Differential membrane targeting of the SERCA and PMCA calcium pumps: experiments with recombinant chimeras
ABSTRACT Structural features underlying retention of the SERCA pump in intracellular compartments and the sorting of the PMCA pump to the plasma membrane are not known. The biochemical properties of the two pumps suggest that their differential localization may respond to specific functional demands...
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| Veröffentlicht in: | The FASEB journal 2002-04, Vol.16 (6), p.519-528 |
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| creator | Guerini, Danilo Guidi, Fabrizio Carafoli, Ernesto |
| description | ABSTRACT
Structural features underlying retention of the SERCA pump in intracellular compartments and the sorting of the PMCA pump to the plasma membrane are not known. The biochemical properties of the two pumps suggest that their differential localization may respond to specific functional demands. The two pumps may control Ca2+ gradients of different magnitude and dynamic properties. For instance, it has recently become clear that the Ca2+ gradient across the endoplasmic reticulum (ER) membrane is smaller than that across the plasma membrane. Previous experiments with chimerical constructs of the SERCA and PMCA pumps had suggested a role for the amino‐terminal domain in the ER retention of the SERCA pump. Experiments aimed at narrowing down the region responsible for the retention now indicate that the first 28 amino acids of the SERCA pump may play a role in membrane localization. Results also suggest that the formation of oligomers (possibly through the first 28 amino acids) might be critical to the retention mechanism.—Guerini, D., Guidi, F., Carafoli, E. Differential membrane targeting of the SERCA and PMCA calcium pumps: experiments with recombinant chimeras. FASEB J. 16, 519–528 (2002) |
| doi_str_mv | 10.1096/fj.01-0362com |
| format | Article |
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Structural features underlying retention of the SERCA pump in intracellular compartments and the sorting of the PMCA pump to the plasma membrane are not known. The biochemical properties of the two pumps suggest that their differential localization may respond to specific functional demands. The two pumps may control Ca2+ gradients of different magnitude and dynamic properties. For instance, it has recently become clear that the Ca2+ gradient across the endoplasmic reticulum (ER) membrane is smaller than that across the plasma membrane. Previous experiments with chimerical constructs of the SERCA and PMCA pumps had suggested a role for the amino‐terminal domain in the ER retention of the SERCA pump. Experiments aimed at narrowing down the region responsible for the retention now indicate that the first 28 amino acids of the SERCA pump may play a role in membrane localization. Results also suggest that the formation of oligomers (possibly through the first 28 amino acids) might be critical to the retention mechanism.—Guerini, D., Guidi, F., Carafoli, E. Differential membrane targeting of the SERCA and PMCA calcium pumps: experiments with recombinant chimeras. FASEB J. 16, 519–528 (2002)</description><identifier>ISSN: 0892-6638</identifier><identifier>EISSN: 1530-6860</identifier><identifier>DOI: 10.1096/fj.01-0362com</identifier><identifier>PMID: 11919154</identifier><language>eng</language><publisher>United States</publisher><subject>Adenosine Triphosphate - metabolism ; Animals ; Biotinylation ; Calcium-Transporting ATPases - analysis ; Calcium-Transporting ATPases - chemistry ; Calcium-Transporting ATPases - genetics ; Calcium-Transporting ATPases - metabolism ; Cation Transport Proteins ; Cell Membrane - enzymology ; Cells, Cultured ; chimeric proteins ; COS Cells ; Endoplasmic Reticulum - enzymology ; ER/SR Ca2+ pump ; Intracellular Membranes - enzymology ; Microscopy, Fluorescence ; plasma membrane Ca2+ pump ; Plasma Membrane Calcium-Transporting ATPases ; Protein Structure, Tertiary ; Protein Transport ; Recombinant Fusion Proteins - analysis ; Sarcoplasmic Reticulum Calcium-Transporting ATPases ; Spodoptera - genetics ; Transfection</subject><ispartof>The FASEB journal, 2002-04, Vol.16 (6), p.519-528</ispartof><rights>FASEB</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c401M-f9c200d63d71194542892a3becacabc90fec5c10e92ef5c2ade6005326e00fe73</citedby><cites>FETCH-LOGICAL-c401M-f9c200d63d71194542892a3becacabc90fec5c10e92ef5c2ade6005326e00fe73</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1096%2Ffj.01-0362com$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1096%2Ffj.01-0362com$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1416,27922,27923,45572,45573</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11919154$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Guerini, Danilo</creatorcontrib><creatorcontrib>Guidi, Fabrizio</creatorcontrib><creatorcontrib>Carafoli, Ernesto</creatorcontrib><title>Differential membrane targeting of the SERCA and PMCA calcium pumps: experiments with recombinant chimeras</title><title>The FASEB journal</title><addtitle>FASEB J</addtitle><description>ABSTRACT
Structural features underlying retention of the SERCA pump in intracellular compartments and the sorting of the PMCA pump to the plasma membrane are not known. The biochemical properties of the two pumps suggest that their differential localization may respond to specific functional demands. The two pumps may control Ca2+ gradients of different magnitude and dynamic properties. For instance, it has recently become clear that the Ca2+ gradient across the endoplasmic reticulum (ER) membrane is smaller than that across the plasma membrane. Previous experiments with chimerical constructs of the SERCA and PMCA pumps had suggested a role for the amino‐terminal domain in the ER retention of the SERCA pump. Experiments aimed at narrowing down the region responsible for the retention now indicate that the first 28 amino acids of the SERCA pump may play a role in membrane localization. Results also suggest that the formation of oligomers (possibly through the first 28 amino acids) might be critical to the retention mechanism.—Guerini, D., Guidi, F., Carafoli, E. Differential membrane targeting of the SERCA and PMCA calcium pumps: experiments with recombinant chimeras. FASEB J. 16, 519–528 (2002)</description><subject>Adenosine Triphosphate - metabolism</subject><subject>Animals</subject><subject>Biotinylation</subject><subject>Calcium-Transporting ATPases - analysis</subject><subject>Calcium-Transporting ATPases - chemistry</subject><subject>Calcium-Transporting ATPases - genetics</subject><subject>Calcium-Transporting ATPases - metabolism</subject><subject>Cation Transport Proteins</subject><subject>Cell Membrane - enzymology</subject><subject>Cells, Cultured</subject><subject>chimeric proteins</subject><subject>COS Cells</subject><subject>Endoplasmic Reticulum - enzymology</subject><subject>ER/SR Ca2+ pump</subject><subject>Intracellular Membranes - enzymology</subject><subject>Microscopy, Fluorescence</subject><subject>plasma membrane Ca2+ pump</subject><subject>Plasma Membrane Calcium-Transporting ATPases</subject><subject>Protein Structure, Tertiary</subject><subject>Protein Transport</subject><subject>Recombinant Fusion Proteins - analysis</subject><subject>Sarcoplasmic Reticulum Calcium-Transporting ATPases</subject><subject>Spodoptera - genetics</subject><subject>Transfection</subject><issn>0892-6638</issn><issn>1530-6860</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUlPwzAQhS0EgrIcuSKfuAXGcePG3KBQFlGBWM6W44ypq2zYiYB_j1ErcQPNwTOaT0_z_Ag5ZHDCQIpTuzwBlgAXqWnrDTJiGYdE5AI2yQhymSZC8HyH7IawBAAGTGyTHcZkrGw8IstLZy16bHqnK1pjXXjdIO21f8PeNW-0tbRfIH2-epqeU92U9HEeG6Mr44aadkPdhTOKnx16V0eVQD9cv6Ae4zWFa3TTU7OIG6_DPtmyugp4sH73yOvs6mV6k9w_XN9Oz-8TMwY2T6w0KUApeDmJZ46zcRpdaF6g0UYXRoJFkxkGKFO0mUl1iQIg46lAiLsJ3yPHK93Ot-8Dhl7VLhisqmisHYKaRONSCvgXZHmW84lkEUxWoPFtCB6t6qJb7b8UA_WTgrJLBUytU4j80Vp4KGosf-n1t0fgbAV8uAq__lZTs-eLdHYXo4vz9GHOvwHHXZY1</recordid><startdate>200204</startdate><enddate>200204</enddate><creator>Guerini, Danilo</creator><creator>Guidi, Fabrizio</creator><creator>Carafoli, Ernesto</creator><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>7QP</scope><scope>7X8</scope></search><sort><creationdate>200204</creationdate><title>Differential membrane targeting of the SERCA and PMCA calcium pumps: experiments with recombinant chimeras</title><author>Guerini, Danilo ; Guidi, Fabrizio ; Carafoli, Ernesto</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c401M-f9c200d63d71194542892a3becacabc90fec5c10e92ef5c2ade6005326e00fe73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Adenosine Triphosphate - metabolism</topic><topic>Animals</topic><topic>Biotinylation</topic><topic>Calcium-Transporting ATPases - analysis</topic><topic>Calcium-Transporting ATPases - chemistry</topic><topic>Calcium-Transporting ATPases - genetics</topic><topic>Calcium-Transporting ATPases - metabolism</topic><topic>Cation Transport Proteins</topic><topic>Cell Membrane - enzymology</topic><topic>Cells, Cultured</topic><topic>chimeric proteins</topic><topic>COS Cells</topic><topic>Endoplasmic Reticulum - enzymology</topic><topic>ER/SR Ca2+ pump</topic><topic>Intracellular Membranes - enzymology</topic><topic>Microscopy, Fluorescence</topic><topic>plasma membrane Ca2+ pump</topic><topic>Plasma Membrane Calcium-Transporting ATPases</topic><topic>Protein Structure, Tertiary</topic><topic>Protein Transport</topic><topic>Recombinant Fusion Proteins - analysis</topic><topic>Sarcoplasmic Reticulum Calcium-Transporting ATPases</topic><topic>Spodoptera - genetics</topic><topic>Transfection</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Guerini, Danilo</creatorcontrib><creatorcontrib>Guidi, Fabrizio</creatorcontrib><creatorcontrib>Carafoli, Ernesto</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The FASEB journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Guerini, Danilo</au><au>Guidi, Fabrizio</au><au>Carafoli, Ernesto</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Differential membrane targeting of the SERCA and PMCA calcium pumps: experiments with recombinant chimeras</atitle><jtitle>The FASEB journal</jtitle><addtitle>FASEB J</addtitle><date>2002-04</date><risdate>2002</risdate><volume>16</volume><issue>6</issue><spage>519</spage><epage>528</epage><pages>519-528</pages><issn>0892-6638</issn><eissn>1530-6860</eissn><abstract>ABSTRACT
Structural features underlying retention of the SERCA pump in intracellular compartments and the sorting of the PMCA pump to the plasma membrane are not known. The biochemical properties of the two pumps suggest that their differential localization may respond to specific functional demands. The two pumps may control Ca2+ gradients of different magnitude and dynamic properties. For instance, it has recently become clear that the Ca2+ gradient across the endoplasmic reticulum (ER) membrane is smaller than that across the plasma membrane. Previous experiments with chimerical constructs of the SERCA and PMCA pumps had suggested a role for the amino‐terminal domain in the ER retention of the SERCA pump. Experiments aimed at narrowing down the region responsible for the retention now indicate that the first 28 amino acids of the SERCA pump may play a role in membrane localization. Results also suggest that the formation of oligomers (possibly through the first 28 amino acids) might be critical to the retention mechanism.—Guerini, D., Guidi, F., Carafoli, E. Differential membrane targeting of the SERCA and PMCA calcium pumps: experiments with recombinant chimeras. FASEB J. 16, 519–528 (2002)</abstract><cop>United States</cop><pmid>11919154</pmid><doi>10.1096/fj.01-0362com</doi><tpages>10</tpages></addata></record> |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Alma/SFX Local Collection |
| subjects | Adenosine Triphosphate - metabolism Animals Biotinylation Calcium-Transporting ATPases - analysis Calcium-Transporting ATPases - chemistry Calcium-Transporting ATPases - genetics Calcium-Transporting ATPases - metabolism Cation Transport Proteins Cell Membrane - enzymology Cells, Cultured chimeric proteins COS Cells Endoplasmic Reticulum - enzymology ER/SR Ca2+ pump Intracellular Membranes - enzymology Microscopy, Fluorescence plasma membrane Ca2+ pump Plasma Membrane Calcium-Transporting ATPases Protein Structure, Tertiary Protein Transport Recombinant Fusion Proteins - analysis Sarcoplasmic Reticulum Calcium-Transporting ATPases Spodoptera - genetics Transfection |
| title | Differential membrane targeting of the SERCA and PMCA calcium pumps: experiments with recombinant chimeras |
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