Proteomics analysis of the non-muscle myosin heavy chain IIa-enriched actin-myosin complex reveals multiple functions within the podocyte
MYH9 encodes non-muscle myosin heavy chain IIA (NMMHCIIA), the predominant force-generating ATPase in non-muscle cells. Several lines of evidence implicate a role for MYH9 in podocytopathies. However, NMMHCIIA's function in podocytes remains unknown. To better understand this function, we perfo...
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| Veröffentlicht in: | PloS one 2014-06, Vol.9 (6), p.e100660-e100660 |
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| creator | Hays, Thomas Ma'ayan, Avi Clark, Neil R Tan, Christopher M Teixeira, Avelino Teixeira, Angela Choi, Jae W Burdis, Nora Jung, Sung Yun Bajaj, Amol O O'Malley, Bert W He, John C Hyink, Deborah P Klotman, Paul E |
| description | MYH9 encodes non-muscle myosin heavy chain IIA (NMMHCIIA), the predominant force-generating ATPase in non-muscle cells. Several lines of evidence implicate a role for MYH9 in podocytopathies. However, NMMHCIIA's function in podocytes remains unknown. To better understand this function, we performed immuno-precipitation followed by mass-spectrometry proteomics to identify proteins interacting with the NMMHCIIA-enriched actin-myosin complexes. Computational analyses revealed that these proteins belong to functional networks including regulators of cytoskeletal organization, metabolism and networks regulated by the HIV-1 gene nef. We further characterized the subcellular localization of NMMHCIIA within podocytes in vivo, and found it to be present within the podocyte major foot processes. Finally, we tested the effect of loss of MYH9 expression in podocytes in vitro, and found that it was necessary for cytoskeletal organization. Our results provide the first survey of NMMHCIIA-enriched actin-myosin-interacting proteins within the podocyte, demonstrating the important role of NMMHCIIA in organizing the elaborate cytoskeleton structure of podocytes. Our characterization of NMMHCIIA's functions goes beyond the podocyte, providing important insights into its general molecular role. |
| doi_str_mv | 10.1371/journal.pone.0100660 |
| format | Article |
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Several lines of evidence implicate a role for MYH9 in podocytopathies. However, NMMHCIIA's function in podocytes remains unknown. To better understand this function, we performed immuno-precipitation followed by mass-spectrometry proteomics to identify proteins interacting with the NMMHCIIA-enriched actin-myosin complexes. Computational analyses revealed that these proteins belong to functional networks including regulators of cytoskeletal organization, metabolism and networks regulated by the HIV-1 gene nef. We further characterized the subcellular localization of NMMHCIIA within podocytes in vivo, and found it to be present within the podocyte major foot processes. Finally, we tested the effect of loss of MYH9 expression in podocytes in vitro, and found that it was necessary for cytoskeletal organization. Our results provide the first survey of NMMHCIIA-enriched actin-myosin-interacting proteins within the podocyte, demonstrating the important role of NMMHCIIA in organizing the elaborate cytoskeleton structure of podocytes. Our characterization of NMMHCIIA's functions goes beyond the podocyte, providing important insights into its general molecular role.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0100660</identifier><identifier>PMID: 24949636</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Acids ; Actin ; Actins - biosynthesis ; Actins - metabolism ; Adenosine triphosphatase ; Animals ; Bioinformatics ; Biology and Life Sciences ; Cell adhesion & migration ; Cellular biology ; Chains ; Computer applications ; Cytoskeletal Proteins - biosynthesis ; Cytoskeletal Proteins - metabolism ; Cytoskeleton ; Enrichment ; Gene Expression Regulation ; Genes ; HIV ; Human immunodeficiency virus ; Humans ; Kidney diseases ; Localization ; Medicine ; Medicine and Health Sciences ; Membrane Proteins - biosynthesis ; Membrane Proteins - metabolism ; Metabolism ; Mice ; Molecular Motor Proteins - biosynthesis ; Molecular Motor Proteins - metabolism ; Multiprotein Complexes - metabolism ; Muscles ; Mutation ; Myosin ; Myosin Heavy Chains - biosynthesis ; Myosin Heavy Chains - metabolism ; nef Gene Products, Human Immunodeficiency Virus - metabolism ; Nef protein ; Pharmacology ; Podocytes - metabolism ; Protein Interaction Maps ; Proteins ; Proteomics ; Regulators ; Spectrometry ; Structural analysis ; Transgenic animals</subject><ispartof>PloS one, 2014-06, Vol.9 (6), p.e100660-e100660</ispartof><rights>2014 Hays et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2014 Hays et al 2014 Hays et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c592t-9d6b765220533e4770f884e0a4fbe899dbf6909d5a581f26618880f3db9a9b543</citedby><cites>FETCH-LOGICAL-c592t-9d6b765220533e4770f884e0a4fbe899dbf6909d5a581f26618880f3db9a9b543</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4065073/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4065073/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,2096,2915,23845,27901,27902,53766,53768,79342,79343</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24949636$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hays, Thomas</creatorcontrib><creatorcontrib>Ma'ayan, Avi</creatorcontrib><creatorcontrib>Clark, Neil R</creatorcontrib><creatorcontrib>Tan, Christopher M</creatorcontrib><creatorcontrib>Teixeira, Avelino</creatorcontrib><creatorcontrib>Teixeira, Angela</creatorcontrib><creatorcontrib>Choi, Jae W</creatorcontrib><creatorcontrib>Burdis, Nora</creatorcontrib><creatorcontrib>Jung, Sung Yun</creatorcontrib><creatorcontrib>Bajaj, Amol O</creatorcontrib><creatorcontrib>O'Malley, Bert W</creatorcontrib><creatorcontrib>He, John C</creatorcontrib><creatorcontrib>Hyink, Deborah P</creatorcontrib><creatorcontrib>Klotman, Paul E</creatorcontrib><title>Proteomics analysis of the non-muscle myosin heavy chain IIa-enriched actin-myosin complex reveals multiple functions within the podocyte</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>MYH9 encodes non-muscle myosin heavy chain IIA (NMMHCIIA), the predominant force-generating ATPase in non-muscle cells. 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Our results provide the first survey of NMMHCIIA-enriched actin-myosin-interacting proteins within the podocyte, demonstrating the important role of NMMHCIIA in organizing the elaborate cytoskeleton structure of podocytes. Our characterization of NMMHCIIA's functions goes beyond the podocyte, providing important insights into its general molecular role.</description><subject>Acids</subject><subject>Actin</subject><subject>Actins - biosynthesis</subject><subject>Actins - metabolism</subject><subject>Adenosine triphosphatase</subject><subject>Animals</subject><subject>Bioinformatics</subject><subject>Biology and Life Sciences</subject><subject>Cell adhesion & migration</subject><subject>Cellular biology</subject><subject>Chains</subject><subject>Computer applications</subject><subject>Cytoskeletal Proteins - biosynthesis</subject><subject>Cytoskeletal Proteins - metabolism</subject><subject>Cytoskeleton</subject><subject>Enrichment</subject><subject>Gene Expression Regulation</subject><subject>Genes</subject><subject>HIV</subject><subject>Human immunodeficiency virus</subject><subject>Humans</subject><subject>Kidney diseases</subject><subject>Localization</subject><subject>Medicine</subject><subject>Medicine and Health Sciences</subject><subject>Membrane Proteins - 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Several lines of evidence implicate a role for MYH9 in podocytopathies. However, NMMHCIIA's function in podocytes remains unknown. To better understand this function, we performed immuno-precipitation followed by mass-spectrometry proteomics to identify proteins interacting with the NMMHCIIA-enriched actin-myosin complexes. Computational analyses revealed that these proteins belong to functional networks including regulators of cytoskeletal organization, metabolism and networks regulated by the HIV-1 gene nef. We further characterized the subcellular localization of NMMHCIIA within podocytes in vivo, and found it to be present within the podocyte major foot processes. Finally, we tested the effect of loss of MYH9 expression in podocytes in vitro, and found that it was necessary for cytoskeletal organization. Our results provide the first survey of NMMHCIIA-enriched actin-myosin-interacting proteins within the podocyte, demonstrating the important role of NMMHCIIA in organizing the elaborate cytoskeleton structure of podocytes. Our characterization of NMMHCIIA's functions goes beyond the podocyte, providing important insights into its general molecular role.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>24949636</pmid><doi>10.1371/journal.pone.0100660</doi><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 1932-6203 |
| ispartof | PloS one, 2014-06, Vol.9 (6), p.e100660-e100660 |
| issn | 1932-6203 1932-6203 |
| language | eng |
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| source | MEDLINE; DOAJ Directory of Open Access Journals; EZB-FREE-00999 freely available EZB journals; PubMed Central; Free Full-Text Journals in Chemistry; Public Library of Science (PLoS) |
| subjects | Acids Actin Actins - biosynthesis Actins - metabolism Adenosine triphosphatase Animals Bioinformatics Biology and Life Sciences Cell adhesion & migration Cellular biology Chains Computer applications Cytoskeletal Proteins - biosynthesis Cytoskeletal Proteins - metabolism Cytoskeleton Enrichment Gene Expression Regulation Genes HIV Human immunodeficiency virus Humans Kidney diseases Localization Medicine Medicine and Health Sciences Membrane Proteins - biosynthesis Membrane Proteins - metabolism Metabolism Mice Molecular Motor Proteins - biosynthesis Molecular Motor Proteins - metabolism Multiprotein Complexes - metabolism Muscles Mutation Myosin Myosin Heavy Chains - biosynthesis Myosin Heavy Chains - metabolism nef Gene Products, Human Immunodeficiency Virus - metabolism Nef protein Pharmacology Podocytes - metabolism Protein Interaction Maps Proteins Proteomics Regulators Spectrometry Structural analysis Transgenic animals |
| title | Proteomics analysis of the non-muscle myosin heavy chain IIa-enriched actin-myosin complex reveals multiple functions within the podocyte |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-08T09%3A13%3A15IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_plos_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Proteomics%20analysis%20of%20the%20non-muscle%20myosin%20heavy%20chain%20IIa-enriched%20actin-myosin%20complex%20reveals%20multiple%20functions%20within%20the%20podocyte&rft.jtitle=PloS%20one&rft.au=Hays,%20Thomas&rft.date=2014-06-20&rft.volume=9&rft.issue=6&rft.spage=e100660&rft.epage=e100660&rft.pages=e100660-e100660&rft.issn=1932-6203&rft.eissn=1932-6203&rft_id=info:doi/10.1371/journal.pone.0100660&rft_dat=%3Cproquest_plos_%3E3341902851%3C/proquest_plos_%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1538589033&rft_id=info:pmid/24949636&rft_doaj_id=oai_doaj_org_article_d884dc3c91e144a4801a86ba899f17b5&rfr_iscdi=true |