adrm1/uch37

ADRM1/UCH37 proteins play a critical role in the regulation of protein degradation processes, specifically by participating in the recognition and processing of ubiquitinated proteins targeted for degradation by the proteasome.

ADRM1/UCH37 proteins can form a larger protein complex known as the 19S regulatory particle of the proteasome, which plays a central role in protein degradation.

The expression or activity of ADRM1/UCH37 proteins can be regulated by various signaling pathways and cellular factors, including proteasome inhibitors and stress-inducing agents.

Post-translational modifications, including phosphorylation and ubiquitination, have been identified on ADRM1/UCH37 proteins, and they can modulate their interaction and function.

Specific domains within ADRM1/UCH37 proteins, such as the MPN domain in ADRM1 and the UCH domain in UCH37, are essential for their interaction and function.

ADRM1/UCH37 proteins exhibit a predominantly cytoplasmic localization, but their subcellular distribution may change in response to specific cellular conditions or stimuli.

The ADRM1/UCH37 complex interacts with ubiquitinated substrates and facilitates their delivery to the proteasome for degradation, contributing to the regulation of protein turnover.

Experimental evidence, such as co-immunoprecipitation and co-localization studies, supports the interaction between ADRM1 and UCH37 proteins.

Experimental approaches, including knockout or overexpression studies in animal models, have been employed to investigate the functional significance of ADRM1/UCH37 proteins in vivo, revealing their importance in protein homeostasis and cellular physiology.

Dysregulation or dysfunction of ADRM1/UCH37 proteins can disrupt protein degradation processes, leading to protein accumulation and potential implications in cellular dysfunction and disease pathogenesis.