Leucine-rich repeat-containing protein 41 (LRRC41)

Leucine-rich repeat-containing protein 41 (LRRC41, also known as MUF1) is a member of the leucine-rich repeat (LRR) protein family whose structure provides a scaffold for protein-protein interactions[1][5]. It serves as a substrate recognition component of ECS-type E3 ubiquitin ligases (specifically Elongin BC–CUL2/5–SOCS-box complexes), thereby contributing to targeted protein degradation via the ubiquitin-proteasome pathway[1][3]. It is predominantly a nuclear protein capable of dimerization and interaction with RhoBTB proteins, which are implicated as tumor suppressors through the formation of cullin 3 (Cul3)-dependent ubiquitin ligase complexes[3]. LRRC41's primary function is not as an enzyme or receptor but rather as a substrate adapter or scaffolding protein for ubiquitin ligase complexes. Its biological role is linked to protein turnover, protein-protein interaction scaffolding, intracellular degradation, and possibly components of signaling pathways, although direct involvement in canonical receptor or enzyme-mediated signaling is not established[3][1][5]. There is no evidence that LRRC41 currently serves as a clinical drug target, nor is it used as a biomarker for patient selection or therapy monitoring. However, its molecular activity connects it to cancer pathways through the regulation of protein degradation and interactions with tumor suppressor complexes[3].

Other names

MUF1leucine-rich repeat-containing 41LRRC41