KLHL4 overexpression 293T lysate (whole cell)

Supplementary info

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

Activity summary

KLHL4 known also as Kelch-like protein 4 plays an important role in cellular processes. It weighs around 67 kDa and is part of the BTB-Kelch protein family known for its involvement in proteasomal degradation pathways. KLHL4 contains broad complex-tramtrack-bric-a-brac (BTB) domains and Kelch repeats which assist in protein-protein interactions. It is mainly expressed in the testes though its presence has also been detected in other tissues at varying levels such as in the kidney.

Biological function summary

KLHL4 functions in the ubiquitination and subsequent proteasomal degradation of target proteins. It forms part of an E3 ubiquitin ligase complex working with other proteins like CUL3 (Cullin 3) to facilitate this process. By tagging proteins with ubiquitin KLHL4 aids in maintaining cellular protein homeostasis. These interactions contribute to a regulatory role where KLHL4 controls stability and turnover of proteins influencing signal transduction pathways and cellular responses.

Pathways

Cellular protein degradation and signal transduction pathways present important roles for KLHL4. It participates in the ubiquitin-proteasome system (UPS) a pathway critical for protein quality control and cell cycle regulation. KLHL4 interacts with proteins like RBX1 (Ring-box 1) within this pathway to mediate the degradation of various substrates therefore influencing cell cycle progression and signaling cascades. Its ability to regulate protein stability links it to the overall control of metabolic and signaling pathways.

Associated diseases and disorders

Mutations or dysregulations in KLHL4 can connect to reproductive disorders and certain cancers. In particular the protein's dysregulation in the testes might affect fertility-related issues due to its tissue-specific expression and role in protein regulation. Alteration in the pathways involving KLHL4 and by extension related proteins such as CUL3 have been associated with abnormal cellular growth potentially contributing to cancer development. Knowledge of such interactions may inform therapeutic strategies targeting KLHL4-associated pathways.