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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Ring finger protein 146

RNF146
Top mentioned proteins: Ubiquitin, tankyrase, CAN, Axin, FGFR2
Papers on RNF146
Tankyrase Inhibitors Target YAP by Stabilizing Angiomotin Family Proteins.
New
Chen et al., Houston, United States. In Cell Rep, Nov 2015
Tankyrases associate with AMOT family proteins and promote their degradation through E3 ligase RNF146.
Poly-ADP ribosylation of PTEN by tankyrases promotes PTEN degradation and tumor growth.
New
Chen et al., Houston, United States. In Genes Dev, Feb 2015
We showed that tankyrases interact with and ribosylate PTEN, which promotes the recognition of PTEN by a PAR-binding E3 ubiquitin ligase, RNF146, leading to PTEN ubiquitination and degradation.
Allosteric activation of the RNF146 ubiquitin ligase by a poly(ADP-ribosyl)ation signal.
New
Impact
Xu et al., Seattle, United States. In Nature, Feb 2015
The RING-type E3 ubiquitin ligase RNF146 (also known as Iduna) is responsible for PARylation-dependent ubiquitination (PARdU).
KIT Mutation and Loss of 14q May Be Sufficient for the Development of Clinically Symptomatic Very Low-Risk GIST.
Delecluse et al., Heidelberg, Germany. In Plos One, 2014
Besides these genetic lesions, only two point mutations that may affect tumour progression were identified: A frame-shift deletion in RNF146 and a missense mutation in a zinc finger of ZNF407.
Tankyrases: structure, function and therapeutic implications in cancer.
Review
Lehtio et al., Oslo, Norway. In Curr Pharm Des, 2013
Modified proteins are subsequently recognized by the E3 ubiquitin ligase RNF146, poly-ubiquitinated and predominantly guided to 26S proteasomal degradation.
Modulation of poly(ADP-ribose) polymerase-1 (PARP-1)-mediated oxidative cell injury by ring finger protein 146 (RNF146) in cardiac myocytes.
Szabo et al., Galveston, United States. In Mol Med, 2013
By using cultured rat cardiomyocytes, here we report that ring finger protein 146 (RNF146), a cytoplasmic E3-ubiquitin ligase, acts as a direct interactor of PARP-1.
Overexpression of RNF146 in non-small cell lung cancer enhances proliferation and invasion of tumors through the Wnt/β-catenin signaling pathway.
Wang et al., Shenyang, China. In Plos One, 2013
Studies have suggested a possible correlation between the newly identified E3 ubiquitin ligase ring finger protein 146 (RNF146) and tumor development.
Structural insight into the interaction of ADP-ribose with the PARP WWE domains.
Muto et al., Yokohama, Japan. In Febs Lett, 2012
Structural information about WWE domains has been obtained for the ubiquitination-related proteins, such as Deltex and RNF146, but not yet for the poly-ADP-ribose polymerases (PARPs).
Recognition of the iso-ADP-ribose moiety in poly(ADP-ribose) by WWE domains suggests a general mechanism for poly(ADP-ribosyl)ation-dependent ubiquitination.
GeneRIF
Xu et al., Seattle, United States. In Genes Dev, 2012
the RNF146 WWE domain recognizes poly(ADP-ribose) (PAR) by interacting with iso-ADP-ribose (iso-ADPR), the smallest internal PAR structural unit containing the characteristic ribose-ribose glycosidic bond formed during poly(ADP-ribosyl)ation.
Loss of Tankyrase-mediated destruction of 3BP2 is the underlying pathogenic mechanism of cherubism.
Impact
Rottapel et al., Toronto, Canada. In Cell, 2012
Here we show that Tankyrase, a member of the poly(ADP-ribose)polymerase (PARP) family, regulates 3BP2 stability through ADP-ribosylation and subsequent ubiquitylation by the E3-ubiquitin ligase RNF146 in osteoclasts.
Ring finger protein 146/Iduna is a poly(ADP-ribose) polymer binding and PARsylation dependent E3 ubiquitin ligase.
Review
GeneRIF
Tan et al., Singapore, Singapore. In Cell Adh Migr, 2011
RNF146/Iduna has been found to be implicated in neurodegenerative disease and cancer development. [Review]
Iduna is a poly(ADP-ribose) (PAR)-dependent E3 ubiquitin ligase that regulates DNA damage.
GeneRIF
Dawson et al., Baltimore, United States. In Proc Natl Acad Sci U S A, 2011
Iduna is a Poly(ADP-ribose)-dependent ubiquitin E3 ligase.
Interactions between genetic variants and breast cancer risk factors in the breast and prostate cancer cohort consortium.
Canzian et al., Heidelberg, Germany. In J Natl Cancer Inst, 2011
We genotyped 17 germline SNPs (FGFR2-rs2981582, FGFR2-rs3750817, TNRC9-rs3803662, 2q35-rs13387042, MAP3K1-rs889312, 8q24-rs13281615, CASP8-rs1045485, LSP1-rs3817198, COL1A1-rs2075555, COX11-rs6504950, RNF146-rs2180341, 6q25-rs2046210, SLC4A7-rs4973768, NOTCH2-rs11249433, 5p12-rs4415084, 5p12-rs10941679, RAD51L1-rs999737), and odds ratios were estimated by logistic regression to confirm previously reported associations with breast cancer risk.
Genetic polymorphisms and breast cancer risk: evidence from meta-analyses, pooled analyses, and genome-wide association studies.
Review
Lai et al., China. In Breast Cancer Res Treat, 2011
Of the 25 SNPs, 20 were noteworthy: C6orf97 (rs2046210 and rs3757318), FGFR2 (rs2981579, rs1219648, and rs2981582), LSP1 (rs909116), RNF146 (rs2180341), SLC4A7 (rs4973768), MRPS30 (rs7716600), TOX3 (rs3803662 and rs4784227), ZNF365 (rs10995190), rs889312, rs614367, rs13281615, rs13387042, rs11249433, rs1011970, rs614367, and rs1562430.
RNF146 is a poly(ADP-ribose)-directed E3 ligase that regulates axin degradation and Wnt signalling.
Impact
Cong et al., Cambridge, United States. In Nat Cell Biol, 2011
Here, we identify RNF146, a RING-domain E3 ubiquitin ligase, as a positive regulator of Wnt signalling.
Ubiquitin ligase RNF146 regulates tankyrase and Axin to promote Wnt signaling.
GeneRIF
Costa et al., San Francisco, United States. In Plos One, 2010
RNF146 RING-type ubiquitin E3 ligase as a positive regulator of Wnt signaling that operates with tankyrase to maintain low steady-state levels of Axin proteins
The RNF146 and ECHDC1 genes as candidates for inherited breast and ovarian cancer in Jewish Ashkenazi women.
GeneRIF
Friedman et al., Israel. In Fam Cancer, 2008
Mutations in the coding regions of the RNF146 and ECHDC1 genes do not contribute to the burden of inherited predisposition of breast cancer in Ashkenazi high risk women.
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