Arabidopsis CROLIN1, a Novel Plant Actin-binding Protein, Functions in Cross-linking and Stabilizing Actin Filaments
Higher order actin filament structures are necessary for cytoplasmic streaming, organelle movement, and other physiological processes. However, the mechanism by which the higher order cytoskeleton is formed in plants remains unknown. In this study, we identified a novel actin-cross-linking protein f...
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| Veröffentlicht in: | The Journal of biological chemistry 2013-11, Vol.288 (45), p.32277-32288 |
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| creator | Jia, Honglei Li, Jisheng Zhu, Jingen Fan, Tingting Qian, Dong Zhou, Yuelong Wang, Jiaojiao Ren, Haiyun Xiang, Yun An, Lizhe |
| description | Higher order actin filament structures are necessary for cytoplasmic streaming, organelle movement, and other physiological processes. However, the mechanism by which the higher order cytoskeleton is formed in plants remains unknown. In this study, we identified a novel actin-cross-linking protein family (named CROLIN) that is well conserved only in the plant kingdom. There are six isovariants of CROLIN in the Arabidopsis genome, with CROLIN1 specifically expressed in pollen. In vitro biochemical analyses showed that CROLIN1 is a novel actin-cross-linking protein with binding and stabilizing activities. Remarkably, CROLIN1 can cross-link actin bundles into actin networks. CROLIN1 loss of function induces pollen germination and pollen tube growth hypersensitive to latrunculin B. All of these results demonstrate that CROLIN1 may play an important role in stabilizing and remodeling actin filaments by binding to and cross-linking actin filaments.
Background: Higher order actin filament structures are involved in many cellular processes.
Results:Arabidopsis CROLIN1 contains a predicted actin-cross-linking domain and shows F-actin binding, cross-linking, and stabilizing activities in vitro.
Conclusion: CROLIN1 functions as an actin-binding and cross-linking protein.
Significance: CROLIN1 is a previously undiscovered plant actin-cross-linking protein. |
| doi_str_mv | 10.1074/jbc.M113.483594 |
| format | Article |
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Background: Higher order actin filament structures are involved in many cellular processes.
Results:Arabidopsis CROLIN1 contains a predicted actin-cross-linking domain and shows F-actin binding, cross-linking, and stabilizing activities in vitro.
Conclusion: CROLIN1 functions as an actin-binding and cross-linking protein.
Significance: CROLIN1 is a previously undiscovered plant actin-cross-linking protein.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M113.483594</identifier><identifier>PMID: 24072702</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Actin ; Actin-cross-linking Protein ; Actins - genetics ; Actins - metabolism ; Amino Acid Sequence ; Arabidopsis ; Arabidopsis - genetics ; Arabidopsis - metabolism ; Arabidopsis Proteins - genetics ; Arabidopsis Proteins - metabolism ; Cell Polarity ; CROLIN1 ; Microfilament Proteins - genetics ; Microfilament Proteins - metabolism ; Molecular Sequence Data ; Novel Actin-binding Protein ; Plant ; Plant Biochemistry ; Plant Biology ; Pollen Tube - genetics ; Pollen Tube - metabolism</subject><ispartof>The Journal of biological chemistry, 2013-11, Vol.288 (45), p.32277-32288</ispartof><rights>2013 © 2013 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><rights>2013 by The American Society for Biochemistry and Molecular Biology, Inc. 2013</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c555t-87c6669a479d0aba4d060744ea5fddf99ff19337c468d1c0e923e31eebb3a4463</citedby><cites>FETCH-LOGICAL-c555t-87c6669a479d0aba4d060744ea5fddf99ff19337c468d1c0e923e31eebb3a4463</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3820865/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3820865/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,724,777,781,882,27905,27906,53772,53774</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24072702$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Jia, Honglei</creatorcontrib><creatorcontrib>Li, Jisheng</creatorcontrib><creatorcontrib>Zhu, Jingen</creatorcontrib><creatorcontrib>Fan, Tingting</creatorcontrib><creatorcontrib>Qian, Dong</creatorcontrib><creatorcontrib>Zhou, Yuelong</creatorcontrib><creatorcontrib>Wang, Jiaojiao</creatorcontrib><creatorcontrib>Ren, Haiyun</creatorcontrib><creatorcontrib>Xiang, Yun</creatorcontrib><creatorcontrib>An, Lizhe</creatorcontrib><title>Arabidopsis CROLIN1, a Novel Plant Actin-binding Protein, Functions in Cross-linking and Stabilizing Actin Filaments</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Higher order actin filament structures are necessary for cytoplasmic streaming, organelle movement, and other physiological processes. However, the mechanism by which the higher order cytoskeleton is formed in plants remains unknown. In this study, we identified a novel actin-cross-linking protein family (named CROLIN) that is well conserved only in the plant kingdom. There are six isovariants of CROLIN in the Arabidopsis genome, with CROLIN1 specifically expressed in pollen. In vitro biochemical analyses showed that CROLIN1 is a novel actin-cross-linking protein with binding and stabilizing activities. Remarkably, CROLIN1 can cross-link actin bundles into actin networks. CROLIN1 loss of function induces pollen germination and pollen tube growth hypersensitive to latrunculin B. All of these results demonstrate that CROLIN1 may play an important role in stabilizing and remodeling actin filaments by binding to and cross-linking actin filaments.
Background: Higher order actin filament structures are involved in many cellular processes.
Results:Arabidopsis CROLIN1 contains a predicted actin-cross-linking domain and shows F-actin binding, cross-linking, and stabilizing activities in vitro.
Conclusion: CROLIN1 functions as an actin-binding and cross-linking protein.
Significance: CROLIN1 is a previously undiscovered plant actin-cross-linking protein.</description><subject>Actin</subject><subject>Actin-cross-linking Protein</subject><subject>Actins - genetics</subject><subject>Actins - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Arabidopsis</subject><subject>Arabidopsis - genetics</subject><subject>Arabidopsis - metabolism</subject><subject>Arabidopsis Proteins - genetics</subject><subject>Arabidopsis Proteins - metabolism</subject><subject>Cell Polarity</subject><subject>CROLIN1</subject><subject>Microfilament Proteins - genetics</subject><subject>Microfilament Proteins - metabolism</subject><subject>Molecular Sequence Data</subject><subject>Novel Actin-binding Protein</subject><subject>Plant</subject><subject>Plant Biochemistry</subject><subject>Plant Biology</subject><subject>Pollen Tube - genetics</subject><subject>Pollen Tube - metabolism</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kUtvEzEURi0EoqGwZoe8ZNFJ_ZwZb5CiiECl9CEeEjvLY98pLhM7tSeR4NfjIW1FF_XGsu7xufb9EHpLyZySRpzedHZ-Timfi5ZLJZ6hGSUtr7ikP56jGSGMVorJ9gi9yvmGlCUUfYmOmCANawiboXGRTOdd3Gaf8fLL5frsgp5ggy_iHgZ8NZgw4oUdfag6H5wP1_gqxRF8OMGrXSiFGDL2AS9TzLkafPg1MSY4_HUs4sH_mc7_DHjlB7OBMObX6EVvhgxv7vZj9H318dvyc7W-_HS2XKwrK6Ucq7axdV0rIxrliOmMcKQunxZgZO9cr1TfU8V5Y0XdOmoJKMaBU4Cu40aImh-jDwfvdtdtwNnSO5lBb5PfmPRbR-P140rwP_V13GveMtLWsgje3wlSvN1BHvXGZwtDGQvEXdZUSEKbRjJW0NMDaqdJJOgf2lCip6x0yUpPWelDVuXGu_9f98Dfh1MAdQCgzGjvIelsPQQLziewo3bRPyn_C_68pJI</recordid><startdate>20131108</startdate><enddate>20131108</enddate><creator>Jia, Honglei</creator><creator>Li, Jisheng</creator><creator>Zhu, Jingen</creator><creator>Fan, Tingting</creator><creator>Qian, Dong</creator><creator>Zhou, Yuelong</creator><creator>Wang, Jiaojiao</creator><creator>Ren, Haiyun</creator><creator>Xiang, Yun</creator><creator>An, Lizhe</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>7X8</scope><scope>5PM</scope></search><sort><creationdate>20131108</creationdate><title>Arabidopsis CROLIN1, a Novel Plant Actin-binding Protein, Functions in Cross-linking and Stabilizing Actin Filaments</title><author>Jia, Honglei ; Li, Jisheng ; Zhu, Jingen ; Fan, Tingting ; Qian, Dong ; Zhou, Yuelong ; Wang, Jiaojiao ; Ren, Haiyun ; Xiang, Yun ; An, Lizhe</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c555t-87c6669a479d0aba4d060744ea5fddf99ff19337c468d1c0e923e31eebb3a4463</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Actin</topic><topic>Actin-cross-linking Protein</topic><topic>Actins - genetics</topic><topic>Actins - metabolism</topic><topic>Amino Acid Sequence</topic><topic>Arabidopsis</topic><topic>Arabidopsis - genetics</topic><topic>Arabidopsis - metabolism</topic><topic>Arabidopsis Proteins - genetics</topic><topic>Arabidopsis Proteins - metabolism</topic><topic>Cell Polarity</topic><topic>CROLIN1</topic><topic>Microfilament Proteins - genetics</topic><topic>Microfilament Proteins - metabolism</topic><topic>Molecular Sequence Data</topic><topic>Novel Actin-binding Protein</topic><topic>Plant</topic><topic>Plant Biochemistry</topic><topic>Plant Biology</topic><topic>Pollen Tube - genetics</topic><topic>Pollen Tube - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Jia, Honglei</creatorcontrib><creatorcontrib>Li, Jisheng</creatorcontrib><creatorcontrib>Zhu, Jingen</creatorcontrib><creatorcontrib>Fan, Tingting</creatorcontrib><creatorcontrib>Qian, Dong</creatorcontrib><creatorcontrib>Zhou, Yuelong</creatorcontrib><creatorcontrib>Wang, Jiaojiao</creatorcontrib><creatorcontrib>Ren, Haiyun</creatorcontrib><creatorcontrib>Xiang, Yun</creatorcontrib><creatorcontrib>An, Lizhe</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>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Jia, Honglei</au><au>Li, Jisheng</au><au>Zhu, Jingen</au><au>Fan, Tingting</au><au>Qian, Dong</au><au>Zhou, Yuelong</au><au>Wang, Jiaojiao</au><au>Ren, Haiyun</au><au>Xiang, Yun</au><au>An, Lizhe</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Arabidopsis CROLIN1, a Novel Plant Actin-binding Protein, Functions in Cross-linking and Stabilizing Actin Filaments</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2013-11-08</date><risdate>2013</risdate><volume>288</volume><issue>45</issue><spage>32277</spage><epage>32288</epage><pages>32277-32288</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Higher order actin filament structures are necessary for cytoplasmic streaming, organelle movement, and other physiological processes. However, the mechanism by which the higher order cytoskeleton is formed in plants remains unknown. In this study, we identified a novel actin-cross-linking protein family (named CROLIN) that is well conserved only in the plant kingdom. There are six isovariants of CROLIN in the Arabidopsis genome, with CROLIN1 specifically expressed in pollen. In vitro biochemical analyses showed that CROLIN1 is a novel actin-cross-linking protein with binding and stabilizing activities. Remarkably, CROLIN1 can cross-link actin bundles into actin networks. CROLIN1 loss of function induces pollen germination and pollen tube growth hypersensitive to latrunculin B. All of these results demonstrate that CROLIN1 may play an important role in stabilizing and remodeling actin filaments by binding to and cross-linking actin filaments.
Background: Higher order actin filament structures are involved in many cellular processes.
Results:Arabidopsis CROLIN1 contains a predicted actin-cross-linking domain and shows F-actin binding, cross-linking, and stabilizing activities in vitro.
Conclusion: CROLIN1 functions as an actin-binding and cross-linking protein.
Significance: CROLIN1 is a previously undiscovered plant actin-cross-linking protein.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>24072702</pmid><doi>10.1074/jbc.M113.483594</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; Alma/SFX Local Collection |
| subjects | Actin Actin-cross-linking Protein Actins - genetics Actins - metabolism Amino Acid Sequence Arabidopsis Arabidopsis - genetics Arabidopsis - metabolism Arabidopsis Proteins - genetics Arabidopsis Proteins - metabolism Cell Polarity CROLIN1 Microfilament Proteins - genetics Microfilament Proteins - metabolism Molecular Sequence Data Novel Actin-binding Protein Plant Plant Biochemistry Plant Biology Pollen Tube - genetics Pollen Tube - metabolism |
| title | Arabidopsis CROLIN1, a Novel Plant Actin-binding Protein, Functions in Cross-linking and Stabilizing Actin Filaments |
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