Anti-Elav-type RNA-binding protein ETR3 antibody [EPR13374] - BSA and Azide free

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

Elav-type RNA-binding protein ETR3 also known as CELF1 (CUGBP Elav-like family member 1) is involved in the regulation of pre-mRNA alternative splicing translation and stability. The protein has a mass of approximately 52 kDa. ETR3 is expressed in several tissues with higher levels found in the heart skeletal muscles and brain. These tissues are indicative of its important role in post-transcriptional mechanism. As a member of the ELAV (embryonic lethal abnormal vision)-like proteins ETR3 contains three RNA recognition motifs which mediate its binding to RNA.

Biological function summary

ETR3 influences various cellular processes by participating in RNA processing and nuclear-cytoplasmic transport. It forms part of ribonucleoprotein complexes that interact with target RNA impacting splicing decisions and gene expression levels. ETR3's activity is important for muscle and neuronal function helping modulate the expression of genes vital for muscle contraction and neuronal communication. Through its role as an RNA-binding regulator it can affect cell differentiation and growth.

Pathways

ETR3 plays significant roles in the regulation of alternative splicing and mRNA decay pathways. It interacts with several other splicing and mRNA degradation factors such as hnRNPH (heterogeneous nuclear ribonucleoprotein H) and PABPN1 (poly(A) binding protein nuclear 1). These interactions help control the turnover and translation of mRNA establishing a balance of protein synthesis important for maintaining cellular homeostasis. By influencing these pathways ETR3 impacts cardiac and neural-specific gene expression demonstrating its role in tissue-specific regulation.

Associated diseases and disorders

ETR3 is linked to myotonic dystrophy and cardiac arrhythmias. ETR3 misregulation leads to disruptions in alternative splicing of specific mRNAs contributing to the pathophysiology of these conditions. The relationship between ETR3 and proteins such as MBNL1 (Muscleblind-like splicing regulator 1) in myotonic dystrophy is particularly significant. Both proteins regulate alternative splicing and their misregulated expression in disease highlights an important area for potential therapeutic interventions. The association of ETR3 with such disorders highlights its relevance in maintaining normal cellular and physiological functions.