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Epidermal growth factor receptor pathway substrate 15

This gene encodes a protein that is part of the EGFR pathway. The protein is present at clatherin-coated pits and is involved in receptor-mediated endocytosis of EGF. Notably, this gene is rearranged with the HRX/ALL/MLL gene in acute myelogeneous leukemias. Alternative splicing results in multiple transcript variants encoding distinct isoforms. [provided by RefSeq, May 2009] (from NCBI)
Top mentioned proteins: p15, V1a, Transferrin, Ubiquitin, Epidermal Growth Factor
Papers using Eps15 antibodies
Hrs regulates early endosome fusion by inhibiting formation of an endosomal SNARE complex
Bean Andrew J. et al., In The Journal of Cell Biology, 1998
... Antibodies were obtained from the following sources: EEA1 and Eps15 (Santa Cruz Biotechnology, Inc.), SV2 (a gift ...
Papers on Eps15
The HIV Rev-Binding protein (HRB) is a co-factor for HIV-1 Nef-mediated CD4 down-regulation.
Verhasselt et al., In J Gen Virol, Jan 2016
Interestingly, the knock-down of the related protein HRBL (HRB Like), but not of the HRB interaction partner EPS15 (Epidermal Growth Factor Receptor Pathway Substrate 15), increased CD4 levels in Vpu-expressing cells significantly.
Over-expression of EPS15 is a favorable prognostic factor in breast cancer.
Zhang et al., Wuxi, China. In Mol Biosyst, Nov 2015
As a crucial player in terminating growth factor signaling, EPS15 plays important roles in many malignancies including breast cancer.
Polymorphisms in Genes Involved in EGFR Turnover Are Predictive for Cetuximab Efficacy in Colorectal Cancer.
Lenz et al., München, Germany. In Mol Cancer Ther, Oct 2015
The following SNPs involved in EGFR degradation were analyzed in a screening cohort of 108 patients treated with cetuximab in the chemorefractory setting: c-CBL (rs7105971; rs4938637; rs4938638; rs251837), EPS15 (rs17567; rs7308; rs1065754), NAE1 (rs363169; rs363170; rs363172), SH3KBP1 (rs7051590; rs5955820; rs1017874; rs11795873), SGIP1 (rs604737; rs6570808; rs7526812), UBE2M (rs895364; rs895374), and UBE2L3 (rs5754216).
The deubiquitinating enzyme USP46 regulates AMPA receptor ubiquitination and trafficking.
Man et al., Boston, United States. In J Neurochem, Sep 2015
Our previous work demonstrated that AMPARs are subject to ubiquitination by the E3 ligase Nedd4, resulting in EPS15-mediated receptor internalization and Ubiquitin (Ub)-proteasome pathway (UPP)-dependent degradation.
Evidence-based RT-PCR methods for the detection of the 8 most common MLL aberrations in acute leukemias.
Marschalek et al., Berlin, Germany. In Leuk Res, Feb 2015
Based on the large data collection of MLL genomic breakpoints in acute leukemias comprising more than 1.600 cases at the Diagnostic Center for Acute Leukemias (DCAL) in Frankfurt, Germany that provide an overview over the experimentally observed fusion transcript variants, we developed RT-PCR methods for the reliable detection of the 8 most common MLL aberrations (MLL-AF4, MLL-AF6, MLL-AF9, MLL-AF10, MLL-ENL, MLL-ELL, MLL-EPS15, MLL PTD), together accounting for around 90% of MLL-r cases.
Genome-wide shRNA screening identifies host factors involved in early endocytic events for HIV-1-induced CD4 down-regulation.
Verhasselt et al., Gent, Belgium. In Retrovirology, 2013
By this stringent validation set-up, we could demonstrate that the knock-down of DNM3 (dynamin 3), SNX22 (sorting nexin 22), ATP6AP1 (ATPase, H+ Transporting, Lysosomal Accessory Protein 1), HRBL (HIV-Rev binding protein Like), IDH3G (Isocitrate dehydrogenase), HSP90B1 (Heat shock protein 90 kDa beta member 1) and EPS15 (Epidermal Growth Factor Receptor Pathway Substrate 15) significantly increases CD4 levels in HIV-infected SupT1 T cells compared to the non-targeting shRNA control.
Identification and selected reaction monitoring (SRM) quantification of endocytosis factors associated with Numb.
McGlade et al., Toronto, Canada. In Mol Cell Proteomics, 2013
In vitro binding measurements indicated exon 9-independent Numb interaction with REPS1 and Eps15 EH domains.
Mosquito cellular factors and functions in mediating the infectious entry of chikungunya virus.
Chu et al., Singapore, Singapore. In Plos Negl Trop Dis, 2012
Several genes such as epsin I (EPN1), epidermal growth factor receptor pathway substrate 15 (EPS15) and Huntingtin interacting protein I (HIP1) were identified to be differentially expressed during CHIKV infection and known to be involved in clathrin-mediated endocytosis (CME).
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.
Recycling of the epidermal growth factor receptor is mediated by a novel form of the clathrin adaptor protein Eps15.
McNiven et al., Rochester, United States. In J Biol Chem, 2011
distinct forms of Eps15 direct EGFR to either the late endosome/lysosome for degradation (Eps15) or to the recycling endosome for transit back to the cell surface (Eps15S)
Characterization of the EFC/F-BAR domain protein, FCHO2.
Nakanishi et al., Kumamoto, Japan. In Genes Cells, 2011
FCHO2 regulates clathrin-mediated endocytosis through its interactions with membranes and Eps15.
FCHo proteins are nucleators of clathrin-mediated endocytosis.
McMahon et al., Cambridge, United Kingdom. In Science, 2010
FCHo1/2 proteins bound specifically to the plasma membrane and recruited the scaffold proteins eps15 and intersectin, which in turn engaged the adaptor complex AP2.
Mechanism for the selective interaction of C-terminal Eps15 homology domain proteins with specific Asn-Pro-Phe-containing partners.
Sorgen et al., Omaha, United States. In J Biol Chem, 2010
analysis of the selective interaction of C-terminal Eps15 homology domain proteins with specific Asn-Pro-Phe-containing partners
Differential interaction of the E3 ligase parkin with the proteasomal subunit S5a and the endocytic protein Eps15.
Shaw et al., London, Canada. In J Biol Chem, 2010
parkin Ubld uses differential surfaces to recruit UIM regions from the S5a proteasomal subunit compared with Eps15 involved in cell signaling.
Eps15 interacts with ubiquitinated Cx43 and mediates its internalization.
Pereira et al., Coimbra, Portugal. In Exp Cell Res, 2010
Nedd4-mediated ubiquitination of Cx43 is required to recruit Eps15, through its ubiquitin-interacting motif, and targets ubiquitinated Cx43 to the endocytic pathway.
Phocein: A potential actor in vesicular trafficking at Purkinje cell dendritic spines.
Castets et al., Strasbourg, France. In Cerebellum, 2006
Due to its association with dynamin via direct interactions with nucleotide diphosphate kinase (NDPK) and EPS15, phocein has been implicated in vesicular trafficking, acting in particular in the endocytic process.
Molecular mechanisms of coupled monoubiquitination.
Polo et al., Milano, Italy. In Nat Cell Biol, 2006
Using a UIM-containing protein, eps15, as a model, we show here that coupled monoubiquitination strictly depends on the ability of the UIM to bind to monoubiquitin (mUb).
Listeria hijacks the clathrin-dependent endocytic machinery to invade mammalian cells.
Cossart et al., Paris, France. In Nat Cell Biol, 2005
Furthermore, RNA interference-mediated knock-down of major components of the endocytic machinery (for example, clathrin, dynamin, eps15, Grb2, CIN85, CD2AP, cortactin and Hrs), inhibit bacterial entry, establishing that the endocytic machinery is key to the bacterial internalization process.
A single motif responsible for ubiquitin recognition and monoubiquitination in endocytic proteins.
Di Fiore et al., Milano, Italy. In Nature, 2002
a short amino-acid stretch at the carboxy-termini of the monoubiquitinated endocytic proteins Eps15 and eps15R is indispensable for their monoubiquitination
Epidermal growth factor pathway substrate 15, Eps15.
Di Fiore et al., Milano, Italy. In Int J Biochem Cell Biol, 1999
Eps15 was originally identified as a substrate for the kinase activity of the epidermal growth factor receptor (EGFR).
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