Structure and Functions of the 20S and 26S Proteasomes
The proteasome is an essential component of the ATP-dependent proteolytic pathway in eukaryotic cells and is responsible for the degradation of most cellular proteins. The 20S (700-kDa) proteasome contains multiple peptidase activities that function through a new type of proteolytic mechanism involv...
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| Veröffentlicht in: | Annual review of biochemistry 1996-01, Vol.65 (1), p.801-847 |
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| container_title | Annual review of biochemistry |
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| creator | Coux, Olivier Tanaka, Keiji Goldberg, Alfred L |
| description | The proteasome is an essential component of the ATP-dependent proteolytic pathway in eukaryotic cells and is responsible for the degradation of most cellular proteins. The 20S (700-kDa) proteasome contains multiple peptidase activities that function through a new type of proteolytic mechanism involving a threonine active site. The 26S (2000-kDa) complex, which degrades ubiquitinated proteins, contains in addition to the 20S proteasome a 19S regulatory complex composed of multiple ATPases and components necessary for binding protein substrates.
The proteasome has been highly conserved during eukaryotic evolution, and simpler forms are even found in archaebacteria and eubacteria. Major advances have been achieved recently in our knowledge about the molecular organization of the 20S and 19S particles, their subunits, the proteasome's role in MHC-class 1 antigen presentation, and regulators of its activities. This article focuses on recent progress concerning the biochemical mechanisms and intracellular functions of the 20S and 26S proteasomes. |
| doi_str_mv | 10.1146/annurev.bi.65.070196.004101 |
| format | Article |
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The proteasome has been highly conserved during eukaryotic evolution, and simpler forms are even found in archaebacteria and eubacteria. Major advances have been achieved recently in our knowledge about the molecular organization of the 20S and 19S particles, their subunits, the proteasome's role in MHC-class 1 antigen presentation, and regulators of its activities. This article focuses on recent progress concerning the biochemical mechanisms and intracellular functions of the 20S and 26S proteasomes.</description><subject>Animals</subject><subject>ATPase</subject><subject>Autoantigens</subject><subject>Cysteine Endopeptidases - chemistry</subject><subject>Cysteine Endopeptidases - metabolism</subject><subject>Humans</subject><subject>multicatalytic proteinase</subject><subject>Multienzyme Complexes - chemistry</subject><subject>Multienzyme Complexes - metabolism</subject><subject>Muscle Proteins</subject><subject>protease</subject><subject>Proteasome Endopeptidase Complex</subject><subject>protein degradation, ubiquitin</subject><subject>Structure-Activity Relationship</subject><issn>0066-4154</issn><issn>1545-4509</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkFtLxDAQhYMo67r6E4SC4FvrpLl0gy_K4qqwoLD6HJI0xUova5Iq_nuztvju0wxz5pwDH0IXGDKMKb9SXTc4-5npOuMsgwKw4BkAxYAP0BwzylLKQByiOQDnKY2XY3Ti_TsAEEHzGZotlxhH1xzxbXCDCTEvUV2ZrIfOhLrvfNJXSXizSQ7bXyHn2-TZ9cEq37fWn6KjSjXenk1zgV7Xdy-rh3TzdP-4ut2kihIRUlHxinEMjDArLDa6EIISDpXOFSnjwnhpqQENOVeCGlpoQ8rcqLziCoMmC3Q55u5c_zFYH2Rbe2ObRnW2H7wsloQWmBXx8Xp8NK733tlK7lzdKvctMcg9NTlRk7qWnMmRmhypRff5VDPo1pZ_3glT1G9GfR-imhhT2y__r4of-PR_Uw</recordid><startdate>19960101</startdate><enddate>19960101</enddate><creator>Coux, Olivier</creator><creator>Tanaka, Keiji</creator><creator>Goldberg, Alfred L</creator><general>Annual Reviews</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19960101</creationdate><title>Structure and Functions of the 20S and 26S Proteasomes</title><author>Coux, Olivier ; Tanaka, Keiji ; Goldberg, Alfred L</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a439t-9f6f5610535e9e1cb7994360fb2a3d36056de4c0b026a94c47bc3d2ca2f6a10b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>Animals</topic><topic>ATPase</topic><topic>Autoantigens</topic><topic>Cysteine Endopeptidases - chemistry</topic><topic>Cysteine Endopeptidases - metabolism</topic><topic>Humans</topic><topic>multicatalytic proteinase</topic><topic>Multienzyme Complexes - chemistry</topic><topic>Multienzyme Complexes - metabolism</topic><topic>Muscle Proteins</topic><topic>protease</topic><topic>Proteasome Endopeptidase Complex</topic><topic>protein degradation, ubiquitin</topic><topic>Structure-Activity Relationship</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Coux, Olivier</creatorcontrib><creatorcontrib>Tanaka, Keiji</creatorcontrib><creatorcontrib>Goldberg, Alfred L</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Annual review of biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Coux, Olivier</au><au>Tanaka, Keiji</au><au>Goldberg, Alfred L</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structure and Functions of the 20S and 26S Proteasomes</atitle><jtitle>Annual review of biochemistry</jtitle><addtitle>Annu Rev Biochem</addtitle><date>1996-01-01</date><risdate>1996</risdate><volume>65</volume><issue>1</issue><spage>801</spage><epage>847</epage><pages>801-847</pages><issn>0066-4154</issn><eissn>1545-4509</eissn><abstract>The proteasome is an essential component of the ATP-dependent proteolytic pathway in eukaryotic cells and is responsible for the degradation of most cellular proteins. The 20S (700-kDa) proteasome contains multiple peptidase activities that function through a new type of proteolytic mechanism involving a threonine active site. The 26S (2000-kDa) complex, which degrades ubiquitinated proteins, contains in addition to the 20S proteasome a 19S regulatory complex composed of multiple ATPases and components necessary for binding protein substrates.
The proteasome has been highly conserved during eukaryotic evolution, and simpler forms are even found in archaebacteria and eubacteria. Major advances have been achieved recently in our knowledge about the molecular organization of the 20S and 19S particles, their subunits, the proteasome's role in MHC-class 1 antigen presentation, and regulators of its activities. This article focuses on recent progress concerning the biochemical mechanisms and intracellular functions of the 20S and 26S proteasomes.</abstract><cop>Palo Alto, CA 94303-0139</cop><cop>4139 El Camino Way, P.O. Box 10139</cop><cop>USA</cop><pub>Annual Reviews</pub><pmid>8811196</pmid><doi>10.1146/annurev.bi.65.070196.004101</doi><tpages>47</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0066-4154 |
| ispartof | Annual review of biochemistry, 1996-01, Vol.65 (1), p.801-847 |
| issn | 0066-4154 1545-4509 |
| language | eng |
| recordid | cdi_pubmed_primary_8811196 |
| source | Annual Reviews; MEDLINE |
| subjects | Animals ATPase Autoantigens Cysteine Endopeptidases - chemistry Cysteine Endopeptidases - metabolism Humans multicatalytic proteinase Multienzyme Complexes - chemistry Multienzyme Complexes - metabolism Muscle Proteins protease Proteasome Endopeptidase Complex protein degradation, ubiquitin Structure-Activity Relationship |
| title | Structure and Functions of the 20S and 26S Proteasomes |
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