Target intelligence / Profile preview

E3 ubiquitin-protein ligase NRDP1 (RNF41)

Target
RNF41
Molecular classification
Enzyme, E3 ubiquitin ligase, RING finger domain-containing protein
01

Overview

E3 ubiquitin-protein ligase NRDP1 (RNF41) is an enzyme that catalyzes the transfer of ubiquitin to specific target proteins, marking them for proteasomal or lysosomal degradation[1][3][4]. It contains a RING finger domain that mediates protein-protein interactions necessary for ubiquitin transfer[1][5]. RNF41 regulates the stability and turnover of several cytokine and growth factor receptors, including erythropoietin receptor, interleukin-3 receptor, and ErbB3[2][3]. It negatively modulates pro-inflammatory signaling (such as MyD88-dependent cytokine production) and plays roles in apoptosis and autophagy/mitophagy by targeting specific signaling molecules for ubiquitination and degradation[3][4][5]. Dysregulation or mutation of RNF41 is implicated in the pathogenesis of cancer, neurodegenerative, autoimmune, and infectious diseases[4][5]. RNF41 interacts with various cellular proteins, including USP8, BRUCE, Parkin (PRKN), VPS52, and participates in dynamic subcellular protein sorting[2].

Other names
Ring finger protein 41NRDP1FLRFSBBI03fetal liver ring fingerneuregulin receptor degradation protein-1E3 ubiquitin protein ligaseRING-type E3 ubiquitin transferase NRDP1
02

Mechanism of action

Ubiquitination-dependent degradation (mainly K48-linked polyubiquitination), Negative regulation of receptor signaling via polyubiquitination and subsequent proteasomal or lysosomal degradation

03

Biological functions

UbiquitinationProtein degradationRegulation of cytokine and growth factor receptor signaling (e.g., JAK2-associated cytokine receptors, ErbB3)Control of cell death (apoptosis)Regulation of immune signalingControl of autophagy/mitophagyIntracellular protein sorting
04

Disease associations

CancerNeurodegenerative diseaseAutoimmune diseaseInfection
05

Safety considerations

Potential for off-target effects due to involvement in essential protein degradation pathways and broad regulatory roles in signaling, immune response, and cell death

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