A lasp family protein of Ciona intestinalis
Lasp-1 and lasp-2 are actin-binding proteins that contain a LIM domain, nebulin repeats, and an SH3 domain and they are significantly conserved in mammalian and avian. Lasp-1 is widely expressed in nonmuscle tissues and lasp-2 is specifically expressed in the brain. Genes encoding proteins homologou...
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| Veröffentlicht in: | Biochimica et biophysica acta 2008, Vol.1779 (1), p.51-59 |
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| container_title | Biochimica et biophysica acta |
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| creator | Terasaki, Asako G. Hiruta, Jin Suzuki, Junko Sakamoto, Sachiko Nishioka, Tatsuji Suzuki, Hiroshi Ohashi, Kazuyo Azumi, Kaoru Ogasawara, Michio |
| description | Lasp-1 and lasp-2 are actin-binding proteins that contain a LIM domain, nebulin repeats, and an SH3 domain and they are significantly conserved in mammalian and avian. Lasp-1 is widely expressed in nonmuscle tissues and lasp-2 is specifically expressed in the brain. Genes encoding proteins homologous to lasp-1 and lasp-2 were deposited in the genome/cDNA database of invertebrates such as sea urchins, nematodes, and insects; however, function of their proteins have not been studied in detail.
In this study, we analyzed the gene structure, actin-binding activity, and expression of the lasp protein of the ascidian
Ciona intestinalis (
Ci lasp). A single gene encoding lasp protein was found in the ascidian, and the amino acid sequences of
Ci lasp and other invertebrate lasp proteins exhibited similarity to vertebrate lasp-1 and lasp-2 to the same extent. A part of the exon–intron boundaries was conserved between the vertebrate
lasp-1, the vertebrate
lasp-2 and the invertebrate
lasp genes.
Ci lasp exhibited actin-binding activity in a co-sedimentation assay.
In situ hybridization revealed that the expression of
Ci lasp mRNA was apparent in nervous system of early embryos and was detected in various tissues in young adults. This suggests that the functions of invertebrate lasp proteins might include the functions of vertebrate lasp-1 and lasp-2. |
| doi_str_mv | 10.1016/j.bbagrm.2007.08.001 |
| format | Article |
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In this study, we analyzed the gene structure, actin-binding activity, and expression of the lasp protein of the ascidian
Ciona intestinalis (
Ci lasp). A single gene encoding lasp protein was found in the ascidian, and the amino acid sequences of
Ci lasp and other invertebrate lasp proteins exhibited similarity to vertebrate lasp-1 and lasp-2 to the same extent. A part of the exon–intron boundaries was conserved between the vertebrate
lasp-1, the vertebrate
lasp-2 and the invertebrate
lasp genes.
Ci lasp exhibited actin-binding activity in a co-sedimentation assay.
In situ hybridization revealed that the expression of
Ci lasp mRNA was apparent in nervous system of early embryos and was detected in various tissues in young adults. This suggests that the functions of invertebrate lasp proteins might include the functions of vertebrate lasp-1 and lasp-2.</description><identifier>ISSN: 1874-9399</identifier><identifier>ISSN: 0006-3002</identifier><identifier>EISSN: 1876-4320</identifier><identifier>DOI: 10.1016/j.bbagrm.2007.08.001</identifier><identifier>PMID: 18078837</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>Actin-binding ; Amino Acid Sequence ; Animals ; Ascidian ; Base Sequence ; Ciona intestinalis ; Ciona intestinalis - embryology ; Ciona intestinalis - genetics ; Ciona intestinalis - metabolism ; Cloning, Molecular ; DNA Primers - genetics ; Echinoidea ; Female ; Gene Expression ; In Situ Hybridization ; Lasp ; LIM domain ; Male ; Microfilament Proteins - chemistry ; Microfilament Proteins - genetics ; Microfilament Proteins - metabolism ; Molecular Sequence Data ; Nebulin repeat ; Nematoda ; Oligonucleotide Array Sequence Analysis ; Phylogeny ; Recombinant Proteins - chemistry ; Recombinant Proteins - genetics ; Recombinant Proteins - metabolism ; Sequence Homology, Amino Acid ; SH3 domain ; src Homology Domains</subject><ispartof>Biochimica et biophysica acta, 2008, Vol.1779 (1), p.51-59</ispartof><rights>2007 Elsevier B.V.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c488t-bae894b2502efdf623c91f93de299a795009a78e169dff2899fe1d78e51eb30d3</citedby><cites>FETCH-LOGICAL-c488t-bae894b2502efdf623c91f93de299a795009a78e169dff2899fe1d78e51eb30d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.bbagrm.2007.08.001$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,4024,27923,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18078837$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Terasaki, Asako G.</creatorcontrib><creatorcontrib>Hiruta, Jin</creatorcontrib><creatorcontrib>Suzuki, Junko</creatorcontrib><creatorcontrib>Sakamoto, Sachiko</creatorcontrib><creatorcontrib>Nishioka, Tatsuji</creatorcontrib><creatorcontrib>Suzuki, Hiroshi</creatorcontrib><creatorcontrib>Ohashi, Kazuyo</creatorcontrib><creatorcontrib>Azumi, Kaoru</creatorcontrib><creatorcontrib>Ogasawara, Michio</creatorcontrib><title>A lasp family protein of Ciona intestinalis</title><title>Biochimica et biophysica acta</title><addtitle>Biochim Biophys Acta</addtitle><description>Lasp-1 and lasp-2 are actin-binding proteins that contain a LIM domain, nebulin repeats, and an SH3 domain and they are significantly conserved in mammalian and avian. Lasp-1 is widely expressed in nonmuscle tissues and lasp-2 is specifically expressed in the brain. Genes encoding proteins homologous to lasp-1 and lasp-2 were deposited in the genome/cDNA database of invertebrates such as sea urchins, nematodes, and insects; however, function of their proteins have not been studied in detail.
In this study, we analyzed the gene structure, actin-binding activity, and expression of the lasp protein of the ascidian
Ciona intestinalis (
Ci lasp). A single gene encoding lasp protein was found in the ascidian, and the amino acid sequences of
Ci lasp and other invertebrate lasp proteins exhibited similarity to vertebrate lasp-1 and lasp-2 to the same extent. A part of the exon–intron boundaries was conserved between the vertebrate
lasp-1, the vertebrate
lasp-2 and the invertebrate
lasp genes.
Ci lasp exhibited actin-binding activity in a co-sedimentation assay.
In situ hybridization revealed that the expression of
Ci lasp mRNA was apparent in nervous system of early embryos and was detected in various tissues in young adults. This suggests that the functions of invertebrate lasp proteins might include the functions of vertebrate lasp-1 and lasp-2.</description><subject>Actin-binding</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Ascidian</subject><subject>Base Sequence</subject><subject>Ciona intestinalis</subject><subject>Ciona intestinalis - embryology</subject><subject>Ciona intestinalis - genetics</subject><subject>Ciona intestinalis - metabolism</subject><subject>Cloning, Molecular</subject><subject>DNA Primers - genetics</subject><subject>Echinoidea</subject><subject>Female</subject><subject>Gene Expression</subject><subject>In Situ Hybridization</subject><subject>Lasp</subject><subject>LIM domain</subject><subject>Male</subject><subject>Microfilament Proteins - chemistry</subject><subject>Microfilament Proteins - genetics</subject><subject>Microfilament Proteins - metabolism</subject><subject>Molecular Sequence Data</subject><subject>Nebulin repeat</subject><subject>Nematoda</subject><subject>Oligonucleotide Array Sequence Analysis</subject><subject>Phylogeny</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - metabolism</subject><subject>Sequence Homology, Amino Acid</subject><subject>SH3 domain</subject><subject>src Homology Domains</subject><issn>1874-9399</issn><issn>0006-3002</issn><issn>1876-4320</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkE1LAzEQhoMotlb_gcievMiuk2S7SS5CKX5BwYueQ3YzkZT9qJut0H9v6ha8qacZhuedGR5CLilkFGhxu87K0rz3TcYARAYyA6BHZEqlKNKcMzj-7vNUcaUm5CyENUBBI3xKJlSCkJKLKblZJLUJm8SZxte7ZNN3A_o26Vyy9F1rEt8OGAbfmtqHc3LiTB3w4lBn5O3h_nX5lK5eHp-Xi1Va5VIOaWlQqrxkc2DorCsYrxR1iltkShmh5gCxSKSFss4xqZRDauNgTrHkYPmMXI974zcf23heNz5UWNemxW4btABGBRP0T5AqkTMG8l8gcJpHMB_Bqu9C6NHpTe8b0-80Bb3Xrtd61K732jVIHbXH2NVh_7Zs0P6EDp4jcDcCGL19eux1qDy2FVrfYzVo2_nfL3wBAAqTgQ</recordid><startdate>2008</startdate><enddate>2008</enddate><creator>Terasaki, Asako G.</creator><creator>Hiruta, Jin</creator><creator>Suzuki, Junko</creator><creator>Sakamoto, Sachiko</creator><creator>Nishioka, Tatsuji</creator><creator>Suzuki, Hiroshi</creator><creator>Ohashi, Kazuyo</creator><creator>Azumi, Kaoru</creator><creator>Ogasawara, Michio</creator><general>Elsevier B.V</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>7TM</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>2008</creationdate><title>A lasp family protein of Ciona intestinalis</title><author>Terasaki, Asako G. ; Hiruta, Jin ; Suzuki, Junko ; Sakamoto, Sachiko ; Nishioka, Tatsuji ; Suzuki, Hiroshi ; Ohashi, Kazuyo ; Azumi, Kaoru ; Ogasawara, Michio</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c488t-bae894b2502efdf623c91f93de299a795009a78e169dff2899fe1d78e51eb30d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Actin-binding</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Ascidian</topic><topic>Base Sequence</topic><topic>Ciona intestinalis</topic><topic>Ciona intestinalis - embryology</topic><topic>Ciona intestinalis - genetics</topic><topic>Ciona intestinalis - metabolism</topic><topic>Cloning, Molecular</topic><topic>DNA Primers - genetics</topic><topic>Echinoidea</topic><topic>Female</topic><topic>Gene Expression</topic><topic>In Situ Hybridization</topic><topic>Lasp</topic><topic>LIM domain</topic><topic>Male</topic><topic>Microfilament Proteins - chemistry</topic><topic>Microfilament Proteins - genetics</topic><topic>Microfilament Proteins - metabolism</topic><topic>Molecular Sequence Data</topic><topic>Nebulin repeat</topic><topic>Nematoda</topic><topic>Oligonucleotide Array Sequence Analysis</topic><topic>Phylogeny</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - metabolism</topic><topic>Sequence Homology, Amino Acid</topic><topic>SH3 domain</topic><topic>src Homology Domains</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Terasaki, Asako G.</creatorcontrib><creatorcontrib>Hiruta, Jin</creatorcontrib><creatorcontrib>Suzuki, Junko</creatorcontrib><creatorcontrib>Sakamoto, Sachiko</creatorcontrib><creatorcontrib>Nishioka, Tatsuji</creatorcontrib><creatorcontrib>Suzuki, Hiroshi</creatorcontrib><creatorcontrib>Ohashi, Kazuyo</creatorcontrib><creatorcontrib>Azumi, Kaoru</creatorcontrib><creatorcontrib>Ogasawara, Michio</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Biochimica et biophysica acta</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Terasaki, Asako G.</au><au>Hiruta, Jin</au><au>Suzuki, Junko</au><au>Sakamoto, Sachiko</au><au>Nishioka, Tatsuji</au><au>Suzuki, Hiroshi</au><au>Ohashi, Kazuyo</au><au>Azumi, Kaoru</au><au>Ogasawara, Michio</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A lasp family protein of Ciona intestinalis</atitle><jtitle>Biochimica et biophysica acta</jtitle><addtitle>Biochim Biophys Acta</addtitle><date>2008</date><risdate>2008</risdate><volume>1779</volume><issue>1</issue><spage>51</spage><epage>59</epage><pages>51-59</pages><issn>1874-9399</issn><issn>0006-3002</issn><eissn>1876-4320</eissn><abstract>Lasp-1 and lasp-2 are actin-binding proteins that contain a LIM domain, nebulin repeats, and an SH3 domain and they are significantly conserved in mammalian and avian. Lasp-1 is widely expressed in nonmuscle tissues and lasp-2 is specifically expressed in the brain. Genes encoding proteins homologous to lasp-1 and lasp-2 were deposited in the genome/cDNA database of invertebrates such as sea urchins, nematodes, and insects; however, function of their proteins have not been studied in detail.
In this study, we analyzed the gene structure, actin-binding activity, and expression of the lasp protein of the ascidian
Ciona intestinalis (
Ci lasp). A single gene encoding lasp protein was found in the ascidian, and the amino acid sequences of
Ci lasp and other invertebrate lasp proteins exhibited similarity to vertebrate lasp-1 and lasp-2 to the same extent. A part of the exon–intron boundaries was conserved between the vertebrate
lasp-1, the vertebrate
lasp-2 and the invertebrate
lasp genes.
Ci lasp exhibited actin-binding activity in a co-sedimentation assay.
In situ hybridization revealed that the expression of
Ci lasp mRNA was apparent in nervous system of early embryos and was detected in various tissues in young adults. This suggests that the functions of invertebrate lasp proteins might include the functions of vertebrate lasp-1 and lasp-2.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>18078837</pmid><doi>10.1016/j.bbagrm.2007.08.001</doi><tpages>9</tpages></addata></record> |
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| ispartof | Biochimica et biophysica acta, 2008, Vol.1779 (1), p.51-59 |
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| language | eng |
| recordid | cdi_proquest_miscellaneous_19742208 |
| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | Actin-binding Amino Acid Sequence Animals Ascidian Base Sequence Ciona intestinalis Ciona intestinalis - embryology Ciona intestinalis - genetics Ciona intestinalis - metabolism Cloning, Molecular DNA Primers - genetics Echinoidea Female Gene Expression In Situ Hybridization Lasp LIM domain Male Microfilament Proteins - chemistry Microfilament Proteins - genetics Microfilament Proteins - metabolism Molecular Sequence Data Nebulin repeat Nematoda Oligonucleotide Array Sequence Analysis Phylogeny Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism Sequence Homology, Amino Acid SH3 domain src Homology Domains |
| title | A lasp family protein of Ciona intestinalis |
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