Structural insights into the activation mechanisms of human HtrA serine proteases
Human HtrA1-4 proteins belong to the HtrA family of evolutionarily conserved serine proteases and function as important modulators of many physiological processes, including maintenance of mitochondrial homeostasis, cell signaling and apoptosis. Disturbances in their action are linked to severe dise...
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| Veröffentlicht in: | Archives of biochemistry and biophysics 2017-05, Vol.621, p.6-23 |
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| container_title | Archives of biochemistry and biophysics |
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| creator | Zurawa-Janicka, Dorota Wenta, Tomasz Jarzab, Miroslaw Skorko-Glonek, Joanna Glaza, Przemyslaw Gieldon, Artur Ciarkowski, Jerzy Lipinska, Barbara |
| description | Human HtrA1-4 proteins belong to the HtrA family of evolutionarily conserved serine proteases and function as important modulators of many physiological processes, including maintenance of mitochondrial homeostasis, cell signaling and apoptosis. Disturbances in their action are linked to severe diseases, including oncogenesis and neurodegeneration. The HtrA1-4 proteins share structural and functional features of other members of the HtrA protein family, however there are several significant differences in structural architecture and mechanisms of action which makes each of them unique. Our goal is to present recent studies regarding human HtrAs. We focus on their physiological functions, structure and regulation, and describe current models of activation mechanisms. Knowledge of molecular basis of the human HtrAs' action is a subject of great interest; it is crucial for understanding their relevance in cellular physiology and pathogenesis as well as for using them as targets in future therapies of diseases such as neurodegenerative disorders and cancer. |
| doi_str_mv | 10.1016/j.abb.2017.04.004 |
| format | Article |
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Disturbances in their action are linked to severe diseases, including oncogenesis and neurodegeneration. The HtrA1-4 proteins share structural and functional features of other members of the HtrA protein family, however there are several significant differences in structural architecture and mechanisms of action which makes each of them unique. Our goal is to present recent studies regarding human HtrAs. We focus on their physiological functions, structure and regulation, and describe current models of activation mechanisms. 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All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c353t-bb494db14beaeb22df508f321db7145b939103d87f5fdfc78cfbc66b89b1bfd43</citedby><cites>FETCH-LOGICAL-c353t-bb494db14beaeb22df508f321db7145b939103d87f5fdfc78cfbc66b89b1bfd43</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.abb.2017.04.004$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,778,782,3539,27907,27908,45978</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28396256$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zurawa-Janicka, Dorota</creatorcontrib><creatorcontrib>Wenta, Tomasz</creatorcontrib><creatorcontrib>Jarzab, Miroslaw</creatorcontrib><creatorcontrib>Skorko-Glonek, Joanna</creatorcontrib><creatorcontrib>Glaza, Przemyslaw</creatorcontrib><creatorcontrib>Gieldon, Artur</creatorcontrib><creatorcontrib>Ciarkowski, Jerzy</creatorcontrib><creatorcontrib>Lipinska, Barbara</creatorcontrib><title>Structural insights into the activation mechanisms of human HtrA serine proteases</title><title>Archives of biochemistry and biophysics</title><addtitle>Arch Biochem Biophys</addtitle><description>Human HtrA1-4 proteins belong to the HtrA family of evolutionarily conserved serine proteases and function as important modulators of many physiological processes, including maintenance of mitochondrial homeostasis, cell signaling and apoptosis. Disturbances in their action are linked to severe diseases, including oncogenesis and neurodegeneration. The HtrA1-4 proteins share structural and functional features of other members of the HtrA protein family, however there are several significant differences in structural architecture and mechanisms of action which makes each of them unique. Our goal is to present recent studies regarding human HtrAs. We focus on their physiological functions, structure and regulation, and describe current models of activation mechanisms. Knowledge of molecular basis of the human HtrAs' action is a subject of great interest; it is crucial for understanding their relevance in cellular physiology and pathogenesis as well as for using them as targets in future therapies of diseases such as neurodegenerative disorders and cancer.</description><subject>Allosteric regulation</subject><subject>Apoptosis - physiology</subject><subject>Binding Sites</subject><subject>Enzyme Activation</subject><subject>HtrA proteins</subject><subject>Humans</subject><subject>Mitochondria - physiology</subject><subject>PDZ domain</subject><subject>PDZ Domains - physiology</subject><subject>Protein Binding</subject><subject>Protein Conformation</subject><subject>Serine Endopeptidases - chemistry</subject><subject>Serine Endopeptidases - metabolism</subject><subject>Serine Endopeptidases - ultrastructure</subject><subject>Serine proteases</subject><subject>Signal Transduction - physiology</subject><subject>Structure-Activity Relationship</subject><issn>0003-9861</issn><issn>1096-0384</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1r3DAQhkVJaLZpf0AuQcdc7I4sWZbpaVmSbGGhlLZnoY9RV8vaTiU5kH8fh01zzGnm8LzvMA8hVwxqBkx-PdTG2roB1tUgagDxgawY9LICrsQZWQEAr3ol2QX5lPMBgDEhm4_kolG8l00rV-Tnr5JmV-ZkjjSOOf7dl7wsZaJlj9S4Eh9NidNIB3R7M8Y8ZDoFup8HM9JtSWuaMcUR6UOaCpqM-TM5D-aY8cvrvCR_7m5_b7bV7sf99816Vzne8lJZK3rhLRMWDdqm8aEFFXjDvO2YaG3Pewbcqy60wQfXKResk9Kq3jIbvOCX5ObUu1z-N2MueojZ4fFoRpzmrJlSsmuh7ZsFZSfUpSnnhEE_pDiY9KQZ6BeT-qAXk_rFpAahF5NL5vq1frYD-rfEf3UL8O0E4PLkY8Sks4s4OvQxoSvaT_Gd-mfc3oU9</recordid><startdate>20170501</startdate><enddate>20170501</enddate><creator>Zurawa-Janicka, Dorota</creator><creator>Wenta, Tomasz</creator><creator>Jarzab, Miroslaw</creator><creator>Skorko-Glonek, Joanna</creator><creator>Glaza, Przemyslaw</creator><creator>Gieldon, Artur</creator><creator>Ciarkowski, Jerzy</creator><creator>Lipinska, Barbara</creator><general>Elsevier Inc</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>20170501</creationdate><title>Structural insights into the activation mechanisms of human HtrA serine proteases</title><author>Zurawa-Janicka, Dorota ; 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| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | Allosteric regulation Apoptosis - physiology Binding Sites Enzyme Activation HtrA proteins Humans Mitochondria - physiology PDZ domain PDZ Domains - physiology Protein Binding Protein Conformation Serine Endopeptidases - chemistry Serine Endopeptidases - metabolism Serine Endopeptidases - ultrastructure Serine proteases Signal Transduction - physiology Structure-Activity Relationship |
| title | Structural insights into the activation mechanisms of human HtrA serine proteases |
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