USP33
USP33 (ubiquitin specific peptidase 33, also known as VDU1 or KIAA1097) is a deubiquitinating enzyme that removes ubiquitin from substrates involved in centrosome duplication, Slit-dependent cell migration and G protein-coupled receptor signalling. Browse Assay Genie's current range of USP33 research reagents below, or read on for the biology behind the target.
USP33 is a deubiquitinating enzyme that cleaves ubiquitin from target proteins and acts on both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. It is involved in centrosome duplication, where it deubiquitinates CCP110 in S and G2/M phase. This stabilises CCP110 during the period in which centrioles duplicate and elongate.
The enzyme also contributes to cell migration through its interaction with the intracellular domain of ROBO1, thereby regulating Slit signalling. It has a role in commissural axon guidance across the ventral midline of the neural tube in a Slit-dependent manner, possibly by deubiquitinating ROBO1. In GPCR signalling, USP33 deubiquitinates the beta-arrestins ARRB1 and ARRB2 and the beta-2 adrenergic receptor (ADRB2). It binds ADRB2 constitutively, deubiquitinates it and inhibits its lysosomal trafficking, supporting receptor recycling and resensitisation after prolonged agonist stimulation. On dissociation it is probably transferred to the translocated beta-arrestins, which suggests a dynamic exchange between ADRB2 and the beta-arrestins. USP33 also deubiquitinates DIO2, which links it to thyroid hormone regulation.
The USP33 gene belongs to the ubiquitin specific peptidases gene group; the protein is a member of the peptidase C19 family, USP20/USP33 subfamily. It was previously named ubiquitin specific protease 33 and is also known as VDU1. According to the NCBI Gene summary, USP33 is negatively regulated through ubiquitination by the von Hippel-Lindau tumour protein (VHL), and alternative splicing produces multiple transcript variants and protein isoforms. Researchers studying the USP33 protein often examine it alongside its substrates and other USP family members. The mouse ortholog is Usp33.
USP33 stabilises CCP110 during S and G2/M phase, making it relevant to studies of centriole duplication and elongation.
By deubiquitinating ADRB2 and beta-arrestins, USP33 shapes receptor recycling, resensitisation and lysosomal sorting after agonist stimulation.
USP33 interacts with ROBO1 to regulate Slit signalling, supporting work on cell migration and commissural axon guidance.
USP33 removes 'Lys-48' and 'Lys-63' chains and deubiquitinates DIO2, connecting protein turnover with thyroid hormone regulation.
USP33 is a deubiquitinating enzyme that removes ubiquitin from specific substrates. It stabilises CCP110 for centrosome duplication, regulates ROBO1 and Slit signalling, and deubiquitinates ADRB2, beta-arrestins and DIO2, influencing GPCR recycling and thyroid hormone regulation.
USP33 is also called VDU1 and KIAA1097, and was previously named ubiquitin specific protease 33. Alternative splicing of the USP33 gene gives multiple transcript variants and protein isoforms, according to the NCBI Gene summary.
USP33 is negatively regulated through ubiquitination by the von Hippel-Lindau tumour protein (VHL). A mouse ortholog, Usp33, exists, so rodent models can be used for functional work; check the datasheet of any product for its validated reactivity.
Other ubiquitin specific peptidases and deubiquitinating enzymes with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q8TEY7; product specifications from Assay Genie datasheets.