EPS15

Last update 08 May 2025

Basic Info

Synonyms

AF-1P, AF1P, epidermal growth factor receptor pathway substrate 15

+ [5]

Introduction

Involved in cell growth regulation. May be involved in the regulation of mitogenic signals and control of cell proliferation. Involved in the internalization of ligand-inducible receptors of the receptor tyrosine kinase (RTK) type, in particular EGFR. Plays a role in the assembly of clathrin-coated pits (CCPs). Acts as a clathrin adapter required for post-Golgi trafficking. Seems to be involved in CCPs maturation including invagination or budding. Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR); internalization of ITGB1 as DAB2-dependent cargo but not TFR seems to require association with DAB2.

100 Clinical Results associated with EPS15

100 Translational Medicine associated with EPS15

0 Patents (Medical) associated with EPS15

417

Literatures (Medical) associated with EPS15

01 Dec 2025·Molecular Genetics and Genomics

Genetic insights into CRP levels in Indian adolescents: confirming adult genetic associations

Article

Author: Nair, Janaki M ; Giri, Anil K ; Chakraborty, Shraddha ; Marwaha, Raman K ; Bandesh, Khushdeep ; Bharadwaj, Dwaipayan ; Tandon, Nikhil ; Basu, Analabha

CRP is a biomarker of acute inflammation linked to metabolic complications. Given the rising prevalence of these conditions in India, we investigated the genetic basis of CRP levels in Indian adolescents, an underrepresented group in genetic studies, to identify early markers of metabolic risk. We performed a two-phased genome-wide association study (GWAS; N = 5052) and an independent Exome-wide association study (ExWAS; N = 4547), to identify both common and rare genetic variants associated with CRP levels. The study identified intergenic variants near CRP and CRPP1 genes, and APOC1 gene as the key regulators of CRP levels establishing the universality of these associations. The GWAS identified the variant rs4247360 (PITPNC1) to be associated at a suggestive significance. The ExWAS single variant association identified novel associations in genes FGL1 (rs35431851), C19orf45 (rs608144, rs475923, rs484870), TRAPPC12 (rs11686212) and KIAA0087 (rs17153822). The SKATO analysis of the rare variants highlighted the role of loss of function and missense variants in genes EPS15, CCDC15, ZNF286A, ELF1, B3GNT8, ZNF850, MAP2, and PSG2. The GWAS and ExWAS in the present study validated the association of 56 variants previously reported for CRP levels. The meta-analysis with the CRP GWAS earlier reported in Indian adults revealed the shared genetic architecture of CRP levels across age groups. The gene-set enrichment analysis highlighted the role of CRP-associated genes in inflammatory and cardiometabolic pathways. The study enhances understanding of genetic predispositions to inflammation and metabolic disorders confirming known associations, identifying novel loci, and validating shared genetic architecture across age-groups, guiding targeted prevention for at-risk youth.

01 Apr 2025·Structure

Laminar organization of molecular complexes in a clathrin coat revealed by nanoscale protein colocalization

Article

Author: Ogawa, Shuichiro ; Kobayashi, Ryouhei ; Elverston, Louis L H ; Vavylonis, Dimitrios ; Kiuchi, Tai ; Watanabe, Naoki

Super-resolution microscopy achieves a few nanometers resolution, but colocalization analysis in a molecular complex is limited by its labeling density. Here we present a method for quantitative mapping of molecular complexes using multiplexed super-resolution imaging, integrating exchangeable single-molecule localization (IRIS). We developed antiserum-derived Fab IRIS probes for high-density labeling of endogenous proteins and protein cluster coloring (PC-coloring), which employs pixel-based principal component analysis and clustering. PC-coloring maps regions of distinct ratios of multiple proteins, and in each region, correlation between two proteins is calculated for evaluating the complex formation. PC-coloring revealed multi-layered complex formation in a clathrin-coated structure (CCS) prior to endocytosis. Upon epidermal growth factor (EGF) stimulation, EGF receptor (EGFR)-dominant, EGFR-Grb2-complex, and Grb2-dominant regions lined up from outside the CCS rim. Along the interior of Grb2-dominant regions, CCS components (Eps15, FCHo1/2 and intersectin-1) formed a complex with Grb2 away from EGFR. The Grb2-dominant region and Grb2-CCS component complex formation probably determine EGFR recruitment sites in the CCS rim.

25 Feb 2025·Journal of Virology

RNASEK interacting with PEDV structural proteins facilitates virus entry via clathrin-mediated endocytosis

Article

Author: Kong, Ning ; Yu, Hai ; Wang, Yahe ; Tong, Wu ; Zhang, Wen ; Liu, Yuchang ; Zheng, Hao ; Cao, Xinyu ; Xie, Shengsong ; Liu, Hailong ; Qin, Wenzhen ; Yang, Xinyu ; Wang, Jiarui ; Shan, Tongling ; Tong, Guangzhi ; Sun, He

ABSTRACTPorcine epidemic diarrhea virus (PEDV), as a type of Alphacoronavirus causing acute diarrhea and high death rate among sucking piglets, poses great financial damage to the swine industry. Nevertheless, the molecular mechanism whereby PEDV enters host cells is unclear, limiting the development of PED vaccines and anti-PEDV agents. The present study found that the host protein ribonuclease kappa (RNASEK) was regulated by USF2, a transcription factor, and facilitated the PEDV replication. RNASEK was identified as a novel binding partner of PEDV, which interacted with a spike (S), envelope (E), and membrane (M) proteins on PEDV virion surfaces to increase the uptake not for attachment of PEDV virions. PEDV enters cells through the endocytosis pathways. RNASEK knockdown or RNASEK knockout assay revealed that through clathrin-mediated endocytosis (CME), RNASEK promoted the internalization of PEDV virions. Clathrin and the adaptor protein EPS15 only interacted with PEDV E protein, demonstrating that the RNASEK could target more virions through interaction with PEDV S, E, and M proteins to clathrin and EPS15 proteins rather than merely interacting with PEDV E protein to mediate the PEDV entry through CME. Moreover, our findings suggest that RNASEK, a newly identified host-entry factor, facilitates PEDV internalization by increasing the interaction of PEDV virions and EPS15-clathrin complex and may also provide a potential target for anti-PEDV therapies.IMPORTANCEPEDV is the causative pathogen of porcine diarrhea, which is a highly infectious acute intestinal condition, that poses significant economic damage to the swine industry. However, the existing PED vaccines fail to provide adequate protection for piglets against PEDV infection. Although PEDV replication in cells has been widely described, the mechanisms beneath PEDV entry of the host cells are incompletely understood. In this study, we showed that RNASEK, regulated by the transcription factor USF2, is a new host factor increasing PEDV infection in LLC-PK1 cells. RNASEK can bind to multiple structural proteins of PEDV (S, E, and M proteins), therefore increasing the interaction between PEDV virions, clathrin, and EPS15 to promote PEDV virion entry. Apart from unraveling the entry mechanisms of PEDV, our findings also contributed to facilitating the development of anti-PEDV agents and PED vaccines.

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EPS15

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