Pim-1 preserves mitochondrial morphology by inhibiting dynamin-related protein 1 translocation
Mitochondrial morphological dynamics affect the outcome of ischemic heart damage and pathogenesis. Recently, mitochondrial fission protein dynamin-related protein 1 (Drp1) has been identified as a mediator of mitochondrial morphological changes and cell death during cardiac ischemic injury. In this...
Gespeichert in:
| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2013-04, Vol.110 (15), p.5969-5974 |
|---|---|
| Hauptverfasser: | , , , , , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 5974 |
|---|---|
| container_issue | 15 |
| container_start_page | 5969 |
| container_title | Proceedings of the National Academy of Sciences - PNAS |
| container_volume | 110 |
| creator | Din, Shabana Mason, Matthew Völkers, Mirko Johnson, Bevan Cottage, Christopher T. Wang, Zeping Joyo, Anya Y. Quijada, Pearl Erhardt, Peter Magnuson, Nancy S. Konstandin, Mathias H. Sussman, Mark A. |
| description | Mitochondrial morphological dynamics affect the outcome of ischemic heart damage and pathogenesis. Recently, mitochondrial fission protein dynamin-related protein 1 (Drp1) has been identified as a mediator of mitochondrial morphological changes and cell death during cardiac ischemic injury. In this study, we report a unique relationship between Pim-1 activity and Drp1 regulation of mitochondrial morphology in cardiomyocytes challenged by ischemic stress. Transgenic hearts overexpressing cardiac Pim-1 display reduction of total Drp1 protein levels, increased phosphorylation of Drp1- S⁶³⁷, and inhibition of Drp1 localization to the mitochondria. Consistent with these findings, adenoviral-induced Pim-1 neonatal rat cardiomyocytes (NRCMs) retain a reticular mitochondrial phenotype after simulated ischemia (sI) and decreased Drp1 mitochondrial sequestration. Interestingly, adenovirus Pim-dominant negative NRCMs show increased expression of Bcl-2 homology 3 (BH3)-only protein p53 up-regulated modulator of apoptosis (PUMA), which has been previously shown to induce Drp1 accumulation at mitochondria and increase sensitivity to apoptotic stimuli. Overexpression of the p53 up-regulated modulator of apoptosis–dominant negative adenovirus attenuates localization of Drp1 to mitochondria in adenovirus Pim-dominant negative NRCMs promotes reticular mitochondrial morphology and inhibits cell death during sI. Therefore, Pim-1 activity prevents Drp1 compartmentalization to the mitochondria and preserves reticular mitochondrial morphology in response to sI. |
| doi_str_mv | 10.1073/pnas.1213294110 |
| format | Article |
| fullrecord | <record><control><sourceid>jstor_pubme</sourceid><recordid>TN_cdi_pubmed_primary_23530233</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><jstor_id>42590338</jstor_id><sourcerecordid>42590338</sourcerecordid><originalsourceid>FETCH-LOGICAL-c590t-ce75271542be2ed0af1e5b70c639e0105e5ae377d00a226b74ae66b7d6d1f5c33</originalsourceid><addsrcrecordid>eNqFkU2P0zAQhiMEYsvCmRMQiQuX7M54Yru5rIRWfEkrgQR7xXKSSesqsYudrtR_T0JLF7hwmoOfefR63ix7jnCBoOly6226QIEkqhIRHmQLhAoLVVbwMFsACF0sS1GeZU9S2gBAJZfwODsTJAkE0SL7_sUNBebbyInjHad8cGNo1sG30dk-H0LcrkMfVvu83ufOr13tRudXebv3dnC-iNzbkdtJEEZ2Psd8jNanPjR2dME_zR51tk_87DjPs9v3775dfyxuPn_4dP32pmhkBWPRsJZCoyxFzYJbsB2yrDU0iioGBMnSMmndAlghVK1Ly2oarWqxkw3ReXZ18G539cBtw36K0ZttdIONexOsM3-_eLc2q3BnSAlJEifBm6Mghh87TqMZXGq4763nsEsGl0BIBFr_HyWhsCQpqwl9_Q-6Cbvop0v8okqhBM7CywPVxJBS5O6UG8HMNZu5ZnNf87Tx8s_vnvjfvU7AqyMwb550s08aWak52osDsUljiCekFFMhRMt7Q2eDsavokrn9KgAVAJJSGugn4HPBgg</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1326426217</pqid></control><display><type>article</type><title>Pim-1 preserves mitochondrial morphology by inhibiting dynamin-related protein 1 translocation</title><source>Jstor Complete Legacy</source><source>MEDLINE</source><source>PubMed Central</source><source>Alma/SFX Local Collection</source><source>Free Full-Text Journals in Chemistry</source><creator>Din, Shabana ; Mason, Matthew ; Völkers, Mirko ; Johnson, Bevan ; Cottage, Christopher T. ; Wang, Zeping ; Joyo, Anya Y. ; Quijada, Pearl ; Erhardt, Peter ; Magnuson, Nancy S. ; Konstandin, Mathias H. ; Sussman, Mark A.</creator><creatorcontrib>Din, Shabana ; Mason, Matthew ; Völkers, Mirko ; Johnson, Bevan ; Cottage, Christopher T. ; Wang, Zeping ; Joyo, Anya Y. ; Quijada, Pearl ; Erhardt, Peter ; Magnuson, Nancy S. ; Konstandin, Mathias H. ; Sussman, Mark A.</creatorcontrib><description>Mitochondrial morphological dynamics affect the outcome of ischemic heart damage and pathogenesis. Recently, mitochondrial fission protein dynamin-related protein 1 (Drp1) has been identified as a mediator of mitochondrial morphological changes and cell death during cardiac ischemic injury. In this study, we report a unique relationship between Pim-1 activity and Drp1 regulation of mitochondrial morphology in cardiomyocytes challenged by ischemic stress. Transgenic hearts overexpressing cardiac Pim-1 display reduction of total Drp1 protein levels, increased phosphorylation of Drp1- S⁶³⁷, and inhibition of Drp1 localization to the mitochondria. Consistent with these findings, adenoviral-induced Pim-1 neonatal rat cardiomyocytes (NRCMs) retain a reticular mitochondrial phenotype after simulated ischemia (sI) and decreased Drp1 mitochondrial sequestration. Interestingly, adenovirus Pim-dominant negative NRCMs show increased expression of Bcl-2 homology 3 (BH3)-only protein p53 up-regulated modulator of apoptosis (PUMA), which has been previously shown to induce Drp1 accumulation at mitochondria and increase sensitivity to apoptotic stimuli. Overexpression of the p53 up-regulated modulator of apoptosis–dominant negative adenovirus attenuates localization of Drp1 to mitochondria in adenovirus Pim-dominant negative NRCMs promotes reticular mitochondrial morphology and inhibits cell death during sI. Therefore, Pim-1 activity prevents Drp1 compartmentalization to the mitochondria and preserves reticular mitochondrial morphology in response to sI.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.1213294110</identifier><identifier>PMID: 23530233</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Adenoviridae - genetics ; Adenoviruses ; Animals ; Apoptosis ; Biological Sciences ; cardiomyocytes ; Cardiovascular disease ; Cell death ; Dynamins - metabolism ; gene overexpression ; genetically modified organisms ; Heart ; Ischemia ; Mice ; Mice, Transgenic ; Mitochondria ; Mitochondria - metabolism ; Mitochondrial DNA ; Morphology ; Myocardium ; Myocytes, Cardiac - cytology ; Pathogenesis ; phenotype ; Phenotypes ; Phosphorylation ; preserves ; Protein Transport ; Proto-Oncogene Proteins c-pim-1 - metabolism ; Proto-Oncogene Proteins c-pim-1 - physiology ; Rats</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2013-04, Vol.110 (15), p.5969-5974</ispartof><rights>copyright © 1993-2008 National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences Apr 9, 2013</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c590t-ce75271542be2ed0af1e5b70c639e0105e5ae377d00a226b74ae66b7d6d1f5c33</citedby><cites>FETCH-LOGICAL-c590t-ce75271542be2ed0af1e5b70c639e0105e5ae377d00a226b74ae66b7d6d1f5c33</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/110/15.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/42590338$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/42590338$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27901,27902,53766,53768,57992,58225</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23530233$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Din, Shabana</creatorcontrib><creatorcontrib>Mason, Matthew</creatorcontrib><creatorcontrib>Völkers, Mirko</creatorcontrib><creatorcontrib>Johnson, Bevan</creatorcontrib><creatorcontrib>Cottage, Christopher T.</creatorcontrib><creatorcontrib>Wang, Zeping</creatorcontrib><creatorcontrib>Joyo, Anya Y.</creatorcontrib><creatorcontrib>Quijada, Pearl</creatorcontrib><creatorcontrib>Erhardt, Peter</creatorcontrib><creatorcontrib>Magnuson, Nancy S.</creatorcontrib><creatorcontrib>Konstandin, Mathias H.</creatorcontrib><creatorcontrib>Sussman, Mark A.</creatorcontrib><title>Pim-1 preserves mitochondrial morphology by inhibiting dynamin-related protein 1 translocation</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Mitochondrial morphological dynamics affect the outcome of ischemic heart damage and pathogenesis. Recently, mitochondrial fission protein dynamin-related protein 1 (Drp1) has been identified as a mediator of mitochondrial morphological changes and cell death during cardiac ischemic injury. In this study, we report a unique relationship between Pim-1 activity and Drp1 regulation of mitochondrial morphology in cardiomyocytes challenged by ischemic stress. Transgenic hearts overexpressing cardiac Pim-1 display reduction of total Drp1 protein levels, increased phosphorylation of Drp1- S⁶³⁷, and inhibition of Drp1 localization to the mitochondria. Consistent with these findings, adenoviral-induced Pim-1 neonatal rat cardiomyocytes (NRCMs) retain a reticular mitochondrial phenotype after simulated ischemia (sI) and decreased Drp1 mitochondrial sequestration. Interestingly, adenovirus Pim-dominant negative NRCMs show increased expression of Bcl-2 homology 3 (BH3)-only protein p53 up-regulated modulator of apoptosis (PUMA), which has been previously shown to induce Drp1 accumulation at mitochondria and increase sensitivity to apoptotic stimuli. Overexpression of the p53 up-regulated modulator of apoptosis–dominant negative adenovirus attenuates localization of Drp1 to mitochondria in adenovirus Pim-dominant negative NRCMs promotes reticular mitochondrial morphology and inhibits cell death during sI. Therefore, Pim-1 activity prevents Drp1 compartmentalization to the mitochondria and preserves reticular mitochondrial morphology in response to sI.</description><subject>Adenoviridae - genetics</subject><subject>Adenoviruses</subject><subject>Animals</subject><subject>Apoptosis</subject><subject>Biological Sciences</subject><subject>cardiomyocytes</subject><subject>Cardiovascular disease</subject><subject>Cell death</subject><subject>Dynamins - metabolism</subject><subject>gene overexpression</subject><subject>genetically modified organisms</subject><subject>Heart</subject><subject>Ischemia</subject><subject>Mice</subject><subject>Mice, Transgenic</subject><subject>Mitochondria</subject><subject>Mitochondria - metabolism</subject><subject>Mitochondrial DNA</subject><subject>Morphology</subject><subject>Myocardium</subject><subject>Myocytes, Cardiac - cytology</subject><subject>Pathogenesis</subject><subject>phenotype</subject><subject>Phenotypes</subject><subject>Phosphorylation</subject><subject>preserves</subject><subject>Protein Transport</subject><subject>Proto-Oncogene Proteins c-pim-1 - metabolism</subject><subject>Proto-Oncogene Proteins c-pim-1 - physiology</subject><subject>Rats</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU2P0zAQhiMEYsvCmRMQiQuX7M54Yru5rIRWfEkrgQR7xXKSSesqsYudrtR_T0JLF7hwmoOfefR63ix7jnCBoOly6226QIEkqhIRHmQLhAoLVVbwMFsACF0sS1GeZU9S2gBAJZfwODsTJAkE0SL7_sUNBebbyInjHad8cGNo1sG30dk-H0LcrkMfVvu83ufOr13tRudXebv3dnC-iNzbkdtJEEZ2Psd8jNanPjR2dME_zR51tk_87DjPs9v3775dfyxuPn_4dP32pmhkBWPRsJZCoyxFzYJbsB2yrDU0iioGBMnSMmndAlghVK1Ly2oarWqxkw3ReXZ18G539cBtw36K0ZttdIONexOsM3-_eLc2q3BnSAlJEifBm6Mghh87TqMZXGq4763nsEsGl0BIBFr_HyWhsCQpqwl9_Q-6Cbvop0v8okqhBM7CywPVxJBS5O6UG8HMNZu5ZnNf87Tx8s_vnvjfvU7AqyMwb550s08aWak52osDsUljiCekFFMhRMt7Q2eDsavokrn9KgAVAJJSGugn4HPBgg</recordid><startdate>20130409</startdate><enddate>20130409</enddate><creator>Din, Shabana</creator><creator>Mason, Matthew</creator><creator>Völkers, Mirko</creator><creator>Johnson, Bevan</creator><creator>Cottage, Christopher T.</creator><creator>Wang, Zeping</creator><creator>Joyo, Anya Y.</creator><creator>Quijada, Pearl</creator><creator>Erhardt, Peter</creator><creator>Magnuson, Nancy S.</creator><creator>Konstandin, Mathias H.</creator><creator>Sussman, Mark A.</creator><general>National Academy of Sciences</general><general>National Acad Sciences</general><scope>FBQ</scope><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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</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>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>7S9</scope><scope>L.6</scope><scope>5PM</scope></search><sort><creationdate>20130409</creationdate><title>Pim-1 preserves mitochondrial morphology by inhibiting dynamin-related protein 1 translocation</title><author>Din, Shabana ; Mason, Matthew ; Völkers, Mirko ; Johnson, Bevan ; Cottage, Christopher T. ; Wang, Zeping ; Joyo, Anya Y. ; Quijada, Pearl ; Erhardt, Peter ; Magnuson, Nancy S. ; Konstandin, Mathias H. ; Sussman, Mark A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c590t-ce75271542be2ed0af1e5b70c639e0105e5ae377d00a226b74ae66b7d6d1f5c33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Adenoviridae - genetics</topic><topic>Adenoviruses</topic><topic>Animals</topic><topic>Apoptosis</topic><topic>Biological Sciences</topic><topic>cardiomyocytes</topic><topic>Cardiovascular disease</topic><topic>Cell death</topic><topic>Dynamins - metabolism</topic><topic>gene overexpression</topic><topic>genetically modified organisms</topic><topic>Heart</topic><topic>Ischemia</topic><topic>Mice</topic><topic>Mice, Transgenic</topic><topic>Mitochondria</topic><topic>Mitochondria - metabolism</topic><topic>Mitochondrial DNA</topic><topic>Morphology</topic><topic>Myocardium</topic><topic>Myocytes, Cardiac - cytology</topic><topic>Pathogenesis</topic><topic>phenotype</topic><topic>Phenotypes</topic><topic>Phosphorylation</topic><topic>preserves</topic><topic>Protein Transport</topic><topic>Proto-Oncogene Proteins c-pim-1 - metabolism</topic><topic>Proto-Oncogene Proteins c-pim-1 - physiology</topic><topic>Rats</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Din, Shabana</creatorcontrib><creatorcontrib>Mason, Matthew</creatorcontrib><creatorcontrib>Völkers, Mirko</creatorcontrib><creatorcontrib>Johnson, Bevan</creatorcontrib><creatorcontrib>Cottage, Christopher T.</creatorcontrib><creatorcontrib>Wang, Zeping</creatorcontrib><creatorcontrib>Joyo, Anya Y.</creatorcontrib><creatorcontrib>Quijada, Pearl</creatorcontrib><creatorcontrib>Erhardt, Peter</creatorcontrib><creatorcontrib>Magnuson, Nancy S.</creatorcontrib><creatorcontrib>Konstandin, Mathias H.</creatorcontrib><creatorcontrib>Sussman, Mark A.</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>AGRICOLA</collection><collection>AGRICOLA - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Din, Shabana</au><au>Mason, Matthew</au><au>Völkers, Mirko</au><au>Johnson, Bevan</au><au>Cottage, Christopher T.</au><au>Wang, Zeping</au><au>Joyo, Anya Y.</au><au>Quijada, Pearl</au><au>Erhardt, Peter</au><au>Magnuson, Nancy S.</au><au>Konstandin, Mathias H.</au><au>Sussman, Mark A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Pim-1 preserves mitochondrial morphology by inhibiting dynamin-related protein 1 translocation</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2013-04-09</date><risdate>2013</risdate><volume>110</volume><issue>15</issue><spage>5969</spage><epage>5974</epage><pages>5969-5974</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>Mitochondrial morphological dynamics affect the outcome of ischemic heart damage and pathogenesis. Recently, mitochondrial fission protein dynamin-related protein 1 (Drp1) has been identified as a mediator of mitochondrial morphological changes and cell death during cardiac ischemic injury. In this study, we report a unique relationship between Pim-1 activity and Drp1 regulation of mitochondrial morphology in cardiomyocytes challenged by ischemic stress. Transgenic hearts overexpressing cardiac Pim-1 display reduction of total Drp1 protein levels, increased phosphorylation of Drp1- S⁶³⁷, and inhibition of Drp1 localization to the mitochondria. Consistent with these findings, adenoviral-induced Pim-1 neonatal rat cardiomyocytes (NRCMs) retain a reticular mitochondrial phenotype after simulated ischemia (sI) and decreased Drp1 mitochondrial sequestration. Interestingly, adenovirus Pim-dominant negative NRCMs show increased expression of Bcl-2 homology 3 (BH3)-only protein p53 up-regulated modulator of apoptosis (PUMA), which has been previously shown to induce Drp1 accumulation at mitochondria and increase sensitivity to apoptotic stimuli. Overexpression of the p53 up-regulated modulator of apoptosis–dominant negative adenovirus attenuates localization of Drp1 to mitochondria in adenovirus Pim-dominant negative NRCMs promotes reticular mitochondrial morphology and inhibits cell death during sI. Therefore, Pim-1 activity prevents Drp1 compartmentalization to the mitochondria and preserves reticular mitochondrial morphology in response to sI.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>23530233</pmid><doi>10.1073/pnas.1213294110</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0027-8424 |
| ispartof | Proceedings of the National Academy of Sciences - PNAS, 2013-04, Vol.110 (15), p.5969-5974 |
| issn | 0027-8424 1091-6490 |
| language | eng |
| recordid | cdi_pubmed_primary_23530233 |
| source | Jstor Complete Legacy; MEDLINE; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Adenoviridae - genetics Adenoviruses Animals Apoptosis Biological Sciences cardiomyocytes Cardiovascular disease Cell death Dynamins - metabolism gene overexpression genetically modified organisms Heart Ischemia Mice Mice, Transgenic Mitochondria Mitochondria - metabolism Mitochondrial DNA Morphology Myocardium Myocytes, Cardiac - cytology Pathogenesis phenotype Phenotypes Phosphorylation preserves Protein Transport Proto-Oncogene Proteins c-pim-1 - metabolism Proto-Oncogene Proteins c-pim-1 - physiology Rats |
| title | Pim-1 preserves mitochondrial morphology by inhibiting dynamin-related protein 1 translocation |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-02T14%3A08%3A09IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-jstor_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Pim-1%20preserves%20mitochondrial%20morphology%20by%20inhibiting%20dynamin-related%20protein%201%20translocation&rft.jtitle=Proceedings%20of%20the%20National%20Academy%20of%20Sciences%20-%20PNAS&rft.au=Din,%20Shabana&rft.date=2013-04-09&rft.volume=110&rft.issue=15&rft.spage=5969&rft.epage=5974&rft.pages=5969-5974&rft.issn=0027-8424&rft.eissn=1091-6490&rft_id=info:doi/10.1073/pnas.1213294110&rft_dat=%3Cjstor_pubme%3E42590338%3C/jstor_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1326426217&rft_id=info:pmid/23530233&rft_jstor_id=42590338&rfr_iscdi=true |