Mitochondrial Creatine Kinase and Mitochondrial Outer Membrane Porin Show a Direct Interaction That Is Modulated by Calcium
Mitochondrial creatine kinase (MtCK) co-localizes with mitochondrial porin (voltage-dependent anion channel) and adenine nucleotide translocator in mitochondrial contact sites. A specific, direct protein-protein interaction between MtCK and mitochondrial porin was demonstrated using surface plasmon...
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| Veröffentlicht in: | The Journal of biological chemistry 2001-12, Vol.276 (51), p.48027-48030 |
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| container_issue | 51 |
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| container_title | The Journal of biological chemistry |
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| creator | Schlattner, Uwe Dolder, Max Wallimann, Theo Tokarska-Schlattner, Malgorzata |
| description | Mitochondrial creatine kinase (MtCK) co-localizes with mitochondrial porin (voltage-dependent anion channel) and adenine nucleotide translocator in mitochondrial contact sites. A specific, direct protein-protein interaction between MtCK and mitochondrial porin was demonstrated using surface plasmon resonance spectroscopy. This interaction was independent of the immobilized binding partner (porin reconstituted in liposomes or MtCK) or the analyzed isoform (chicken sarcomeric MtCK or human ubiquitous MtCK, human recombinant porin, or purified bovine porin). Increased ionic strength reduced the binding of MtCK to porin, suggesting predominantly ionic interactions. By contrast, micromolar concentrations of Ca2+ increased the amount of bound MtCK, indicating a physiological regulation of complex formation. No interaction of MtCK with reconstituted adenine nucleotide translocator was detectable in our experimental setup. The relevance of these findings for structure and function of mitochondrial contact sites is discussed. |
| doi_str_mv | 10.1074/jbc.M106524200 |
| format | Article |
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A specific, direct protein-protein interaction between MtCK and mitochondrial porin was demonstrated using surface plasmon resonance spectroscopy. This interaction was independent of the immobilized binding partner (porin reconstituted in liposomes or MtCK) or the analyzed isoform (chicken sarcomeric MtCK or human ubiquitous MtCK, human recombinant porin, or purified bovine porin). Increased ionic strength reduced the binding of MtCK to porin, suggesting predominantly ionic interactions. By contrast, micromolar concentrations of Ca2+ increased the amount of bound MtCK, indicating a physiological regulation of complex formation. No interaction of MtCK with reconstituted adenine nucleotide translocator was detectable in our experimental setup. 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Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c477t-7726afa3a6ab02cc91bdd2f90e115fbd19df333a485b3cd501268bd7b2d787ad3</citedby><cites>FETCH-LOGICAL-c477t-7726afa3a6ab02cc91bdd2f90e115fbd19df333a485b3cd501268bd7b2d787ad3</cites><orcidid>0000-0003-1159-5911</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,315,781,785,886,27929,27930</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11602586$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://inserm.hal.science/inserm-00390835$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Schlattner, Uwe</creatorcontrib><creatorcontrib>Dolder, Max</creatorcontrib><creatorcontrib>Wallimann, Theo</creatorcontrib><creatorcontrib>Tokarska-Schlattner, Malgorzata</creatorcontrib><title>Mitochondrial Creatine Kinase and Mitochondrial Outer Membrane Porin Show a Direct Interaction That Is Modulated by Calcium</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Mitochondrial creatine kinase (MtCK) co-localizes with mitochondrial porin (voltage-dependent anion channel) and adenine nucleotide translocator in mitochondrial contact sites. A specific, direct protein-protein interaction between MtCK and mitochondrial porin was demonstrated using surface plasmon resonance spectroscopy. This interaction was independent of the immobilized binding partner (porin reconstituted in liposomes or MtCK) or the analyzed isoform (chicken sarcomeric MtCK or human ubiquitous MtCK, human recombinant porin, or purified bovine porin). Increased ionic strength reduced the binding of MtCK to porin, suggesting predominantly ionic interactions. By contrast, micromolar concentrations of Ca2+ increased the amount of bound MtCK, indicating a physiological regulation of complex formation. No interaction of MtCK with reconstituted adenine nucleotide translocator was detectable in our experimental setup. The relevance of these findings for structure and function of mitochondrial contact sites is discussed.</description><subject>adenine nucleotide translocator</subject><subject>Animals</subject><subject>anion channels</subject><subject>Biochemistry, Molecular Biology</subject><subject>Calcium</subject><subject>Calcium - metabolism</subject><subject>Cattle</subject><subject>Chickens</subject><subject>Creatine Kinase</subject><subject>Creatine Kinase - metabolism</subject><subject>Humans</subject><subject>Life Sciences</subject><subject>Microscopy, Electron</subject><subject>Mitochondria</subject><subject>Mitochondria - enzymology</subject><subject>porin</subject><subject>Porins</subject><subject>Porins - metabolism</subject><subject>Protein Binding</subject><subject>Surface Plasmon Resonance</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkctv1DAQhy0EokvhyhH5gDiRxY84do7V8mjFropEkbhZ40eIqyRu7aRVxT-Py66oOCB8sTT6ZjTz-xB6ScmaElm_uzR2vaOkEaxmhDxCK0oUr7ig3x-jFSGMVi0T6gg9y_mSlFe39Ck6orQhpdys0M9dmKPt4-RSgAFvkoc5TB5_DhNkj2Fy-G_ifJl9wjs_mgSF-xJTmPDXPt5iwO9D8nbGZ1NBwM4hTviih1LIeBfdMsDsHTZ3eAODDcv4HD3pYMj-xeE_Rt8-frjYnFbb809nm5NtZWsp50pK1kAHHBowhFnbUuMc61riKRWdcbR1HeccaiUMt04QyhplnDTMSSXB8WP0dj-3h0FfpTBCutMRgj492eowZZ9GTQhvS3Lihhb8zR6_SvF68XnWY8jWD0O5Ny5ZS8aFbAT5L0gVrxVV9-B6D9oUc06--7MFJfpeoy4a9YPG0vDqMHkxo3cP-MFbAV4fTgo_-tsSuzahSPKjZrLRgupaESYLpvaYL_HeBJ90tsFP1rvfprSL4V8r_AJ-n7eM</recordid><startdate>20011221</startdate><enddate>20011221</enddate><creator>Schlattner, Uwe</creator><creator>Dolder, Max</creator><creator>Wallimann, Theo</creator><creator>Tokarska-Schlattner, Malgorzata</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</scope><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><scope>1XC</scope><orcidid>https://orcid.org/0000-0003-1159-5911</orcidid></search><sort><creationdate>20011221</creationdate><title>Mitochondrial Creatine Kinase and Mitochondrial Outer Membrane Porin Show a Direct Interaction That Is Modulated by Calcium</title><author>Schlattner, Uwe ; Dolder, Max ; Wallimann, Theo ; Tokarska-Schlattner, Malgorzata</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c477t-7726afa3a6ab02cc91bdd2f90e115fbd19df333a485b3cd501268bd7b2d787ad3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>adenine nucleotide translocator</topic><topic>Animals</topic><topic>anion channels</topic><topic>Biochemistry, Molecular Biology</topic><topic>Calcium</topic><topic>Calcium - metabolism</topic><topic>Cattle</topic><topic>Chickens</topic><topic>Creatine Kinase</topic><topic>Creatine Kinase - metabolism</topic><topic>Humans</topic><topic>Life Sciences</topic><topic>Microscopy, Electron</topic><topic>Mitochondria</topic><topic>Mitochondria - enzymology</topic><topic>porin</topic><topic>Porins</topic><topic>Porins - metabolism</topic><topic>Protein Binding</topic><topic>Surface Plasmon Resonance</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Schlattner, Uwe</creatorcontrib><creatorcontrib>Dolder, Max</creatorcontrib><creatorcontrib>Wallimann, Theo</creatorcontrib><creatorcontrib>Tokarska-Schlattner, Malgorzata</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><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><collection>Hyper Article en Ligne (HAL)</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Schlattner, Uwe</au><au>Dolder, Max</au><au>Wallimann, Theo</au><au>Tokarska-Schlattner, Malgorzata</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Mitochondrial Creatine Kinase and Mitochondrial Outer Membrane Porin Show a Direct Interaction That Is Modulated by Calcium</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2001-12-21</date><risdate>2001</risdate><volume>276</volume><issue>51</issue><spage>48027</spage><epage>48030</epage><pages>48027-48030</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Mitochondrial creatine kinase (MtCK) co-localizes with mitochondrial porin (voltage-dependent anion channel) and adenine nucleotide translocator in mitochondrial contact sites. A specific, direct protein-protein interaction between MtCK and mitochondrial porin was demonstrated using surface plasmon resonance spectroscopy. This interaction was independent of the immobilized binding partner (porin reconstituted in liposomes or MtCK) or the analyzed isoform (chicken sarcomeric MtCK or human ubiquitous MtCK, human recombinant porin, or purified bovine porin). Increased ionic strength reduced the binding of MtCK to porin, suggesting predominantly ionic interactions. By contrast, micromolar concentrations of Ca2+ increased the amount of bound MtCK, indicating a physiological regulation of complex formation. No interaction of MtCK with reconstituted adenine nucleotide translocator was detectable in our experimental setup. The relevance of these findings for structure and function of mitochondrial contact sites is discussed.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>11602586</pmid><doi>10.1074/jbc.M106524200</doi><tpages>4</tpages><orcidid>https://orcid.org/0000-0003-1159-5911</orcidid><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | adenine nucleotide translocator Animals anion channels Biochemistry, Molecular Biology Calcium Calcium - metabolism Cattle Chickens Creatine Kinase Creatine Kinase - metabolism Humans Life Sciences Microscopy, Electron Mitochondria Mitochondria - enzymology porin Porins Porins - metabolism Protein Binding Surface Plasmon Resonance |
| title | Mitochondrial Creatine Kinase and Mitochondrial Outer Membrane Porin Show a Direct Interaction That Is Modulated by Calcium |
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