Twitchin, a thick-filament protein from molluscan catch muscle, interacts with F-actin in a phosphorylation-dependent way
Twitchin belongs to the titin-like giant proteins family, it is co-localized with thick filaments in molluscan catch muscles and regulates the catch state depending on its level of phosphorylation. The mechanism by which twitchin controls the catch state remains to be established. We report for the...
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| Veröffentlicht in: | Archives of biochemistry and biophysics 2004-12, Vol.432 (2), p.269-277 |
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| container_title | Archives of biochemistry and biophysics |
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| creator | Shelud’ko, Nikolai S. Matusovskaya, Galina G. Permyakova, Tatiana V. Matusovsky, Oleg S. |
| description | Twitchin belongs to the titin-like giant proteins family, it is co-localized with thick filaments in molluscan catch muscles and regulates the catch state depending on its level of phosphorylation. The mechanism by which twitchin controls the catch state remains to be established. We report for the first time the ability of twitchin to interact with F-actin. The interaction is observed at low and physiological ionic strengths, irrespective of the presence or absence of Ca
2+. It was demonstrated by viscosity and turbidity measurements, low- and high-speed co-sedimentation, and with the light-scattering particle size analysis revealing the specific twitchin–actin particles. The twitchin–actin interaction is regulated by twitchin phosphorylation: in vitro phosphorylated twitchin does not interact with F-actin. We speculate that the catch muscle twitchin might provide a mechanical link between thin and thick filaments, which contributes to catch force maintenance. |
| doi_str_mv | 10.1016/j.abb.2004.10.006 |
| format | Article |
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2+. It was demonstrated by viscosity and turbidity measurements, low- and high-speed co-sedimentation, and with the light-scattering particle size analysis revealing the specific twitchin–actin particles. The twitchin–actin interaction is regulated by twitchin phosphorylation: in vitro phosphorylated twitchin does not interact with F-actin. We speculate that the catch muscle twitchin might provide a mechanical link between thin and thick filaments, which contributes to catch force maintenance.</description><identifier>ISSN: 0003-9861</identifier><identifier>EISSN: 1096-0384</identifier><identifier>DOI: 10.1016/j.abb.2004.10.006</identifier><identifier>PMID: 15542066</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Actins - chemistry ; Actin–twitchin interaction ; Animals ; Binding Sites ; Caenorhabditis elegans Proteins ; Calmodulin-Binding Proteins - chemistry ; Catch muscle ; Hydrogen-Ion Concentration ; Molecular Motor Proteins - chemistry ; Mollusca - metabolism ; Molluscs ; Multiprotein Complexes - chemistry ; Muscle Proteins - chemistry ; Muscle, Skeletal - metabolism ; Particle Size ; Phosphorylation ; Protein Binding ; Twitchin phosphorylation ; Viscosity</subject><ispartof>Archives of biochemistry and biophysics, 2004-12, Vol.432 (2), p.269-277</ispartof><rights>2004 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c349t-b2539dccc7d13228b050b109385fc1c2fe9f42052be26dd993538a34163935783</citedby><cites>FETCH-LOGICAL-c349t-b2539dccc7d13228b050b109385fc1c2fe9f42052be26dd993538a34163935783</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.abb.2004.10.006$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>315,782,786,3552,27931,27932,46002</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15542066$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Shelud’ko, Nikolai S.</creatorcontrib><creatorcontrib>Matusovskaya, Galina G.</creatorcontrib><creatorcontrib>Permyakova, Tatiana V.</creatorcontrib><creatorcontrib>Matusovsky, Oleg S.</creatorcontrib><title>Twitchin, a thick-filament protein from molluscan catch muscle, interacts with F-actin in a phosphorylation-dependent way</title><title>Archives of biochemistry and biophysics</title><addtitle>Arch Biochem Biophys</addtitle><description>Twitchin belongs to the titin-like giant proteins family, it is co-localized with thick filaments in molluscan catch muscles and regulates the catch state depending on its level of phosphorylation. The mechanism by which twitchin controls the catch state remains to be established. We report for the first time the ability of twitchin to interact with F-actin. The interaction is observed at low and physiological ionic strengths, irrespective of the presence or absence of Ca
2+. It was demonstrated by viscosity and turbidity measurements, low- and high-speed co-sedimentation, and with the light-scattering particle size analysis revealing the specific twitchin–actin particles. The twitchin–actin interaction is regulated by twitchin phosphorylation: in vitro phosphorylated twitchin does not interact with F-actin. We speculate that the catch muscle twitchin might provide a mechanical link between thin and thick filaments, which contributes to catch force maintenance.</description><subject>Actins - chemistry</subject><subject>Actin–twitchin interaction</subject><subject>Animals</subject><subject>Binding Sites</subject><subject>Caenorhabditis elegans Proteins</subject><subject>Calmodulin-Binding Proteins - chemistry</subject><subject>Catch muscle</subject><subject>Hydrogen-Ion Concentration</subject><subject>Molecular Motor Proteins - chemistry</subject><subject>Mollusca - metabolism</subject><subject>Molluscs</subject><subject>Multiprotein Complexes - chemistry</subject><subject>Muscle Proteins - chemistry</subject><subject>Muscle, Skeletal - metabolism</subject><subject>Particle Size</subject><subject>Phosphorylation</subject><subject>Protein Binding</subject><subject>Twitchin phosphorylation</subject><subject>Viscosity</subject><issn>0003-9861</issn><issn>1096-0384</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE9rGzEQxUVpaZy0HyCXolNPWWck7cq75FRC8wcCuaRnoZVmsZxdrSvJCf72GWNDbwUJzYj3fvAeY5cClgKEvt4sbd8vJUBN-xJAf2ILAZ2uQLX1Z7YAAFV1rRZn7DznDYAQtZZf2ZlomlqC1gu2f3kPxa1DvOKWl3Vwr9UQRjthLHyb5oIh8iHNE5_mcdxlZyN3lgx8omXEKx5iwWRdyZxAa35X0UweOpZv13Omm_ajLWGOlcctRn9Av9v9N_ZlsGPG76f3gv25-_1y-1A9Pd8_3v56qpyqu1L1slGdd86tvFBStj000FNI1TaDE04O2A2UpZE9Su1916lGtVbVQisaV626YD-PXIrzd4e5mClkh-NoI867bPQKdN1pRUJxFLo055xwMNsUJpv2RoA59G02hvo2h74PX9Q3eX6c4Lt-Qv_PcSqYBDdHAVLEt4DJZBcwOvQhoSvGz-E_-A-uR5Eg</recordid><startdate>20041215</startdate><enddate>20041215</enddate><creator>Shelud’ko, Nikolai S.</creator><creator>Matusovskaya, Galina G.</creator><creator>Permyakova, Tatiana V.</creator><creator>Matusovsky, Oleg S.</creator><general>Elsevier Inc</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>7X8</scope></search><sort><creationdate>20041215</creationdate><title>Twitchin, a thick-filament protein from molluscan catch muscle, interacts with F-actin in a phosphorylation-dependent way</title><author>Shelud’ko, Nikolai S. ; Matusovskaya, Galina G. ; Permyakova, Tatiana V. ; Matusovsky, Oleg S.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c349t-b2539dccc7d13228b050b109385fc1c2fe9f42052be26dd993538a34163935783</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Actins - chemistry</topic><topic>Actin–twitchin interaction</topic><topic>Animals</topic><topic>Binding Sites</topic><topic>Caenorhabditis elegans Proteins</topic><topic>Calmodulin-Binding Proteins - chemistry</topic><topic>Catch muscle</topic><topic>Hydrogen-Ion Concentration</topic><topic>Molecular Motor Proteins - chemistry</topic><topic>Mollusca - metabolism</topic><topic>Molluscs</topic><topic>Multiprotein Complexes - chemistry</topic><topic>Muscle Proteins - chemistry</topic><topic>Muscle, Skeletal - metabolism</topic><topic>Particle Size</topic><topic>Phosphorylation</topic><topic>Protein Binding</topic><topic>Twitchin phosphorylation</topic><topic>Viscosity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Shelud’ko, Nikolai S.</creatorcontrib><creatorcontrib>Matusovskaya, Galina G.</creatorcontrib><creatorcontrib>Permyakova, Tatiana V.</creatorcontrib><creatorcontrib>Matusovsky, Oleg S.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Archives of biochemistry and biophysics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Shelud’ko, Nikolai S.</au><au>Matusovskaya, Galina G.</au><au>Permyakova, Tatiana V.</au><au>Matusovsky, Oleg S.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Twitchin, a thick-filament protein from molluscan catch muscle, interacts with F-actin in a phosphorylation-dependent way</atitle><jtitle>Archives of biochemistry and biophysics</jtitle><addtitle>Arch Biochem Biophys</addtitle><date>2004-12-15</date><risdate>2004</risdate><volume>432</volume><issue>2</issue><spage>269</spage><epage>277</epage><pages>269-277</pages><issn>0003-9861</issn><eissn>1096-0384</eissn><abstract>Twitchin belongs to the titin-like giant proteins family, it is co-localized with thick filaments in molluscan catch muscles and regulates the catch state depending on its level of phosphorylation. The mechanism by which twitchin controls the catch state remains to be established. We report for the first time the ability of twitchin to interact with F-actin. The interaction is observed at low and physiological ionic strengths, irrespective of the presence or absence of Ca
2+. It was demonstrated by viscosity and turbidity measurements, low- and high-speed co-sedimentation, and with the light-scattering particle size analysis revealing the specific twitchin–actin particles. The twitchin–actin interaction is regulated by twitchin phosphorylation: in vitro phosphorylated twitchin does not interact with F-actin. We speculate that the catch muscle twitchin might provide a mechanical link between thin and thick filaments, which contributes to catch force maintenance.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>15542066</pmid><doi>10.1016/j.abb.2004.10.006</doi><tpages>9</tpages></addata></record> |
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| ispartof | Archives of biochemistry and biophysics, 2004-12, Vol.432 (2), p.269-277 |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Actins - chemistry Actin–twitchin interaction Animals Binding Sites Caenorhabditis elegans Proteins Calmodulin-Binding Proteins - chemistry Catch muscle Hydrogen-Ion Concentration Molecular Motor Proteins - chemistry Mollusca - metabolism Molluscs Multiprotein Complexes - chemistry Muscle Proteins - chemistry Muscle, Skeletal - metabolism Particle Size Phosphorylation Protein Binding Twitchin phosphorylation Viscosity |
| title | Twitchin, a thick-filament protein from molluscan catch muscle, interacts with F-actin in a phosphorylation-dependent way |
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