P. Pearce, and Richard J.H. Wojcikiewicz. Rnf170 protein, an endoplasmic reticulum membrane ubiquitin ligase, mediates inositol 1,4,5-trisphosphate receptor ubiquitination and degradation. Journal of Biological Chemistry, 286:24426-24433, Jul 2011. URL: https://doi.org/10.1074/jbc.m111.251983, doi:10.1074/jbc.m111.251983. This article has 134 citations and is from a domain leading peer-reviewed journal.
(veronese2024erlin12scaffoldsbridge pages 1-2): Matteo Veronese, Sebastian Kallabis, Alexander Tobias Kaczmarek, Anushka Das, Lennart Robers, Simon Schumacher, Alessia Lofrano, Susanne Brodesser, Stefan Müller, Kay Hofmann, Marcus Krüger, and Elena I Rugarli. Erlin1/2 scaffolds bridge tmub1 and rnf170 and restrict cholesterol esterification to regulate the secretory pathway. Life Science Alliance, 7:e202402620, May 2024. URL: https://doi.org/10.26508/lsa.202402620, doi:10.26508/lsa.202402620. This article has 8 citations and is from a peer-reviewed journal.
(veronese2024erlin12scaffoldsbridge pages 12-12): Matteo Veronese, Sebastian Kallabis, Alexander Tobias Kaczmarek, Anushka Das, Lennart Robers, Simon Schumacher, Alessia Lofrano, Susanne Brodesser, Stefan Müller, Kay Hofmann, Marcus Krüger, and Elena I Rugarli. Erlin1/2 scaffolds bridge tmub1 and rnf170 and restrict cholesterol esterification to regulate the secretory pathway. Life Science Alliance, 7:e202402620, May 2024. URL: https://doi.org/10.26508/lsa.202402620, doi:10.26508/lsa.202402620. This article has 8 citations and is from a peer-reviewed journal.
(lu2011rnf170proteinan media b065ce9e): Justine P. Lu, Yuan Wang, Danielle A. Sliter, Margaret M.P. Pearce, and Richard J.H. Wojcikiewicz. Rnf170 protein, an endoplasmic reticulum membrane ubiquitin ligase, mediates inositol 1,4,5-trisphosphate receptor ubiquitination and degradation. Journal of Biological Chemistry, 286:24426-24433, Jul 2011. URL: https://doi.org/10.1074/jbc.m111.251983, doi:10.1074/jbc.m111.251983. This article has 134 citations and is from a domain leading peer-reviewed journal.
(lu2011rnf170proteinan pages 8-9): Justine P. Lu, Yuan Wang, Danielle A. Sliter, Margaret M.P. Pearce, and Richard J.H. Wojcikiewicz. Rnf170 protein, an endoplasmic reticulum membrane ubiquitin ligase, mediates inositol 1,4,5-trisphosphate receptor ubiquitination and degradation. Journal of Biological Chemistry, 286:24426-24433, Jul 2011. URL: https://doi.org/10.1074/jbc.m111.251983, doi:10.1074/jbc.m111.251983. This article has 134 citations and is from a domain leading peer-reviewed journal.
(song2020e3ubiquitinligase pages 6-7): Xiaoqi Song, Shuo Liu, Wen-die Wang, Zhong-fei Ma, Xuetao Cao, and Minghong Jiang. E3 ubiquitin ligase rnf170 inhibits innate immune responses by targeting and degrading tlr3 in murine cells. Cellular & Molecular Immunology, 17:865-874, May 2020. URL: https://doi.org/10.1038/s41423-019-0236-y, doi:10.1038/s41423-019-0236-y. This article has 28 citations and is from a peer-reviewed journal.
(song2020e3ubiquitinligase pages 7-9): Xiaoqi Song, Shuo Liu, Wen-die Wang, Zhong-fei Ma, Xuetao Cao, and Minghong Jiang. E3 ubiquitin ligase rnf170 inhibits innate immune responses by targeting and degrading tlr3 in murine cells. Cellular & Molecular Immunology, 17:865-874, May 2020. URL: https://doi.org/10.1038/s41423-019-0236-y, doi:10.1038/s41423-019-0236-y. This article has 28 citations and is from a peer-reviewed journal.
(lari2016resolutionofproteotoxic pages 111-115): F Lari. Resolution of proteotoxic stress in the endoplasmic reticulum by ubiquitin ligase complexes. Unknown journal, 2016.
(veronese2024erlin12scaffoldsbridge pages 4-6): Matteo Veronese, Sebastian Kallabis, Alexander Tobias Kaczmarek, Anushka Das, Lennart Robers, Simon Schumacher, Alessia Lofrano, Susanne Brodesser, Stefan Müller, Kay Hofmann, Marcus Krüger, and Elena I Rugarli. Erlin1/2 scaffolds bridge tmub1 and rnf170 and restrict cholesterol esterification to regulate the secretory pathway. Life Science Alliance, 7:e202402620, May 2024. URL: https://doi.org/10.26508/lsa.202402620, doi:10.26508/lsa.202402620. This article has 8 citations and is from a peer-reviewed journal.
(veronese2024erlin12scaffoldsbridge pages 10-12): Matteo Veronese, Sebastian Kallabis, Alexander Tobias Kaczmarek, Anushka Das, Lennart Robers, Simon Schumacher, Alessia Lofrano, Susanne Brodesser, Stefan Müller, Kay Hofmann, Marcus Krüger, and Elena I Rugarli. Erlin1/2 scaffolds bridge tmub1 and rnf170 and restrict cholesterol esterification to regulate the secretory pathway. Life Science Alliance, 7:e202402620, May 2024. URL: https://doi.org/10.26508/lsa.202402620, doi:10.26508/lsa.202402620. This article has 8 citations and is from a peer-reviewed journal.
(wang2024hostfactorsmodulate pages 13-14): Jingjing Wang, Yirui Dong, Xuewei Zheng, Haodi Ma, Mengjiao Huang, Dongliao Fu, Jiangbo Liu, and Qinan Yin. Host factors modulate virus-induced ifn production via pattern recognition receptors. Journal of Inflammation Research, 17:3737-3752, Jun 2024. URL: https://doi.org/10.2147/jir.s455035, doi:10.2147/jir.s455035. This article has 6 citations and is from a peer-reviewed journal.
(li2024thernabindingproteins pages 12-13): Jianguo Li, Jingge Yu, Ao Shen, Suwen Lai, Zhiping Liu, and Tian-Sheng He. The rna-binding proteins regulate innate antiviral immune signaling by modulating pattern recognition receptors. Virology Journal, Sep 2024. URL: https://doi.org/10.1186/s12985-024-02503-x, doi:10.1186/s12985-024-02503-x. This article has 13 citations and is from a peer-reviewed journal.
(OpenTargets Search: hereditary spastic paraplegia,spastic paraplegia,sensory ataxia,spinocerebellar ataxia,neuroaxonal dystrophy-RNF170): Open Targets Query (hereditary spastic paraplegia,spastic paraplegia,sensory ataxia,spinocerebellar ataxia,neuroaxonal dystrophy-RNF170, 2 results). Buniello, A. et al. (2025). Open Targets Platform: facilitating therapeutic hypotheses building in drug discovery. Nucleic Acids Research.
(vondel2024overarchingpathomechanismsin pages 5-8): Liedewei Van de Vondel, Jonathan De Winter, Vincent Timmerman, and Jonathan Baets. Overarching pathomechanisms in inherited peripheral neuropathies, spastic paraplegias, and cerebellar ataxias. Mar 2024. URL: https://doi.org/10.1016/j.tins.2024.01.004, doi:10.1016/j.tins.2024.01.004. This article has 11 citations and is from a highest quality peer-reviewed journal.
(cogan2024biallelicvariantsin pages 1-6): Guillaume Cogan, Maha S. Zaki, Mahmoud Issa, Boris Keren, Marine Guillaud-Bataille, Florence Renaldo, Arnaud Isapof, Pauline Lallemant, Giovanni Stevanin, Lena Guillot-Noel, Thomas Courtin, Julien Buratti, Cécile Freihuber, Joseph G. Gleeson, Robyn Howarth, Alexandra Durr, Jean-Madeleine de Sainte Agathe, and Cyril Mignot. Biallelic variants in erlin1: a series of 13 individuals with spastic paraparesis. Human genetics, 143:1353-1362, Oct 2024. URL: https://doi.org/10.1007/s00439-024-02702-0, doi:10.1007/s00439-024-02702-0. This article has 3 citations and is from a peer-reviewed journal.
(cogan2024biallelicvariantsin pages 12-16): Guillaume Cogan, Maha S. Zaki, Mahmoud Issa, Boris Keren, Marine Guillaud-Bataille, Florence Renaldo, Arnaud Isapof, Pauline Lallemant, Giovanni Stevanin, Lena Guillot-Noel, Thomas Courtin, Julien Buratti, Cécile Freihuber, Joseph G. Gleeson, Robyn Howarth, Alexandra Durr, Jean-Madeleine de Sainte Agathe, and Cyril Mignot. Biallelic variants in erlin1: a series of 13 individuals with spastic paraparesis. Human genetics, 143:1353-1362, Oct 2024. URL: https://doi.org/10.1007/s00439-024-02702-0, doi:10.1007/s00439-024-02702-0. This article has 3 citations and is from a peer-reviewed journal.
(song2020e3ubiquitinligase pages 1-2): Xiaoqi Song, Shuo Liu, Wen-die Wang, Zhong-fei Ma, Xuetao Cao, and Minghong Jiang. E3 ubiquitin ligase rnf170 inhibits innate immune responses by targeting and degrading tlr3 in murine cells. Cellular & Molecular Immunology, 17:865-874, May 2020. URL: https://doi.org/10.1038/s41423-019-0236-y, doi:10.1038/s41423-019-0236-y. This article has 28 citations and is from a peer-reviewed journal.
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