The membrane-associated fraction of cyclase associate protein 1 translocates to the cytosol upon platelet stimulation
Platelets undergo profound shape changes upon adhesion to damaged blood vessel walls that are mediated by reorganisation of the actin cytoskeleton in response to receptor-mediated signalling cascades. The highly conserved 56 kDa multidomain cyclase associated protein 1 (CAP1) works in concert with c...
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| Veröffentlicht in: | Scientific reports 2018-07, Vol.8 (1), p.10804-12, Article 10804 |
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| creator | Joshi, Pooja Riley, David R. J. Khalil, Jawad S. Xiong, Huajiang Ji, Wei Rivero, Francisco |
| description | Platelets undergo profound shape changes upon adhesion to damaged blood vessel walls that are mediated by reorganisation of the actin cytoskeleton in response to receptor-mediated signalling cascades. The highly conserved 56 kDa multidomain cyclase associated protein 1 (CAP1) works in concert with cofilin and profilin to modulate actin filament turnover by facilitating cofilin-mediated actin filament severing and depolymerisation and catalysing profilin-mediated regeneration of actin monomers for reutilisation in growing filaments. CAP1 is abundant in platelets but its roles remain unexplored. We report that in suspended platelets CAP1 localises predominantly at the cell cortex whereas in spread platelets it is uniformly distributed in the cytoplasm, with enrichment at the cell cortex and the periphery of actin nodules. Upon subcellular fractionation most CAP1 was found cytosolic but part associated to the membrane fraction in an actin-independent manner. Interestingly, upon stimulation with thrombin a significant proportion of the membrane-associated CAP1 translocates to the cytosol. This relocalisation was prevented by prior treatment with PGI2 or the nitric oxide donor GSNO, or by inhibition of GSK3. Our results place CAP1 at a crossroad of signalling pathways that control platelet activation by contributing to actin remodelling at the cell cortex and actin nodules during platelet spreading. |
| doi_str_mv | 10.1038/s41598-018-29151-w |
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J. ; Khalil, Jawad S. ; Xiong, Huajiang ; Ji, Wei ; Rivero, Francisco</creator><creatorcontrib>Joshi, Pooja ; Riley, David R. J. ; Khalil, Jawad S. ; Xiong, Huajiang ; Ji, Wei ; Rivero, Francisco</creatorcontrib><description>Platelets undergo profound shape changes upon adhesion to damaged blood vessel walls that are mediated by reorganisation of the actin cytoskeleton in response to receptor-mediated signalling cascades. The highly conserved 56 kDa multidomain cyclase associated protein 1 (CAP1) works in concert with cofilin and profilin to modulate actin filament turnover by facilitating cofilin-mediated actin filament severing and depolymerisation and catalysing profilin-mediated regeneration of actin monomers for reutilisation in growing filaments. CAP1 is abundant in platelets but its roles remain unexplored. We report that in suspended platelets CAP1 localises predominantly at the cell cortex whereas in spread platelets it is uniformly distributed in the cytoplasm, with enrichment at the cell cortex and the periphery of actin nodules. Upon subcellular fractionation most CAP1 was found cytosolic but part associated to the membrane fraction in an actin-independent manner. Interestingly, upon stimulation with thrombin a significant proportion of the membrane-associated CAP1 translocates to the cytosol. This relocalisation was prevented by prior treatment with PGI2 or the nitric oxide donor GSNO, or by inhibition of GSK3. Our results place CAP1 at a crossroad of signalling pathways that control platelet activation by contributing to actin remodelling at the cell cortex and actin nodules during platelet spreading.</description><identifier>ISSN: 2045-2322</identifier><identifier>EISSN: 2045-2322</identifier><identifier>DOI: 10.1038/s41598-018-29151-w</identifier><identifier>PMID: 30018317</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>13 ; 13/1 ; 13/51 ; 13/95 ; 14/63 ; 631/80/128/1276 ; 631/80/84/1756 ; 631/80/86/820 ; 82 ; Acids ; Actin ; Actins - metabolism ; Antibodies ; Blood & organ donations ; Blood platelets ; Blood Platelets - drug effects ; Blood Platelets - metabolism ; Cell Cycle Proteins - metabolism ; Cell Line ; Cofilin ; Cytoplasm ; Cytoskeletal Proteins - metabolism ; Cytoskeleton ; Cytosol ; Cytosol - metabolism ; Depolymerization ; Filaments ; Fractionation ; Glucose ; Glycogen Synthase Kinase 3 - antagonists & inhibitors ; Glycogen Synthase Kinase 3 - metabolism ; Humanities and Social Sciences ; Humans ; Immunoglobulins ; Kinases ; Localization ; Mammals ; Monomers ; Morphology ; Motility ; multidisciplinary ; Nitric oxide ; Nodules ; Platelet Activation - physiology ; Platelets ; Profilin ; Proteins ; S-Nitrosoglutathione - pharmacology ; Science ; Science (multidisciplinary) ; Signal transduction ; Thrombin ; Thrombin - pharmacology</subject><ispartof>Scientific reports, 2018-07, Vol.8 (1), p.10804-12, Article 10804</ispartof><rights>The Author(s) 2018</rights><rights>2018. 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J.</creatorcontrib><creatorcontrib>Khalil, Jawad S.</creatorcontrib><creatorcontrib>Xiong, Huajiang</creatorcontrib><creatorcontrib>Ji, Wei</creatorcontrib><creatorcontrib>Rivero, Francisco</creatorcontrib><title>The membrane-associated fraction of cyclase associate protein 1 translocates to the cytosol upon platelet stimulation</title><title>Scientific reports</title><addtitle>Sci Rep</addtitle><addtitle>Sci Rep</addtitle><description>Platelets undergo profound shape changes upon adhesion to damaged blood vessel walls that are mediated by reorganisation of the actin cytoskeleton in response to receptor-mediated signalling cascades. The highly conserved 56 kDa multidomain cyclase associated protein 1 (CAP1) works in concert with cofilin and profilin to modulate actin filament turnover by facilitating cofilin-mediated actin filament severing and depolymerisation and catalysing profilin-mediated regeneration of actin monomers for reutilisation in growing filaments. CAP1 is abundant in platelets but its roles remain unexplored. We report that in suspended platelets CAP1 localises predominantly at the cell cortex whereas in spread platelets it is uniformly distributed in the cytoplasm, with enrichment at the cell cortex and the periphery of actin nodules. Upon subcellular fractionation most CAP1 was found cytosolic but part associated to the membrane fraction in an actin-independent manner. Interestingly, upon stimulation with thrombin a significant proportion of the membrane-associated CAP1 translocates to the cytosol. This relocalisation was prevented by prior treatment with PGI2 or the nitric oxide donor GSNO, or by inhibition of GSK3. Our results place CAP1 at a crossroad of signalling pathways that control platelet activation by contributing to actin remodelling at the cell cortex and actin nodules during platelet spreading.</description><subject>13</subject><subject>13/1</subject><subject>13/51</subject><subject>13/95</subject><subject>14/63</subject><subject>631/80/128/1276</subject><subject>631/80/84/1756</subject><subject>631/80/86/820</subject><subject>82</subject><subject>Acids</subject><subject>Actin</subject><subject>Actins - metabolism</subject><subject>Antibodies</subject><subject>Blood & organ donations</subject><subject>Blood platelets</subject><subject>Blood Platelets - drug effects</subject><subject>Blood Platelets - metabolism</subject><subject>Cell Cycle Proteins - metabolism</subject><subject>Cell Line</subject><subject>Cofilin</subject><subject>Cytoplasm</subject><subject>Cytoskeletal Proteins - metabolism</subject><subject>Cytoskeleton</subject><subject>Cytosol</subject><subject>Cytosol - metabolism</subject><subject>Depolymerization</subject><subject>Filaments</subject><subject>Fractionation</subject><subject>Glucose</subject><subject>Glycogen Synthase Kinase 3 - antagonists & inhibitors</subject><subject>Glycogen Synthase Kinase 3 - metabolism</subject><subject>Humanities and Social Sciences</subject><subject>Humans</subject><subject>Immunoglobulins</subject><subject>Kinases</subject><subject>Localization</subject><subject>Mammals</subject><subject>Monomers</subject><subject>Morphology</subject><subject>Motility</subject><subject>multidisciplinary</subject><subject>Nitric oxide</subject><subject>Nodules</subject><subject>Platelet Activation - physiology</subject><subject>Platelets</subject><subject>Profilin</subject><subject>Proteins</subject><subject>S-Nitrosoglutathione - pharmacology</subject><subject>Science</subject><subject>Science (multidisciplinary)</subject><subject>Signal transduction</subject><subject>Thrombin</subject><subject>Thrombin - pharmacology</subject><issn>2045-2322</issn><issn>2045-2322</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><sourceid>C6C</sourceid><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNp9Uctu1DAUtRCIVqU_wAJZYsMmxdceT5INEqp4VKrEpqwtx7lpUzlx8HWo5u-57ZShsMAbP87DPj5CvAZ1Bso072kDtm0qBU2lW7BQ3T0Tx1ptbKWN1s-frI_EKdGt4mF1u4H2pTgyinUG6mOxXt2gnHDqsp-x8kQpjL5gL4fsQxnTLNMgwy5ETygPsFxyKjjOEmRhIcUU-JRkSbKwX9iVRCnKdWH9EhmKWCSVcVp5w6avxIvBR8LTx_lEfP_86er8a3X57cvF-cfLKliAUtUG-l71oQ9Gd60N28DJofO1Ds2AVnV1o6HmjFahGdD7pulw4GBq2ytjenMiPux9l7WbsA8483OjW_I4-bxzyY_ub2Qeb9x1-um2yioDwAbvHg1y-rEiFTeNFDBG_q20ktOqBlsbvVFMffsP9TateeZ4D6x7mtXM0ntWyIko43B4DCh3X6zbF-u4IPdQrLtj0ZunMQ6S3zUywewJxNB8jfnP3f-x_QUw5LGO</recordid><startdate>20180717</startdate><enddate>20180717</enddate><creator>Joshi, Pooja</creator><creator>Riley, David R. 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J.</creatorcontrib><creatorcontrib>Khalil, Jawad S.</creatorcontrib><creatorcontrib>Xiong, Huajiang</creatorcontrib><creatorcontrib>Ji, Wei</creatorcontrib><creatorcontrib>Rivero, Francisco</creatorcontrib><collection>Springer Nature OA Free Journals</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Biological Science Database</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Scientific reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Joshi, Pooja</au><au>Riley, David R. J.</au><au>Khalil, Jawad S.</au><au>Xiong, Huajiang</au><au>Ji, Wei</au><au>Rivero, Francisco</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The membrane-associated fraction of cyclase associate protein 1 translocates to the cytosol upon platelet stimulation</atitle><jtitle>Scientific reports</jtitle><stitle>Sci Rep</stitle><addtitle>Sci Rep</addtitle><date>2018-07-17</date><risdate>2018</risdate><volume>8</volume><issue>1</issue><spage>10804</spage><epage>12</epage><pages>10804-12</pages><artnum>10804</artnum><issn>2045-2322</issn><eissn>2045-2322</eissn><abstract>Platelets undergo profound shape changes upon adhesion to damaged blood vessel walls that are mediated by reorganisation of the actin cytoskeleton in response to receptor-mediated signalling cascades. The highly conserved 56 kDa multidomain cyclase associated protein 1 (CAP1) works in concert with cofilin and profilin to modulate actin filament turnover by facilitating cofilin-mediated actin filament severing and depolymerisation and catalysing profilin-mediated regeneration of actin monomers for reutilisation in growing filaments. CAP1 is abundant in platelets but its roles remain unexplored. We report that in suspended platelets CAP1 localises predominantly at the cell cortex whereas in spread platelets it is uniformly distributed in the cytoplasm, with enrichment at the cell cortex and the periphery of actin nodules. Upon subcellular fractionation most CAP1 was found cytosolic but part associated to the membrane fraction in an actin-independent manner. Interestingly, upon stimulation with thrombin a significant proportion of the membrane-associated CAP1 translocates to the cytosol. This relocalisation was prevented by prior treatment with PGI2 or the nitric oxide donor GSNO, or by inhibition of GSK3. Our results place CAP1 at a crossroad of signalling pathways that control platelet activation by contributing to actin remodelling at the cell cortex and actin nodules during platelet spreading.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>30018317</pmid><doi>10.1038/s41598-018-29151-w</doi><tpages>12</tpages><orcidid>https://orcid.org/0000-0001-5435-6991</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | 13 13/1 13/51 13/95 14/63 631/80/128/1276 631/80/84/1756 631/80/86/820 82 Acids Actin Actins - metabolism Antibodies Blood & organ donations Blood platelets Blood Platelets - drug effects Blood Platelets - metabolism Cell Cycle Proteins - metabolism Cell Line Cofilin Cytoplasm Cytoskeletal Proteins - metabolism Cytoskeleton Cytosol Cytosol - metabolism Depolymerization Filaments Fractionation Glucose Glycogen Synthase Kinase 3 - antagonists & inhibitors Glycogen Synthase Kinase 3 - metabolism Humanities and Social Sciences Humans Immunoglobulins Kinases Localization Mammals Monomers Morphology Motility multidisciplinary Nitric oxide Nodules Platelet Activation - physiology Platelets Profilin Proteins S-Nitrosoglutathione - pharmacology Science Science (multidisciplinary) Signal transduction Thrombin Thrombin - pharmacology |
| title | The membrane-associated fraction of cyclase associate protein 1 translocates to the cytosol upon platelet stimulation |
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