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Ring finger protein 11

RNF11, RING finger protein 11
The protein encoded by this gene contains a RING-H2 finger motif, which is known to be important for protein-protein interactions. The expression of this gene has been shown to be induced by mutant RET proteins (MEN2A/MEN2B). The germline mutations in RET gene are known to be responsible for the development of multiple endocrine neoplasia (MEN). [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Ubiquitin, A20, Itch, CAN, EGFR
Papers on RNF11
RNF11 is a GGA protein cargo and acts as a molecular adaptor for GGA3 ubiquitination mediated by Itch.
Castagnoli et al., Roma, Italy. In Oncogene, Jun 2015
Ring finger protein 11 (RNF11) is a RING (really interesting new gene)-H2 E3 ligase that is overexpressed in several human tumor tissues.
Elucidating dynamic protein-protein interactions and ubiquitination in NF-κB signaling pathways.
Harhaj et al., Miami, United States. In Methods Mol Biol, 2014
A20 inducibly interacts with the adaptor molecule TAX1BP1 and the E3 ligases Itch and RNF11 to form an A20 ubiquitin-editing enzyme complex.
Identification of a novel role of RING finger protein 11 promoting the metastasis of murine melanoma cells.
Feng et al., Xinxiang, China. In Am J Transl Res, 2014
Here, wedemonstrate that RING finger protein 11 (RNF11) disruption by insertional mutagenesis impairs the metastatic potential of murine melanoma B16F10 cells.
RING finger proteins are involved in the progression of barrett esophagus to esophageal adenocarcinoma: a preliminary study.
Fang et al., Chongqing, China. In Gut Liver, 2014
Among these proteins, the RNF32 and RNF121 expression in BE was 20.3-fold and 16.4-fold higher, respectively, than that in NE, and the expression of RNF24, RNF130, RNF141, RNF139, RNF11, RNF14, and RNF159 was upregulated more than 2-fold compared with NE.
Protein microarray characterization of the S-nitrosoproteome.
Dawson et al., In Mol Cell Proteomics, 2014
We identify eight ubiquitin E3 ligases, RNF10, RNF11, RNF41, RNF141, RNF181, RNF208, WWP2, and UBE3A, whose activities are modulated by S-nitrosylation, providing a unique regulatory mechanism of the ubiquitin proteasome system.
Association mapping of the PARK10 region for Parkinson's disease susceptibility genes.
Zabetian et al., Seattle, United States. In Parkinsonism Relat Disord, 2014
BACKGROUND: Previous studies indicate that as many as six genes within the PARK10 region (RNF11, UQCRH, HIVEP3, EIF2B3, USP24, ELAVL4) might modify susceptibility or age at onset in Parkinson's disease (PD).
SARA and RNF11 at the crossroads of EGFR signaling and trafficking.
Murphy et al., Ioánnina, Greece. In Methods Enzymol, 2013
Recently, SARA has been shown to interact with the E3 ubiquitin ligase RNF11 (RING finger protein 11) and members of the ESCRT-0 (endosomal sorting complex required for transport) complex functionally participating in the degradation of EGFR.
NF-κB activity is inversely correlated to RNF11 expression in Parkinson's disease.
Betarbet et al., Atlanta, United States. In Neurosci Lett, 2013
RING finger protein 11 (RNF11), a negative regulator of NF-κB signaling pathway, colocalizes with α-synuclein and is sequestered in Lewy bodies in Parkinson's disease (PD).
Genetic myostatin decrease in the golden retriever muscular dystrophy model does not significantly affect the ubiquitin proteasome system despite enhancing the severity of disease.
Willis et al., Columbus, United States. In Am J Transl Res, 2012
To examine the role of the ubiquitin proteasome and calpain systems in this accelerated decline, we determined the expression of the muscle ubiquitin ligases MuRF1, Atrogin-1, RNF25, RNF11, and CHIP: the proteasome subunits PSMA6, PSMB4, and PSME1: and calpain 1/2 by real time PCR in the cranial sartorius and vastus lateralis muscles in control, affected GRMD, and GRippet dogs.
WWP1: a versatile ubiquitin E3 ligase in signaling and diseases.
Chen et al., Kunming, China. In Cell Mol Life Sci, 2012
WWP1 has been suggested to function as the E3 ligase for several PY motif-containing proteins, such as Smad2, KLF5, p63, ErbB4/HER4, RUNX2, JunB, RNF11, SPG20, and Gag, as well as several non-PY motif containing proteins, such as TβR1, Smad4, KLF2, and EPS15.
The kinase IKKα inhibits activation of the transcription factor NF-κB by phosphorylating the regulatory molecule TAX1BP1.
Harhaj et al., Miami, United States. In Nat Immunol, 2011
In response to stimulation with proinflammatory cytokines, the deubiquitinase A20 inducibly interacts with the regulatory molecules TAX1BP1, Itch and RNF11 to form the A20 ubiquitin-editing complex.
Inflammation-induced airway smooth muscle responsiveness is strain dependent in mice.
Adner et al., Stockholm, Sweden. In Pulm Pharmacol Ther, 2011
In addition, gene expression of TLR1-TLR9, pivotal inflammatory signal transduction proteins (jun-kinase, p38 and p65) and critical negative regulators of inflammation (A20, Itch, Tax1bp1 and RNF11) were studied in tracheal smooth muscle strips, fresh and following treatment for 4 days with LPS, from both strains.
Expression, biological activities and mechanisms of action of A20 (TNFAIP3).
Beyaert et al., Gent, Belgium. In Biochem Pharmacol, 2011
Induction of K48-polyubiquitination by A20 involves its C-terminal zinc-finger ubiquitin-binding domain, which may promote interaction with E3 ligases, such as Itch and RNF11 that are involved in mediating A20 inhibitory functions.
Multiple modification and protein interaction signals drive the Ring finger protein 11 (RNF11) E3 ligase to the endosomal compartment.
Castagnoli et al., Roma, Italy. In Oncogene, 2010
Data show that membrane anchoring through acylation is necessary for RNF11 to be post-translationally modified by the addition of several ubiquitin moieties.
The ubiquitin-editing enzyme A20 requires RNF11 to downregulate NF-kappaB signalling.
Harhaj et al., Miami, United States. In Embo J, 2009
RNF11, together with TAX1BP1 and Itch, is an essential component of an A20 ubiquitin-editing protein complex that ensures transient activation of inflammatory signalling pathways.
Analysis of electrostatic contributions to the selectivity of interactions between RING-finger domains and ubiquitin-conjugating enzymes.
Thomson et al., Barcelona, Spain. In Proteins, 2009
Analysis reveals that the main determinants of selectivity between ubiquitin ligases RNF11 and E2 ubiquitin-conjugating enzymes resides on ring domains, rather than on the E2s.
The WW domain containing E3 ubiquitin protein ligase 1 upregulates ErbB2 and EGFR through RING finger protein 11.
Seth et al., Albany, United States. In Oncogene, 2008
WWP1 may promote cell proliferation and survival partially through suppressing RNF11-mediated ErbB2 and EGFR downregulation in human cancer cells.
PARK10 candidate RNF11 is expressed by vulnerable neurons and localizes to Lewy bodies in Parkinson disease brain.
Levey et al., Atlanta, United States. In J Neuropathol Exp Neurol, 2007
these findings identify RNF11 as a strong candidate gene at the PARK10 locus and highlight its potential significance in the development of the common form of Parkinson disease
Novel RING E3 ubiquitin ligases in breast cancer.
Seth et al., Toronto, Canada. In Neoplasia, 2006
RNF11 is a small RING E3 ligase that affects transforming growth factorbeta and EGF-R signaling and is overexpressed in invasive breast cancers
RNF11 is a multifunctional modulator of growth factor receptor signalling and transcriptional regulation.
Seth et al., Toronto, Canada. In Eur J Cancer, 2005
Our laboratory has found that the 154aa RING finger protein 11 (RNF11), has modular domains and motifs including a RING-H2 finger domain, a PY motif, an ubiquitin interacting motif (UIM), a 14-3-3 binding sequence and an AKT phosphorylation site.
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