PSMB7

PSMB7
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4R3O, 4R67, 5A0Q
Identifiers
Aliases	PSMB7 , proteasome subunit beta 7, Z, proteasome 20S subunit beta 7
External IDs	OMIM: 604030 MGI: 107637 HomoloGene: 2093 GeneCards: PSMB7
Gene location (Human) Chr. Chromosome 9 (human) [1] Band 9q33.3 Start 124,353,465 bp [1] End 124,415,444 bp [1]
Gene location (Mouse) Chr. Chromosome 2 (mouse) [2] Band 2 B|2 24.42 cM Start 38,478,048 bp [2] End 38,534,099 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in ganglionic eminence right adrenal gland left adrenal gland skin of abdomen stromal cell of endometrium body of pancreas prefrontal cortex rectum nucleus accumbens caudate nucleus Top expressed in medial ganglionic eminence somite triceps brachii muscle temporal muscle digastric muscle sternocleidomastoid muscle maxillary prominence right ventricle optic nerve vastus lateralis muscle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function endopeptidase activity peptidase activity protein binding threonine-type endopeptidase activity hydrolase activity Cellular component nucleoplasm proteasome complex extracellular exosome nucleus proteasome core complex extracellular region cytoplasm cytosol secretory granule lumen ficolin-1-rich granule lumen proteasome core complex, beta-subunit complex Biological process regulation of cellular amino acid metabolic process antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent regulation of mRNA stability positive regulation of protein targeting to mitochondrion positive regulation of canonical Wnt signaling pathway protein polyubiquitination stimulatory C-type lectin receptor signaling pathway tumor necrosis factor-mediated signaling pathway MAPK cascade proteolysis Fc-epsilon receptor signaling pathway NIK/NF-kappaB signaling anaphase-promoting complex-dependent catabolic process proteolysis involved in cellular protein catabolic process T cell receptor signaling pathway negative regulation of canonical Wnt signaling pathway Wnt signaling pathway, planar cell polarity pathway proteasome-mediated ubiquitin-dependent protein catabolic process viral process negative regulation of G2/M transition of mitotic cell cycle protein deubiquitination SCF-dependent proteasomal ubiquitin-dependent protein catabolic process neutrophil degranulation transmembrane transport regulation of transcription from RNA polymerase II promoter in response to hypoxia post-translational protein modification regulation of hematopoietic stem cell differentiation proteasomal protein catabolic process proteasomal ubiquitin-independent protein catabolic process interleukin-1-mediated signaling pathway regulation of mitotic cell cycle phase transition Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 5695 19177 Ensembl ENSG00000136930 ENSMUSG00000026750 UniProt Q99436 Q5TBG5 P70195 RefSeq (mRNA) NM_002799 NM_011187 RefSeq (protein) NP_002790 NP_035317 Location (UCSC) Chr 9: 124.35 – 124.42 Mb Chr 2: 38.48 – 38.53 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Proteasome subunit beta type-7 as known as 20S proteasome subunit beta-2 is a protein that in humans is encoded by the PSMB7 gene. ^{[5] [6]}

This protein is one of the 17 essential subunits (alpha subunits 1-7, constitutive beta subunits 1-7, and inducible subunits including beta1i, beta2i, beta5i) that contributes to the complete assembly of 20S proteasome complex. In particular, proteasome subunit beta type-5, along with other beta subunits, assemble into two heptameric rings and subsequently a proteolytic chamber for substrate degradation. This protein contains "Trypsin-like" activity and is capable of cleaving after basic residues of peptide. ^[5] The eukaryotic proteasome recognized degradable proteins, including damaged proteins for protein quality control purpose or key regulatory protein components for dynamic biological processes. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides.

Structure

Gene

The human PSMB7 gene has 8 exons and locates at chromosome band 9q34.11-q34.12.

Protein

The gene PSMB7 encodes a member of the proteasome B-type family, also known as the T1B family, that is a 20S core beta subunit in the proteasome. Expression of this catalytic subunit (beta 2, according to systematic nomenclature) is downregulated by gamma interferon due to an alternatively elevated expression of inducible subunit beta2i, which leads to augmented incorporation of beta2i instead of beta2 into the final assembled 20S complex. ^[6] The human protein proteasome subunit beta type-7 is 25 kDa in size and composed of 234 amino acids. The calculated theoretical pI of this protein is 5.61.

Complex assembly

The proteasome is a multicatalytic proteinase complex with a highly ordered 20S core structure. This barrel-shaped core structure is composed of 4 axially stacked rings of 28 non-identical subunits: the two end rings are each formed by 7 alpha subunits, and the two central rings are each formed by 7 beta subunits. Three beta subunits (beta1, beta2, beta5) each contains a proteolytic active site and has distinct substrate preferences. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. ^{[7] [8]}

Function

Protein functions are supported by its tertiary structure and its interaction with associating partners. As one of 28 subunits of 20S proteasome, protein proteasome subunit beta type-2 contributes to form a proteolytic environment for substrate degradation. Evidences of the crystal structures of isolated 20S proteasome complex demonstrate that the two rings of beta subunits form a proteolytic chamber and maintain all their active sites of proteolysis within the chamber. ^[8] Concomitantly, the rings of alpha subunits form the entrance for substrates entering the proteolytic chamber. In an inactivated 20S proteasome complex, the gate into the internal proteolytic chamber are guarded by the N-terminal tails of specific alpha-subunit. This unique structure design prevents random encounter between proteolytic active sites and protein substrate, which makes protein degradation a well-regulated process. ^{[9] [10]} 20S proteasome complex, by itself, is usually functionally inactive. The proteolytic capacity of 20S core particle (CP) can be activated when CP associates with one or two regulatory particles (RP) on one or both side of alpha rings. These regulatory particles include 19S proteasome complexes, 11S proteasome complex, etc. Following the CP-RP association, the confirmation of certain alpha subunits will change and consequently cause the opening of substrate entrance gate. Besides RPs, the 20S proteasomes can also be effectively activated by other mild chemical treatments, such as exposure to low levels of sodium dodecylsulfate (SDS) or NP-14. ^{[10] [11]}

The 20S proteasome subunit beta-2 (systematic nomenclature) is originally expressed as a precursor with 277 amino acids. The fragment of 43 amino acids at peptide N-terminal is essential for proper protein folding and subsequent complex assembly. At the end-stage of complex assembly, the N-terminal fragment of beta5 subunit is cleaved, forming the mature beta2 subunit of 20S complex. ^[12] During the basal assembly, and proteolytic processing is required to generate a mature subunit. This subunit is not present in the immunoproteasome and is replaced by catalytic subunit 2i (proteasome beta 10 subunit).

Clinical significance

The proteasome and its subunits are of clinical significance for at least two reasons: (1) a compromised complex assembly or a dysfunctional proteasome can be associated with the underlying pathophysiology of specific diseases, and (2) they can be exploited as drug targets for therapeutic interventions. More recently, more effort has been made to consider the proteasome for the development of novel diagnostic markers and strategies. An improved and comprehensive understanding of the pathophysiology of the proteasome should lead to clinical applications in the future.

The proteasomes form a pivotal component for the ubiquitin–proteasome system (UPS) ^[13] and corresponding cellular Protein Quality Control (PQC). Protein ubiquitination and subsequent proteolysis and degradation by the proteasome are important mechanisms in the regulation of the cell cycle, cell growth and differentiation, gene transcription, signal transduction and apoptosis. ^[14] Subsequently, a compromised proteasome complex assembly and function lead to reduced proteolytic activities and the accumulation of damaged or misfolded protein species. Such protein accumulation may contribute to the pathogenesis and phenotypic characteristics in neurodegenerative diseases, ^{[15] [16]} cardiovascular diseases, ^{[17] [18] [19]} inflammatory responses and autoimmune diseases, ^[20] and systemic DNA damage responses leading to malignancies. ^[21]

Several experimental and clinical studies have indicated that aberrations and deregulations of the UPS contribute to the pathogenesis of several neurodegenerative and myodegenerative disorders, including Alzheimer's disease, ^[22] Parkinson's disease ^[23] and Pick's disease, ^[24] Amyotrophic lateral sclerosis (ALS), ^[24] Huntington's disease, ^[23] Creutzfeldt–Jakob disease, ^[25] and motor neuron diseases, polyglutamine (PolyQ) diseases, Muscular dystrophies ^[26] and several rare forms of neurodegenerative diseases associated with dementia. ^[27] As part of the ubiquitin–proteasome system (UPS), the proteasome maintains cardiac protein homeostasis and thus plays a significant role in cardiac ischemic injury, ^[28] ventricular hypertrophy ^[29] and heart failure. ^[30] Additionally, evidence is accumulating that the UPS plays an essential role in malignant transformation. UPS proteolysis plays a major role in responses of cancer cells to stimulatory signals that are critical for the development of cancer. Accordingly, gene expression by degradation of transcription factors, such as p53, c-jun, c-Fos, NF-κB, c-Myc, HIF-1α, MATα2, STAT3, sterol-regulated element-binding proteins and androgen receptors are all controlled by the UPS and thus involved in the development of various malignancies. ^[31] Moreover, the UPS regulates the degradation of tumor suppressor gene products such as adenomatous polyposis coli (APC) in colorectal cancer, retinoblastoma (Rb). and von Hippel–Lindau tumor suppressor (VHL), as well as a number of proto-oncogenes (Raf, Myc, Myb, Rel, Src, Mos, ABL). The UPS is also involved in the regulation of inflammatory responses. This activity is usually attributed to the role of proteasomes in the activation of NF-κB which further regulates the expression of pro inflammatory cytokines such as TNF-α, IL-β, IL-8, adhesion molecules (ICAM-1, VCAM-1, P-selectin) and prostaglandins and nitric oxide (NO). ^[20] Additionally, the UPS also plays a role in inflammatory responses as regulators of leukocyte proliferation, mainly through proteolysis of cyclines and the degradation of CDK inhibitors. ^[32] Lastly, autoimmune disease patients with SLE, Sjögren syndrome and rheumatoid arthritis (RA) predominantly exhibit circulating proteasomes which can be applied as clinical biomarkers. ^[33]

The PSMB7 protein has a variety of clinically relevant constituents. For instance, in breast cancer cells, a high expression level of the PSMB7 protein suggests a shorter survival than in cells with a lower expression level. ^[34] This interesting finding indicates that the PSMB7 protein may be used as a clinical prognostic biomarker in breast cancer. ^[34] The same study also suggested that the PSMB7 protein is involved in anthracycline resistance, which is an antibiotic derived from streptomyces bacteria and used as an anticancer chemotherapy for leukemias, lymphomas, breast cancer, uterine, ovarian and lung cancers. ^[35] Furthermore, the PSMB7 protein may also be involved in the resistance to 5-fluoro uracil (5-FU) therapy. Targeting the PSMB7 gene, to down-regulate PSMB7 protein, may overcome resistance to 5-FU and thus a possible new approach to treat hepatocellular carcinoma with this chemotherapeutic drug. ^[36] High PSMB7 expression is an unfavourable prognostic marker in breast cancer. ^[34] In this, survival of resistant breast cancer cell lines decreased after doxorubicin or paclitaxel treatment when PSMB7 was knocked down by RNA interference. These results were validated in 1592 microarray samples: patients with high PSMB7 expression had a significantly shorter survival than patients with low expression. Knockdown of the PSMB7 gene may also induce autophagy in cardiomyocytes. ^[37]

References

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2. GRCm38: Ensembl release 89: ENSMUSG00000026750 - Ensembl, May 2017
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15. Sulistio YA, Heese K (March 2016). "The Ubiquitin–Proteasome System and Molecular Chaperone Deregulation in Alzheimer's Disease". Molecular Neurobiology. 53 (2): 905–31. doi:10.1007/s12035-014-9063-4. PMID   25561438. S2CID   14103185.
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34. Munkácsy G, Abdul-Ghani R, Mihály Z, Tegze B, Tchernitsa O, Surowiak P, Schäfer R, Györffy B (January 2010). "PSMB7 is associated with anthracycline resistance and is a prognostic biomarker in breast cancer". British Journal of Cancer. 102 (2): 361–8. doi:10.1038/sj.bjc.6605478. PMC   2816652 . PMID   20010949.
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37. Kyrychenko VO, Nagibin VS, Tumanovska LV, Pashevin DO, Gurianova VL, Moibenko AA, Dosenko VE, Klionsky DJ (2014). "Knockdown of PSMB7 induces autophagy in cardiomyocyte cultures: possible role in endoplasmic reticulum stress". Pathobiology. 81 (1): 8–14. doi: 10.1159/000350704 . PMID   23969338.

Further reading

• Rivett AJ, Bose S, Brooks P, Broadfoot KI (2001). "Regulation of proteasome complexes by gamma-interferon and phosphorylation". Biochimie. 83 (3–4): 363–6. doi:10.1016/S0300-9084(01)01249-4. PMID   11295498.
• Goff SP (August 2003). "Death by deamination: a novel host restriction system for HIV-1". Cell. 114 (3): 281–3. doi: 10.1016/S0092-8674(03)00602-0 . PMID   12914693. S2CID   16340355.
• Kristensen P, Johnsen AH, Uerkvitz W, Tanaka K, Hendil KB (December 1994). "Human proteasome subunits from 2-dimensional gels identified by partial sequencing". Biochemical and Biophysical Research Communications. 205 (3): 1785–9. doi:10.1006/bbrc.1994.2876. PMID   7811265.
• Maruyama K, Sugano S (January 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID   8125298.
• Hisamatsu H, Shimbara N, Saito Y, Kristensen P, Hendil KB, Fujiwara T, Takahashi E, Tanahashi N, Tamura T, Ichihara A, Tanaka K (April 1996). "Newly identified pair of proteasomal subunits regulated reciprocally by interferon gamma". The Journal of Experimental Medicine. 183 (4): 1807–16. doi:10.1084/jem.183.4.1807. PMC   2192534 . PMID   8666937.
• Seeger M, Ferrell K, Frank R, Dubiel W (March 1997). "HIV-1 tat inhibits the 20 S proteasome and its 11 S regulator-mediated activation". The Journal of Biological Chemistry. 272 (13): 8145–8. doi: 10.1074/jbc.272.13.8145 . PMID   9079628.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID   9373149.
• Madani N, Kabat D (December 1998). "An endogenous inhibitor of human immunodeficiency virus in human lymphocytes is overcome by the viral Vif protein". Journal of Virology. 72 (12): 10251–5. doi:10.1128/JVI.72.12.10251-10255.1998. PMC   110608 . PMID   9811770.
• Simon JH, Gaddis NC, Fouchier RA, Malim MH (December 1998). "Evidence for a newly discovered cellular anti-HIV-1 phenotype". Nature Medicine. 4 (12): 1397–400. doi:10.1038/3987. PMID   9846577. S2CID   25235070.
• O'Hare T, Wiens GD, Whitcomb EA, Enns CA, Rittenberg MB (July 1999). "Cutting edge: proteasome involvement in the degradation of unassembled Ig light chains". Journal of Immunology. 163 (1): 11–4. doi:10.4049/jimmunol.163.1.11. PMID   10384092.
• Elenich LA, Nandi D, Kent AE, McCluskey TS, Cruz M, Iyer MN, Woodward EC, Conn CW, Ochoa AL, Ginsburg DB, Monaco JJ (September 1999). "The complete primary structure of mouse 20S proteasomes". Immunogenetics. 49 (10): 835–42. doi:10.1007/s002510050562. PMID   10436176. S2CID   20977116.
• Mulder LC, Muesing MA (September 2000). "Degradation of HIV-1 integrase by the N-end rule pathway". The Journal of Biological Chemistry. 275 (38): 29749–53. doi: 10.1074/jbc.M004670200 . PMID   10893419.
• Feng Y, Longo DL, Ferris DK (January 2001). "Polo-like kinase interacts with proteasomes and regulates their activity". Cell Growth & Differentiation. 12 (1): 29–37. PMID   11205743.
• Sheehy AM, Gaddis NC, Choi JD, Malim MH (August 2002). "Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein". Nature. 418 (6898): 646–50. Bibcode:2002Natur.418..646S. doi:10.1038/nature00939. PMID   12167863. S2CID   4403228.
• Huang X, Seifert U, Salzmann U, Henklein P, Preissner R, Henke W, Sijts AJ, Kloetzel PM, Dubiel W (November 2002). "The RTP site shared by the HIV-1 Tat protein and the 11S regulator subunit alpha is crucial for their effects on proteasome function including antigen processing". Journal of Molecular Biology. 323 (4): 771–82. doi:10.1016/S0022-2836(02)00998-1. PMID   12419264.
• Gaddis NC, Chertova E, Sheehy AM, Henderson LE, Malim MH (May 2003). "Comprehensive investigation of the molecular defect in vif-deficient human immunodeficiency virus type 1 virions". Journal of Virology. 77 (10): 5810–20. doi:10.1128/JVI.77.10.5810-5820.2003. PMC   154025 . PMID   12719574.