Targeting of parvulin interactors by diazirine mediated cross-linking discloses a cellular role of human Par14/17 in actin polymerization
The peptidyl-prolyl isomerases (PPIases) Parvulin 14 (Par14) and Parvulin 17 (Par17) result from alternative transcription initiation of the gene. Whereas Par14 is present in all metazoan, Par17 is only expressed in Hominidae. Par14 resides mainly within the cellular nucleus, while Par17 is transloc...
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| Veröffentlicht in: | Biological chemistry 2020-07, Vol.401 (8), p.955-968 |
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| creator | Goehring, Anna Michin, Irina Gerdes, Tina Schulze, Nina Blueggel, Mike Rehic, Edisa Kaschani, Farnusch Kaiser, Markus Bayer, Peter |
| description | The peptidyl-prolyl
isomerases (PPIases) Parvulin 14 (Par14) and Parvulin 17 (Par17) result from alternative transcription initiation of the
gene. Whereas Par14 is present in all metazoan, Par17 is only expressed in Hominidae. Par14 resides mainly within the cellular nucleus, while Par17 is translocated into mitochondria. Using photo-affinity labeling, cross-linking and mass spectrometry (MS) we identified binding partners for both enzymes from HeLa lysates and disentangled their cellular roles. Par14 is involved in biogenesis of ribonucleoprotein (RNP)-complexes, RNA processing and DNA repair. Its elongated isoform Par17 participates in protein transport/translocation and in cytoskeleton organization. Nuclear magnetic resonance (NMR) spectroscopy reveals that Par17 binds to β-actin with its N-terminal region, while both parvulins initiate actin polymerization depending on their PPIase activity as monitored by fluorescence spectroscopy. The knockdown (KD) of Par17 in HCT116 cells results in a defect in cell motility and migration. |
| doi_str_mv | 10.1515/hsz-2019-0423 |
| format | Article |
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isomerases (PPIases) Parvulin 14 (Par14) and Parvulin 17 (Par17) result from alternative transcription initiation of the
gene. Whereas Par14 is present in all metazoan, Par17 is only expressed in Hominidae. Par14 resides mainly within the cellular nucleus, while Par17 is translocated into mitochondria. Using photo-affinity labeling, cross-linking and mass spectrometry (MS) we identified binding partners for both enzymes from HeLa lysates and disentangled their cellular roles. Par14 is involved in biogenesis of ribonucleoprotein (RNP)-complexes, RNA processing and DNA repair. Its elongated isoform Par17 participates in protein transport/translocation and in cytoskeleton organization. Nuclear magnetic resonance (NMR) spectroscopy reveals that Par17 binds to β-actin with its N-terminal region, while both parvulins initiate actin polymerization depending on their PPIase activity as monitored by fluorescence spectroscopy. The knockdown (KD) of Par17 in HCT116 cells results in a defect in cell motility and migration.</description><identifier>ISSN: 1431-6730</identifier><identifier>EISSN: 1437-4315</identifier><identifier>DOI: 10.1515/hsz-2019-0423</identifier><identifier>PMID: 32142471</identifier><language>eng</language><publisher>Germany: De Gruyter</publisher><subject>Actin ; Affinity labeling ; Cell migration ; Crosslinking ; Cytoskeleton ; Deoxyribonucleic acid ; DNA ; DNA repair ; Fluorescence ; Fluorescence spectroscopy ; isomerase ; LC-MS ; Lysates ; Mass spectrometry ; Mass spectroscopy ; Mitochondria ; NMR ; Nuclear magnetic resonance ; Nuclei (cytology) ; peptidyl-prolyl ; Peptidylprolyl isomerase ; photo-affinity labeling ; Photoaffinity labeling ; Polymerization ; PPIase ; Protein transport ; RNA processing ; Spectroscopy ; Transcription initiation ; Translocation</subject><ispartof>Biological chemistry, 2020-07, Vol.401 (8), p.955-968</ispartof><rights>2020 Walter de Gruyter GmbH, Berlin/Boston</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c374t-acb895d79a64cf9d988328e9bbac6419112bf6eb69b23591ede31ade75fb9a5c3</citedby><cites>FETCH-LOGICAL-c374t-acb895d79a64cf9d988328e9bbac6419112bf6eb69b23591ede31ade75fb9a5c3</cites><orcidid>0000-0003-0435-7202</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.degruyter.com/document/doi/10.1515/hsz-2019-0423/pdf$$EPDF$$P50$$Gwalterdegruyter$$H</linktopdf><linktohtml>$$Uhttps://www.degruyter.com/document/doi/10.1515/hsz-2019-0423/html$$EHTML$$P50$$Gwalterdegruyter$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,66754,68538</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/32142471$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Goehring, Anna</creatorcontrib><creatorcontrib>Michin, Irina</creatorcontrib><creatorcontrib>Gerdes, Tina</creatorcontrib><creatorcontrib>Schulze, Nina</creatorcontrib><creatorcontrib>Blueggel, Mike</creatorcontrib><creatorcontrib>Rehic, Edisa</creatorcontrib><creatorcontrib>Kaschani, Farnusch</creatorcontrib><creatorcontrib>Kaiser, Markus</creatorcontrib><creatorcontrib>Bayer, Peter</creatorcontrib><title>Targeting of parvulin interactors by diazirine mediated cross-linking discloses a cellular role of human Par14/17 in actin polymerization</title><title>Biological chemistry</title><addtitle>Biol Chem</addtitle><description>The peptidyl-prolyl
isomerases (PPIases) Parvulin 14 (Par14) and Parvulin 17 (Par17) result from alternative transcription initiation of the
gene. Whereas Par14 is present in all metazoan, Par17 is only expressed in Hominidae. Par14 resides mainly within the cellular nucleus, while Par17 is translocated into mitochondria. Using photo-affinity labeling, cross-linking and mass spectrometry (MS) we identified binding partners for both enzymes from HeLa lysates and disentangled their cellular roles. Par14 is involved in biogenesis of ribonucleoprotein (RNP)-complexes, RNA processing and DNA repair. Its elongated isoform Par17 participates in protein transport/translocation and in cytoskeleton organization. Nuclear magnetic resonance (NMR) spectroscopy reveals that Par17 binds to β-actin with its N-terminal region, while both parvulins initiate actin polymerization depending on their PPIase activity as monitored by fluorescence spectroscopy. The knockdown (KD) of Par17 in HCT116 cells results in a defect in cell motility and migration.</description><subject>Actin</subject><subject>Affinity labeling</subject><subject>Cell migration</subject><subject>Crosslinking</subject><subject>Cytoskeleton</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>DNA repair</subject><subject>Fluorescence</subject><subject>Fluorescence spectroscopy</subject><subject>isomerase</subject><subject>LC-MS</subject><subject>Lysates</subject><subject>Mass spectrometry</subject><subject>Mass spectroscopy</subject><subject>Mitochondria</subject><subject>NMR</subject><subject>Nuclear magnetic resonance</subject><subject>Nuclei (cytology)</subject><subject>peptidyl-prolyl</subject><subject>Peptidylprolyl isomerase</subject><subject>photo-affinity labeling</subject><subject>Photoaffinity labeling</subject><subject>Polymerization</subject><subject>PPIase</subject><subject>Protein transport</subject><subject>RNA processing</subject><subject>Spectroscopy</subject><subject>Transcription initiation</subject><subject>Translocation</subject><issn>1431-6730</issn><issn>1437-4315</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><recordid>eNptkUtv1TAQhSMEoqWwZIsssWET6vEjjiU2qOIlVaKLso5sZ3Lr4sQXOym69x_wr3F6C5WqbuxZfHPm6Jyqeg30PUiQp1d5XzMKuqaC8SfVMQiuasFBPr2doW4Up0fVi5yvKaUtFfx5dcQZCCYUHFd_Lk3a4OynDYkD2Zp0swQ_ET_NmIybY8rE7kjvzd4nPyEZscwz9sSlmHNd2J_rbu-zCzFjJoY4DGEJJpEUA66qV8toJnJhEohTUEWbFOXybmPYjZj83sw-Ti-rZ4MJGV_d_SfVj8-fLs--1uffv3w7-3heO67EXBtnWy17pU0j3KB73bactaitNa4RoAGYHRq0jbaMSw3YIwfTo5KD1UY6flK9O-huU_y1YJ67sZgvns2EcckdK2c4qFZBQd8-QK_jkqbirmOCNaqhUopC1QfqNpKEQ7dNfjRp1wHt1o660lG3dtStHRX-zZ3qYkuc_-l_pRTgwwH4bUKpocdNWnZluL_-qLCgUJKR_C_szqKu</recordid><startdate>20200728</startdate><enddate>20200728</enddate><creator>Goehring, Anna</creator><creator>Michin, Irina</creator><creator>Gerdes, Tina</creator><creator>Schulze, Nina</creator><creator>Blueggel, Mike</creator><creator>Rehic, Edisa</creator><creator>Kaschani, Farnusch</creator><creator>Kaiser, Markus</creator><creator>Bayer, Peter</creator><general>De Gruyter</general><general>Walter de Gruyter GmbH</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QO</scope><scope>7QP</scope><scope>7QR</scope><scope>7T5</scope><scope>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0003-0435-7202</orcidid></search><sort><creationdate>20200728</creationdate><title>Targeting of parvulin interactors by diazirine mediated cross-linking discloses a cellular role of human Par14/17 in actin polymerization</title><author>Goehring, Anna ; 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gene. Whereas Par14 is present in all metazoan, Par17 is only expressed in Hominidae. Par14 resides mainly within the cellular nucleus, while Par17 is translocated into mitochondria. Using photo-affinity labeling, cross-linking and mass spectrometry (MS) we identified binding partners for both enzymes from HeLa lysates and disentangled their cellular roles. Par14 is involved in biogenesis of ribonucleoprotein (RNP)-complexes, RNA processing and DNA repair. Its elongated isoform Par17 participates in protein transport/translocation and in cytoskeleton organization. Nuclear magnetic resonance (NMR) spectroscopy reveals that Par17 binds to β-actin with its N-terminal region, while both parvulins initiate actin polymerization depending on their PPIase activity as monitored by fluorescence spectroscopy. The knockdown (KD) of Par17 in HCT116 cells results in a defect in cell motility and migration.</abstract><cop>Germany</cop><pub>De Gruyter</pub><pmid>32142471</pmid><doi>10.1515/hsz-2019-0423</doi><tpages>14</tpages><orcidid>https://orcid.org/0000-0003-0435-7202</orcidid></addata></record> |
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| ispartof | Biological chemistry, 2020-07, Vol.401 (8), p.955-968 |
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| source | De Gruyter journals |
| subjects | Actin Affinity labeling Cell migration Crosslinking Cytoskeleton Deoxyribonucleic acid DNA DNA repair Fluorescence Fluorescence spectroscopy isomerase LC-MS Lysates Mass spectrometry Mass spectroscopy Mitochondria NMR Nuclear magnetic resonance Nuclei (cytology) peptidyl-prolyl Peptidylprolyl isomerase photo-affinity labeling Photoaffinity labeling Polymerization PPIase Protein transport RNA processing Spectroscopy Transcription initiation Translocation |
| title | Targeting of parvulin interactors by diazirine mediated cross-linking discloses a cellular role of human Par14/17 in actin polymerization |
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