Protein N-myristoylation plays a critical role in the endoplasmic reticulum morphological change induced by overexpression of protein Lunapark, an integral membrane protein of the endoplasmic reticulum
N-myristoylation of eukaryotic cellular proteins has been recognized as a modification that occurs mainly on cytoplasmic proteins. In this study, we examined the membrane localization, membrane integration, and intracellular localization of four recently identified human N-myristoylated proteins wit...
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| Veröffentlicht in: | PloS one 2013-11, Vol.8 (11), p.e78235-e78235 |
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| creator | Moriya, Koko Nagatoshi, Kei Noriyasu, Yoshimi Okamura, Tsuyoshi Takamitsu, Emi Suzuki, Takashi Utsumi, Toshihiko |
| description | N-myristoylation of eukaryotic cellular proteins has been recognized as a modification that occurs mainly on cytoplasmic proteins. In this study, we examined the membrane localization, membrane integration, and intracellular localization of four recently identified human N-myristoylated proteins with predicted transmembrane domains. As a result, it was found that protein Lunapark, the human ortholog of yeast protein Lnp1p that has recently been found to be involved in network formation of the endoplasmic reticulum (ER), is an N-myristoylated polytopic integral membrane protein. Analysis of tumor necrosis factor-fusion proteins with each of the two putative transmembrane domains and their flanking regions of protein Lunapark revealed that transmembrane domain 1 and 2 functioned as type II signal anchor sequence and stop transfer sequence, respectively, and together generated a double-spanning integral membrane protein with an N-/C-terminal cytoplasmic orientation. Immunofluorescence staining of HEK293T cells transfected with a cDNA encoding protein Lunapark tagged with FLAG-tag at its C-terminus revealed that overexpressed protein Lunapark localized mainly to the peripheral ER and induced the formation of large polygonal tubular structures. Morphological changes in the ER induced by overexpressed protein Lunapark were significantly inhibited by the inhibition of protein N-myristoylation by means of replacing Gly2 with Ala. These results indicated that protein N-myristoylation plays a critical role in the ER morphological change induced by overexpression of protein Lunapark. |
| doi_str_mv | 10.1371/journal.pone.0078235 |
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Gisou</contributor><creatorcontrib>Moriya, Koko ; Nagatoshi, Kei ; Noriyasu, Yoshimi ; Okamura, Tsuyoshi ; Takamitsu, Emi ; Suzuki, Takashi ; Utsumi, Toshihiko ; van der Goot, F. Gisou</creatorcontrib><description>N-myristoylation of eukaryotic cellular proteins has been recognized as a modification that occurs mainly on cytoplasmic proteins. In this study, we examined the membrane localization, membrane integration, and intracellular localization of four recently identified human N-myristoylated proteins with predicted transmembrane domains. As a result, it was found that protein Lunapark, the human ortholog of yeast protein Lnp1p that has recently been found to be involved in network formation of the endoplasmic reticulum (ER), is an N-myristoylated polytopic integral membrane protein. Analysis of tumor necrosis factor-fusion proteins with each of the two putative transmembrane domains and their flanking regions of protein Lunapark revealed that transmembrane domain 1 and 2 functioned as type II signal anchor sequence and stop transfer sequence, respectively, and together generated a double-spanning integral membrane protein with an N-/C-terminal cytoplasmic orientation. Immunofluorescence staining of HEK293T cells transfected with a cDNA encoding protein Lunapark tagged with FLAG-tag at its C-terminus revealed that overexpressed protein Lunapark localized mainly to the peripheral ER and induced the formation of large polygonal tubular structures. Morphological changes in the ER induced by overexpressed protein Lunapark were significantly inhibited by the inhibition of protein N-myristoylation by means of replacing Gly2 with Ala. These results indicated that protein N-myristoylation plays a critical role in the ER morphological change induced by overexpression of protein Lunapark.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0078235</identifier><identifier>PMID: 24223779</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Amino Acid Sequence ; Analysis ; Animals ; Aquaporins ; C-Terminus ; Cellular proteins ; DNA, Complementary - genetics ; DNA, Complementary - metabolism ; Endoplasmic reticulum ; Endoplasmic Reticulum - genetics ; Endoplasmic Reticulum - metabolism ; Gene Expression Regulation ; Genetic Vectors ; HEK293 Cells ; Homeodomain Proteins - genetics ; Homeodomain Proteins - metabolism ; Humans ; Immunofluorescence ; Integral membrane proteins ; Integrals ; Localization ; Medicine ; Membrane proteins ; Membrane Proteins - genetics ; Membrane Proteins - metabolism ; Membranes ; Mitochondria ; Molecular Sequence Data ; Morphology ; Myristic Acid - metabolism ; Myristoylation ; Network formation ; Physiology ; Protein Processing, Post-Translational ; Protein synthesis ; Proteins ; Sequence Alignment ; Sequence Homology, Amino Acid ; Signal Transduction ; Transfection ; Transmembrane domains ; Tumor necrosis factor ; Yeast ; Yeasts ; Zinc Fingers - genetics</subject><ispartof>PloS one, 2013-11, Vol.8 (11), p.e78235-e78235</ispartof><rights>COPYRIGHT 2013 Public Library of Science</rights><rights>2013 Moriya et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: https://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. 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Gisou</contributor><creatorcontrib>Moriya, Koko</creatorcontrib><creatorcontrib>Nagatoshi, Kei</creatorcontrib><creatorcontrib>Noriyasu, Yoshimi</creatorcontrib><creatorcontrib>Okamura, Tsuyoshi</creatorcontrib><creatorcontrib>Takamitsu, Emi</creatorcontrib><creatorcontrib>Suzuki, Takashi</creatorcontrib><creatorcontrib>Utsumi, Toshihiko</creatorcontrib><title>Protein N-myristoylation plays a critical role in the endoplasmic reticulum morphological change induced by overexpression of protein Lunapark, an integral membrane protein of the endoplasmic reticulum</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>N-myristoylation of eukaryotic cellular proteins has been recognized as a modification that occurs mainly on cytoplasmic proteins. In this study, we examined the membrane localization, membrane integration, and intracellular localization of four recently identified human N-myristoylated proteins with predicted transmembrane domains. 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These results indicated that protein N-myristoylation plays a critical role in the ER morphological change induced by overexpression of protein Lunapark.</description><subject>Amino Acid Sequence</subject><subject>Analysis</subject><subject>Animals</subject><subject>Aquaporins</subject><subject>C-Terminus</subject><subject>Cellular proteins</subject><subject>DNA, Complementary - genetics</subject><subject>DNA, Complementary - metabolism</subject><subject>Endoplasmic reticulum</subject><subject>Endoplasmic Reticulum - genetics</subject><subject>Endoplasmic Reticulum - metabolism</subject><subject>Gene Expression Regulation</subject><subject>Genetic Vectors</subject><subject>HEK293 Cells</subject><subject>Homeodomain Proteins - genetics</subject><subject>Homeodomain Proteins - metabolism</subject><subject>Humans</subject><subject>Immunofluorescence</subject><subject>Integral membrane proteins</subject><subject>Integrals</subject><subject>Localization</subject><subject>Medicine</subject><subject>Membrane proteins</subject><subject>Membrane Proteins - 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Gisou</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Protein N-myristoylation plays a critical role in the endoplasmic reticulum morphological change induced by overexpression of protein Lunapark, an integral membrane protein of the endoplasmic reticulum</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2013-11-04</date><risdate>2013</risdate><volume>8</volume><issue>11</issue><spage>e78235</spage><epage>e78235</epage><pages>e78235-e78235</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>N-myristoylation of eukaryotic cellular proteins has been recognized as a modification that occurs mainly on cytoplasmic proteins. In this study, we examined the membrane localization, membrane integration, and intracellular localization of four recently identified human N-myristoylated proteins with predicted transmembrane domains. As a result, it was found that protein Lunapark, the human ortholog of yeast protein Lnp1p that has recently been found to be involved in network formation of the endoplasmic reticulum (ER), is an N-myristoylated polytopic integral membrane protein. Analysis of tumor necrosis factor-fusion proteins with each of the two putative transmembrane domains and their flanking regions of protein Lunapark revealed that transmembrane domain 1 and 2 functioned as type II signal anchor sequence and stop transfer sequence, respectively, and together generated a double-spanning integral membrane protein with an N-/C-terminal cytoplasmic orientation. Immunofluorescence staining of HEK293T cells transfected with a cDNA encoding protein Lunapark tagged with FLAG-tag at its C-terminus revealed that overexpressed protein Lunapark localized mainly to the peripheral ER and induced the formation of large polygonal tubular structures. Morphological changes in the ER induced by overexpressed protein Lunapark were significantly inhibited by the inhibition of protein N-myristoylation by means of replacing Gly2 with Ala. These results indicated that protein N-myristoylation plays a critical role in the ER morphological change induced by overexpression of protein Lunapark.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>24223779</pmid><doi>10.1371/journal.pone.0078235</doi><tpages>e78235</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 1932-6203 |
| ispartof | PloS one, 2013-11, Vol.8 (11), p.e78235-e78235 |
| issn | 1932-6203 1932-6203 |
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| recordid | cdi_plos_journals_1448416185 |
| source | MEDLINE; DOAJ Directory of Open Access Journals; Public Library of Science (PLoS); EZB-FREE-00999 freely available EZB journals; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Amino Acid Sequence Analysis Animals Aquaporins C-Terminus Cellular proteins DNA, Complementary - genetics DNA, Complementary - metabolism Endoplasmic reticulum Endoplasmic Reticulum - genetics Endoplasmic Reticulum - metabolism Gene Expression Regulation Genetic Vectors HEK293 Cells Homeodomain Proteins - genetics Homeodomain Proteins - metabolism Humans Immunofluorescence Integral membrane proteins Integrals Localization Medicine Membrane proteins Membrane Proteins - genetics Membrane Proteins - metabolism Membranes Mitochondria Molecular Sequence Data Morphology Myristic Acid - metabolism Myristoylation Network formation Physiology Protein Processing, Post-Translational Protein synthesis Proteins Sequence Alignment Sequence Homology, Amino Acid Signal Transduction Transfection Transmembrane domains Tumor necrosis factor Yeast Yeasts Zinc Fingers - genetics |
| title | Protein N-myristoylation plays a critical role in the endoplasmic reticulum morphological change induced by overexpression of protein Lunapark, an integral membrane protein of the endoplasmic reticulum |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-06T07%3A20%3A40IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_plos_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Protein%20N-myristoylation%20plays%20a%20critical%20role%20in%20the%20endoplasmic%20reticulum%20morphological%20change%20induced%20by%20overexpression%20of%20protein%20Lunapark,%20an%20integral%20membrane%20protein%20of%20the%20endoplasmic%20reticulum&rft.jtitle=PloS%20one&rft.au=Moriya,%20Koko&rft.date=2013-11-04&rft.volume=8&rft.issue=11&rft.spage=e78235&rft.epage=e78235&rft.pages=e78235-e78235&rft.issn=1932-6203&rft.eissn=1932-6203&rft_id=info:doi/10.1371/journal.pone.0078235&rft_dat=%3Cgale_plos_%3EA478425970%3C/gale_plos_%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1448416185&rft_id=info:pmid/24223779&rft_galeid=A478425970&rft_doaj_id=oai_doaj_org_article_850fcb816d2346e2a4345dd7f3257404&rfr_iscdi=true |