SERCA1 Truncated Proteins Unable to Pump Calcium Reduce the Endoplasmic Reticulum Calcium Concentration and Induce Apoptosis
By pumping calcium from the cytosol to the ER, sarco/endoplasmic reticulum calcium ATPases (SERCAs) play a major role in the control of calcium signaling. We describe two SERCA1 splice variants (S1Ts) characterized by exon 4 and/or exon 11 splicing, encoding COOH terminally truncated proteins, havin...
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| Veröffentlicht in: | The Journal of cell biology 2001-06, Vol.153 (6), p.1301-1313 |
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| container_title | The Journal of cell biology |
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| creator | Chami, Mounia Gozuacik, Devrim Lagorce, David Brini, Marisa Falson, Pierre Peaucellier, Gérard Pinton, Paolo Lecoeur, Hervé Gougeon, Marie-Lyse le Maire, Marc Rizzuto, Rosario Bréchot, Christian Paterlini-Bréchot, Patrizia |
| description | By pumping calcium from the cytosol to the ER, sarco/endoplasmic reticulum calcium ATPases (SERCAs) play a major role in the control of calcium signaling. We describe two SERCA1 splice variants (S1Ts) characterized by exon 4 and/or exon 11 splicing, encoding COOH terminally truncated proteins, having only one of the seven calcium-binding residues, and thus unable to pump calcium. As shown by semiquantitative RT-PCR, S1T transcripts are differentially expressed in several adult and fetal human tissues, but not in skeletal muscle and heart. S1T proteins expression was detected by Western blot in nontransfected cell lines. In transiently transfected cells, S1T homodimers were revealed by Western blot using mildly denaturing conditions. S1T proteins were shown, by confocal scanning microscopy, to colocalize with endogenous SERCA2b into the ER membrane. Using ER-targeted aequorin (erAEQ), we have found that S1T proteins reduce ER calcium and reverse elevation of ER calcium loading induced by SERCA1 and SERCA2b. Our results also show that SERCA1 variants increase ER calcium leakage and are consistent with the hypothesis of a cation channel formed by S1T homodimers. Finally, when overexpressed in liver-derived cells, S1T proteins significantly induce apoptosis. These data reveal a further mechanism modulating Ca2+accumulation into the ER of nonmuscle cells and highlight the relevance of S1T proteins to the control of apoptosis. |
| doi_str_mv | 10.1083/jcb.153.6.1301 |
| format | Article |
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We describe two SERCA1 splice variants (S1Ts) characterized by exon 4 and/or exon 11 splicing, encoding COOH terminally truncated proteins, having only one of the seven calcium-binding residues, and thus unable to pump calcium. As shown by semiquantitative RT-PCR, S1T transcripts are differentially expressed in several adult and fetal human tissues, but not in skeletal muscle and heart. S1T proteins expression was detected by Western blot in nontransfected cell lines. In transiently transfected cells, S1T homodimers were revealed by Western blot using mildly denaturing conditions. S1T proteins were shown, by confocal scanning microscopy, to colocalize with endogenous SERCA2b into the ER membrane. Using ER-targeted aequorin (erAEQ), we have found that S1T proteins reduce ER calcium and reverse elevation of ER calcium loading induced by SERCA1 and SERCA2b. Our results also show that SERCA1 variants increase ER calcium leakage and are consistent with the hypothesis of a cation channel formed by S1T homodimers. Finally, when overexpressed in liver-derived cells, S1T proteins significantly induce apoptosis. These data reveal a further mechanism modulating Ca2+accumulation into the ER of nonmuscle cells and highlight the relevance of S1T proteins to the control of apoptosis.</description><identifier>ISSN: 0021-9525</identifier><identifier>EISSN: 1540-8140</identifier><identifier>DOI: 10.1083/jcb.153.6.1301</identifier><identifier>PMID: 11402072</identifier><identifier>CODEN: JCLBA3</identifier><language>eng</language><publisher>United States: Rockefeller University Press</publisher><subject>Adult ; Amino Acid Sequence ; Antibodies ; Apoptosis ; Biochemistry, Molecular Biology ; Calcium ; Calcium - metabolism ; Calcium-Transporting ATPases - chemistry ; Calcium-Transporting ATPases - genetics ; Calcium-Transporting ATPases - metabolism ; Cell lines ; Cellular biology ; Cloning, Molecular ; Dimerization ; Endoplasmic Reticulum - metabolism ; Exons ; Gene Expression ; HeLa Cells ; Humans ; Intracellular Membranes - metabolism ; Life Sciences ; Liver ; Molecular Sequence Data ; Original ; P values ; Protein Isoforms - chemistry ; Protein Isoforms - genetics ; Protein Isoforms - metabolism ; Protein Structure, Secondary ; Proteins ; Pumps ; RNA Splicing ; Sarcoplasmic Reticulum Calcium-Transporting ATPases ; Splicing ; Tissue Distribution ; Transfection ; Tumor Cells, Cultured</subject><ispartof>The Journal of cell biology, 2001-06, Vol.153 (6), p.1301-1313</ispartof><rights>Copyright 2001 The Rockefeller University Press</rights><rights>Copyright Rockefeller University Press Jun 11, 2001</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><rights>2001 The Rockefeller University Press 2001 The Rockefeller University Press</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c470t-c487553f069288cac659b22dd2612c1eab3d6a120fb20cc76c395569b2d5ce733</citedby><cites>FETCH-LOGICAL-c470t-c487553f069288cac659b22dd2612c1eab3d6a120fb20cc76c395569b2d5ce733</cites><orcidid>0000-0002-9760-4577 ; 0000-0003-1498-7187</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,776,780,881,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11402072$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-00314165$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Chami, Mounia</creatorcontrib><creatorcontrib>Gozuacik, Devrim</creatorcontrib><creatorcontrib>Lagorce, David</creatorcontrib><creatorcontrib>Brini, Marisa</creatorcontrib><creatorcontrib>Falson, Pierre</creatorcontrib><creatorcontrib>Peaucellier, Gérard</creatorcontrib><creatorcontrib>Pinton, Paolo</creatorcontrib><creatorcontrib>Lecoeur, Hervé</creatorcontrib><creatorcontrib>Gougeon, Marie-Lyse</creatorcontrib><creatorcontrib>le Maire, Marc</creatorcontrib><creatorcontrib>Rizzuto, Rosario</creatorcontrib><creatorcontrib>Bréchot, Christian</creatorcontrib><creatorcontrib>Paterlini-Bréchot, Patrizia</creatorcontrib><title>SERCA1 Truncated Proteins Unable to Pump Calcium Reduce the Endoplasmic Reticulum Calcium Concentration and Induce Apoptosis</title><title>The Journal of cell biology</title><addtitle>J Cell Biol</addtitle><description>By pumping calcium from the cytosol to the ER, sarco/endoplasmic reticulum calcium ATPases (SERCAs) play a major role in the control of calcium signaling. We describe two SERCA1 splice variants (S1Ts) characterized by exon 4 and/or exon 11 splicing, encoding COOH terminally truncated proteins, having only one of the seven calcium-binding residues, and thus unable to pump calcium. As shown by semiquantitative RT-PCR, S1T transcripts are differentially expressed in several adult and fetal human tissues, but not in skeletal muscle and heart. S1T proteins expression was detected by Western blot in nontransfected cell lines. In transiently transfected cells, S1T homodimers were revealed by Western blot using mildly denaturing conditions. S1T proteins were shown, by confocal scanning microscopy, to colocalize with endogenous SERCA2b into the ER membrane. Using ER-targeted aequorin (erAEQ), we have found that S1T proteins reduce ER calcium and reverse elevation of ER calcium loading induced by SERCA1 and SERCA2b. Our results also show that SERCA1 variants increase ER calcium leakage and are consistent with the hypothesis of a cation channel formed by S1T homodimers. Finally, when overexpressed in liver-derived cells, S1T proteins significantly induce apoptosis. These data reveal a further mechanism modulating Ca2+accumulation into the ER of nonmuscle cells and highlight the relevance of S1T proteins to the control of apoptosis.</description><subject>Adult</subject><subject>Amino Acid Sequence</subject><subject>Antibodies</subject><subject>Apoptosis</subject><subject>Biochemistry, Molecular Biology</subject><subject>Calcium</subject><subject>Calcium - metabolism</subject><subject>Calcium-Transporting ATPases - chemistry</subject><subject>Calcium-Transporting ATPases - genetics</subject><subject>Calcium-Transporting ATPases - metabolism</subject><subject>Cell lines</subject><subject>Cellular biology</subject><subject>Cloning, Molecular</subject><subject>Dimerization</subject><subject>Endoplasmic Reticulum - metabolism</subject><subject>Exons</subject><subject>Gene Expression</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>Intracellular Membranes - metabolism</subject><subject>Life Sciences</subject><subject>Liver</subject><subject>Molecular Sequence Data</subject><subject>Original</subject><subject>P values</subject><subject>Protein Isoforms - chemistry</subject><subject>Protein Isoforms - genetics</subject><subject>Protein Isoforms - metabolism</subject><subject>Protein Structure, Secondary</subject><subject>Proteins</subject><subject>Pumps</subject><subject>RNA Splicing</subject><subject>Sarcoplasmic Reticulum Calcium-Transporting ATPases</subject><subject>Splicing</subject><subject>Tissue Distribution</subject><subject>Transfection</subject><subject>Tumor Cells, Cultured</subject><issn>0021-9525</issn><issn>1540-8140</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdks9rFDEUx4Modq1ePYkED4KHXV-SSWbmUliG1RYWLLU9h0wm62aZScYkUxD84806q9VeEvi-z3vf_Pgi9JrAikDFPh50uyKcrcSKMCBP0ILwApYVKeApWgBQsqw55WfoRYwHACjKgj1HZyTXKZR0gX5-3dw0a4Jvw-S0SqbD18EnY13Ed061vcHJ4-tpGHGjem2nAd-YbtJZ3hu8cZ0fexUHq7OcrJ76DPwBG--0cSmoZL3DynX4yv1uXY9-TD7a-BI926k-mlen_RzdfdrcNpfL7ZfPV816u9RFCSmvVck524GoaVVppQWvW0q7jgpCNTGqZZ1QhMKupaB1KTSrOReZ6bg2JWPn6GKeO07tYLr5VL0cgx1U-CG9svL_irN7-c3fS0pqCoznAR_mAftHbZfrrTxqAIwURPB7ktn3J7Pgv08mJjnYqE3fK2f8FGUJNakqKDP47hF48FNw-SGyb6ZYWVcZWs2QDj7GYHZ_7QnIYwJkToDMCZBCHhOQG97-e9cH_PTlGXgzA4eYfHioCwqCEvYL3iW14A</recordid><startdate>20010611</startdate><enddate>20010611</enddate><creator>Chami, Mounia</creator><creator>Gozuacik, Devrim</creator><creator>Lagorce, David</creator><creator>Brini, Marisa</creator><creator>Falson, Pierre</creator><creator>Peaucellier, Gérard</creator><creator>Pinton, Paolo</creator><creator>Lecoeur, Hervé</creator><creator>Gougeon, Marie-Lyse</creator><creator>le Maire, Marc</creator><creator>Rizzuto, Rosario</creator><creator>Bréchot, Christian</creator><creator>Paterlini-Bréchot, Patrizia</creator><general>Rockefeller University Press</general><general>The Rockefeller University Press</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>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</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>1XC</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-9760-4577</orcidid><orcidid>https://orcid.org/0000-0003-1498-7187</orcidid></search><sort><creationdate>20010611</creationdate><title>SERCA1 Truncated Proteins Unable to Pump Calcium Reduce the Endoplasmic Reticulum Calcium Concentration and Induce Apoptosis</title><author>Chami, Mounia ; Gozuacik, Devrim ; Lagorce, David ; Brini, Marisa ; Falson, Pierre ; Peaucellier, Gérard ; Pinton, Paolo ; Lecoeur, Hervé ; Gougeon, Marie-Lyse ; le Maire, Marc ; Rizzuto, Rosario ; Bréchot, Christian ; Paterlini-Bréchot, Patrizia</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c470t-c487553f069288cac659b22dd2612c1eab3d6a120fb20cc76c395569b2d5ce733</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Adult</topic><topic>Amino Acid Sequence</topic><topic>Antibodies</topic><topic>Apoptosis</topic><topic>Biochemistry, Molecular Biology</topic><topic>Calcium</topic><topic>Calcium - metabolism</topic><topic>Calcium-Transporting ATPases - chemistry</topic><topic>Calcium-Transporting ATPases - genetics</topic><topic>Calcium-Transporting ATPases - metabolism</topic><topic>Cell lines</topic><topic>Cellular biology</topic><topic>Cloning, Molecular</topic><topic>Dimerization</topic><topic>Endoplasmic Reticulum - metabolism</topic><topic>Exons</topic><topic>Gene Expression</topic><topic>HeLa Cells</topic><topic>Humans</topic><topic>Intracellular Membranes - metabolism</topic><topic>Life Sciences</topic><topic>Liver</topic><topic>Molecular Sequence Data</topic><topic>Original</topic><topic>P values</topic><topic>Protein Isoforms - chemistry</topic><topic>Protein Isoforms - genetics</topic><topic>Protein Isoforms - metabolism</topic><topic>Protein Structure, Secondary</topic><topic>Proteins</topic><topic>Pumps</topic><topic>RNA Splicing</topic><topic>Sarcoplasmic Reticulum Calcium-Transporting ATPases</topic><topic>Splicing</topic><topic>Tissue Distribution</topic><topic>Transfection</topic><topic>Tumor Cells, Cultured</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Chami, Mounia</creatorcontrib><creatorcontrib>Gozuacik, Devrim</creatorcontrib><creatorcontrib>Lagorce, David</creatorcontrib><creatorcontrib>Brini, Marisa</creatorcontrib><creatorcontrib>Falson, Pierre</creatorcontrib><creatorcontrib>Peaucellier, Gérard</creatorcontrib><creatorcontrib>Pinton, Paolo</creatorcontrib><creatorcontrib>Lecoeur, Hervé</creatorcontrib><creatorcontrib>Gougeon, Marie-Lyse</creatorcontrib><creatorcontrib>le Maire, Marc</creatorcontrib><creatorcontrib>Rizzuto, Rosario</creatorcontrib><creatorcontrib>Bréchot, Christian</creatorcontrib><creatorcontrib>Paterlini-Bréchot, Patrizia</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids 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>Hyper Article en Ligne (HAL)</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The Journal of cell biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Chami, Mounia</au><au>Gozuacik, Devrim</au><au>Lagorce, David</au><au>Brini, Marisa</au><au>Falson, Pierre</au><au>Peaucellier, Gérard</au><au>Pinton, Paolo</au><au>Lecoeur, Hervé</au><au>Gougeon, Marie-Lyse</au><au>le Maire, Marc</au><au>Rizzuto, Rosario</au><au>Bréchot, Christian</au><au>Paterlini-Bréchot, Patrizia</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>SERCA1 Truncated Proteins Unable to Pump Calcium Reduce the Endoplasmic Reticulum Calcium Concentration and Induce Apoptosis</atitle><jtitle>The Journal of cell biology</jtitle><addtitle>J Cell Biol</addtitle><date>2001-06-11</date><risdate>2001</risdate><volume>153</volume><issue>6</issue><spage>1301</spage><epage>1313</epage><pages>1301-1313</pages><issn>0021-9525</issn><eissn>1540-8140</eissn><coden>JCLBA3</coden><abstract>By pumping calcium from the cytosol to the ER, sarco/endoplasmic reticulum calcium ATPases (SERCAs) play a major role in the control of calcium signaling. We describe two SERCA1 splice variants (S1Ts) characterized by exon 4 and/or exon 11 splicing, encoding COOH terminally truncated proteins, having only one of the seven calcium-binding residues, and thus unable to pump calcium. As shown by semiquantitative RT-PCR, S1T transcripts are differentially expressed in several adult and fetal human tissues, but not in skeletal muscle and heart. S1T proteins expression was detected by Western blot in nontransfected cell lines. In transiently transfected cells, S1T homodimers were revealed by Western blot using mildly denaturing conditions. S1T proteins were shown, by confocal scanning microscopy, to colocalize with endogenous SERCA2b into the ER membrane. Using ER-targeted aequorin (erAEQ), we have found that S1T proteins reduce ER calcium and reverse elevation of ER calcium loading induced by SERCA1 and SERCA2b. Our results also show that SERCA1 variants increase ER calcium leakage and are consistent with the hypothesis of a cation channel formed by S1T homodimers. Finally, when overexpressed in liver-derived cells, S1T proteins significantly induce apoptosis. These data reveal a further mechanism modulating Ca2+accumulation into the ER of nonmuscle cells and highlight the relevance of S1T proteins to the control of apoptosis.</abstract><cop>United States</cop><pub>Rockefeller University Press</pub><pmid>11402072</pmid><doi>10.1083/jcb.153.6.1301</doi><tpages>13</tpages><orcidid>https://orcid.org/0000-0002-9760-4577</orcidid><orcidid>https://orcid.org/0000-0003-1498-7187</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Adult Amino Acid Sequence Antibodies Apoptosis Biochemistry, Molecular Biology Calcium Calcium - metabolism Calcium-Transporting ATPases - chemistry Calcium-Transporting ATPases - genetics Calcium-Transporting ATPases - metabolism Cell lines Cellular biology Cloning, Molecular Dimerization Endoplasmic Reticulum - metabolism Exons Gene Expression HeLa Cells Humans Intracellular Membranes - metabolism Life Sciences Liver Molecular Sequence Data Original P values Protein Isoforms - chemistry Protein Isoforms - genetics Protein Isoforms - metabolism Protein Structure, Secondary Proteins Pumps RNA Splicing Sarcoplasmic Reticulum Calcium-Transporting ATPases Splicing Tissue Distribution Transfection Tumor Cells, Cultured |
| title | SERCA1 Truncated Proteins Unable to Pump Calcium Reduce the Endoplasmic Reticulum Calcium Concentration and Induce Apoptosis |
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