USP8
Description
The USP8 (ubiquitin specific peptidase 8) is a protein-coding gene located on chromosome 15.
Ubiquitin carboxyl-terminal hydrolase 8 is an enzyme that in humans is encoded by the USP8 gene.
== Interactions == USP8 has been shown to interact with RNF41 and STAM2.
USP8 is a deubiquitinase that removes ubiquitin from proteins, playing a crucial role in regulating protein turnover by preventing degradation. It can process both 'Lys-48' and 'Lys-63'-linked ubiquitin chains. Its activity is enhanced during the M phase of the cell cycle. USP8 is involved in cell proliferation and is required for entry into the S phase in response to serum stimulation. It might regulate T-cell anergy mediated by RNF128 through a complex containing RNF128 and OTUB1. USP8 likely regulates the stability of STAM2 and RASGRF1. It governs endosomal ubiquitin dynamics, cargo sorting, membrane traffic at early endosomes, and maintains ESCRT-0 stability. The level of protein ubiquitination on endosomes is crucial for maintaining the organelle's morphology. USP8 deubiquitinates EPS15 and controls tyrosine kinase stability. It removes conjugated ubiquitin from EGFR, regulating EGFR degradation and downstream MAPK signaling. USP8 is involved in acrosome biogenesis through interaction with the spermatid ESCRT-0 complex and microtubules. It deubiquitinates BIRC6/bruce and KIF23/MKLP1. USP8 deubiquitinates BACE1, inhibiting its lysosomal degradation and modulating BACE-mediated APP cleavage and amyloid-beta formation (PubMed:27302062).
USP8 is also known as HumORF8, PITA4, SPG59, UBPY.
Associated Diseases
- Autosomal recessive spastic paraplegia type 59
- Pituitary adenoma 4, ACTH-secreting, somatic
- Cushing disease
