What is PSMD2 protein?

PSMD2 (Proteasome 26S Subunit Ubiquitin Receptor, Non-ATPase 2) is a Protein Coding gene.

How many proteasomes are in a cell?

In 2012, two independent efforts have elucidated the molecular architecture of the 26S proteasome by single particle electron microscopy.

What is 20S proteasome?

The 20S proteasome is a multicatalytic proteinase, which is the catalytic unit of the 26S proteasome, the eukaryotic adenosine triphosphate (ATP)-dependent protease complex responsible for degrading a variety of cellular proteins that have acquired a specific degradation signal(s) such as a multiubiquitin chain.

What is the function of proteasomes?

The proteasome is a multisubunit enzyme complex that plays a central role in the regulation of proteins that control cell-cycle progression and apoptosis, and has therefore become an important target for anticancer therapy.

Why do we need proteasomes?

Proteasomes. Proteasomes are complex intracellular proteases that function in regulated degradation of cellular proteins. Turnover of proteins by the proteasome regulates many processes, including the cell cycle, circadian cycles, transcription, growth, development, as well as removal of abnormal proteins.

What is 26 S proteasome?

The 26S proteasome is the major protease in eukaryotic cells, responsible for protein degradation in both the cytosol and the nucleus. Ubiquitin modifications target condemned proteins to the proteasome.

What is the difference between lysosomes and proteasomes?

Generally, the proteasome can degrade individual cellular proteins in a highly targeted fashion via the ubiquitin-proteasome system (UPS) while lysosomes degrade cytoplasmic components, including some individual proteins, protein aggregates, and defective or surplus organelles, through autophagy.

What is the role of ubiquitin and proteasomes?

The ubiquitin-proteasome system is the major protein degradation pathway in the cell. Specifically, the proteasome is responsible for clearance of abnormal, denatured or in general damaged proteins as well as for the regulated degradation of short-lived proteins.

What are proteasomes made of?

The proteasome is made up of two subcomplexes: a catalytic core particle (CP; also known as the 20S proteasome) and one or two terminal 19S regulatory particle(s) (RP) that serves as a proteasome activator with a molecular mass of approximately 700 kDa (called PA700) (Table 1).

What is the PSMD2 gene?

The gene PSMD2 encodes one of the non-ATPase subunits of the 19S regulator lid. In addition to participation in proteasome function, this subunit may also participate in the TNF signalling pathway since it interacts with the tumor necrosis factor type 1 receptor. A pseudogene has been identified on chromosome 1.

What is a plasmid?

A plasmid is a small, often circular DNA molecule found in bacteria and other cells. Plasmids are separate from the bacterial chromosome and replicate independently of it. They generally carry only a small number of genes, notably some associated with antibiotic resistance. Plasmids may be passed between different bacterial cells.

What is the role of PSMD2 in cell cycle arrest?

Rescue assays demonstrated that the cell cycle arrest caused by silencing PSMD2 partially resulted from increased p21 and/or p27. Mechanically, PSMD2 physically interacted with p21 and p27 and mediated their ubiquitin-proteasome degradation with the cooperation of USP14.

Is PSMD2 a potential therapeutic target in lung adenocarcinoma?

“Proteasomal non-catalytic subunit PSMD2 as a potential therapeutic target in association with various clinicopathologic features in lung adenocarcinomas”. Molecular Carcinogenesis. 50 (4): 301–9. doi: 10.1002/mc.20632.