Characterization of a Myosin VII MyTH/FERM Domain
A group of closely related myosins is characterized by the presence of at least one MyTH/FERM ( myosin tail homology; band 4.1, ezrin, radixin, moesin) domain in their C-terminal tails. This domain interacts with a variety of binding partners, and mutations in either the MyTH4 or the FERM domain of...
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| Veröffentlicht in: | Journal of molecular biology 2011-10, Vol.413 (1), p.17-23 |
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| creator | Moen, Rebecca J. Johnsrud, Daniel O. Thomas, David D. Titus, Margaret A. |
| description | A group of closely related myosins is characterized by the presence of at least one MyTH/FERM (
myosin
tail
homology; band
4.1,
ezrin,
radixin,
moesin) domain in their C-terminal tails. This domain interacts with a variety of binding partners, and mutations in either the MyTH4 or the FERM domain of myosin VII and myosin XV result in deafness, highlighting the functional importance of each domain. The N-terminal MyTH/FERM region of
Dictyostelium myosin VII (M7) has been isolated as a first step toward gaining insight into the function of this domain and its interaction with binding partners. The M7 MyTH4/FERM domain (MF1) binds to both actin and microtubules
in vitro, with dissociation constants of 13.7 and 1.7 μM, respectively. Gel filtration and UV spectroscopy reveal that MF1 exists as a monomer in solution and forms a well-folded, compact conformation with a high degree of secondary structure. These results indicate that MF1 forms an integrated structural domain that serves to couple actin filaments and microtubules in specific regions of the cytoskeleton. |
| doi_str_mv | 10.1016/j.jmb.2011.08.036 |
| format | Article |
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myosin
tail
homology; band
4.1,
ezrin,
radixin,
moesin) domain in their C-terminal tails. This domain interacts with a variety of binding partners, and mutations in either the MyTH4 or the FERM domain of myosin VII and myosin XV result in deafness, highlighting the functional importance of each domain. The N-terminal MyTH/FERM region of
Dictyostelium myosin VII (M7) has been isolated as a first step toward gaining insight into the function of this domain and its interaction with binding partners. The M7 MyTH4/FERM domain (MF1) binds to both actin and microtubules
in vitro, with dissociation constants of 13.7 and 1.7 μM, respectively. Gel filtration and UV spectroscopy reveal that MF1 exists as a monomer in solution and forms a well-folded, compact conformation with a high degree of secondary structure. These results indicate that MF1 forms an integrated structural domain that serves to couple actin filaments and microtubules in specific regions of the cytoskeleton.</description><identifier>ISSN: 0022-2836</identifier><identifier>EISSN: 1089-8638</identifier><identifier>DOI: 10.1016/j.jmb.2011.08.036</identifier><identifier>PMID: 21875595</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>actin ; Actins ; Actins - metabolism ; chemistry ; Chromatography, Gel ; deafness ; Dictyostelium ; Dictyostelium - chemistry ; Dictyostelium - metabolism ; dissociation ; FERM ; gel chromatography ; isolation & purification ; Kinetics ; metabolism ; microfilaments ; microtubules ; Microtubules - metabolism ; mutation ; myosin ; myosin VII ; Myosins ; Myosins - chemistry ; Myosins - isolation & purification ; Myosins - metabolism ; MyTH4 ; Protein Binding ; Protein Conformation ; Protein Structure, Tertiary ; Protozoan Proteins ; Protozoan Proteins - chemistry ; Protozoan Proteins - isolation & purification ; Protozoan Proteins - metabolism ; Spectrum Analysis ; ultraviolet-visible spectroscopy</subject><ispartof>Journal of molecular biology, 2011-10, Vol.413 (1), p.17-23</ispartof><rights>2011 Elsevier Ltd</rights><rights>Copyright © 2011 Elsevier Ltd. All rights reserved.</rights><rights>2011 Elsevier Ltd. All rights reserved. 2011</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c483t-37c804791f5c5679d56dc87265133bba6bf7cd97bc58bfed64c3e578044460953</citedby><cites>FETCH-LOGICAL-c483t-37c804791f5c5679d56dc87265133bba6bf7cd97bc58bfed64c3e578044460953</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S002228361100934X$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>230,314,776,780,881,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21875595$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Moen, Rebecca J.</creatorcontrib><creatorcontrib>Johnsrud, Daniel O.</creatorcontrib><creatorcontrib>Thomas, David D.</creatorcontrib><creatorcontrib>Titus, Margaret A.</creatorcontrib><title>Characterization of a Myosin VII MyTH/FERM Domain</title><title>Journal of molecular biology</title><addtitle>J Mol Biol</addtitle><description>A group of closely related myosins is characterized by the presence of at least one MyTH/FERM (
myosin
tail
homology; band
4.1,
ezrin,
radixin,
moesin) domain in their C-terminal tails. This domain interacts with a variety of binding partners, and mutations in either the MyTH4 or the FERM domain of myosin VII and myosin XV result in deafness, highlighting the functional importance of each domain. The N-terminal MyTH/FERM region of
Dictyostelium myosin VII (M7) has been isolated as a first step toward gaining insight into the function of this domain and its interaction with binding partners. The M7 MyTH4/FERM domain (MF1) binds to both actin and microtubules
in vitro, with dissociation constants of 13.7 and 1.7 μM, respectively. Gel filtration and UV spectroscopy reveal that MF1 exists as a monomer in solution and forms a well-folded, compact conformation with a high degree of secondary structure. These results indicate that MF1 forms an integrated structural domain that serves to couple actin filaments and microtubules in specific regions of the cytoskeleton.</description><subject>actin</subject><subject>Actins</subject><subject>Actins - metabolism</subject><subject>chemistry</subject><subject>Chromatography, Gel</subject><subject>deafness</subject><subject>Dictyostelium</subject><subject>Dictyostelium - chemistry</subject><subject>Dictyostelium - metabolism</subject><subject>dissociation</subject><subject>FERM</subject><subject>gel chromatography</subject><subject>isolation & purification</subject><subject>Kinetics</subject><subject>metabolism</subject><subject>microfilaments</subject><subject>microtubules</subject><subject>Microtubules - metabolism</subject><subject>mutation</subject><subject>myosin</subject><subject>myosin VII</subject><subject>Myosins</subject><subject>Myosins - chemistry</subject><subject>Myosins - isolation & purification</subject><subject>Myosins - metabolism</subject><subject>MyTH4</subject><subject>Protein Binding</subject><subject>Protein Conformation</subject><subject>Protein Structure, Tertiary</subject><subject>Protozoan Proteins</subject><subject>Protozoan Proteins - chemistry</subject><subject>Protozoan Proteins - isolation & purification</subject><subject>Protozoan Proteins - metabolism</subject><subject>Spectrum Analysis</subject><subject>ultraviolet-visible spectroscopy</subject><issn>0022-2836</issn><issn>1089-8638</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kVtLwzAYhoMoOg8_wBvpnd60fmmaQxEEmdMNFEHU25CmqctYG026wfz1RqeiN94kgTzvy5c8CB1iyDBgdjrLZm2V5YBxBiIDwjbQAIMoU8GI2EQDgDxPc0HYDtoNYQYAlBRiG-3kWHBKSzpAeDhVXuneePumeuu6xDWJSm5XLtgueZpM4vFhfHo1ur9NLl2rbLePtho1D-bga99Dj1ejh-E4vbm7ngwvblJdCNKnhGsBBS9xQzVlvKwpq7XgOaOYkKpSrGq4rkteaSqqxtSs0MRQHjNFwaCkZA-dr3tfFlVram263qu5fPG2VX4lnbLy701np_LZLSVhwFlexILjrwLvXhcm9LK1QZv5XHXGLYIUJRU0LmUkT_4lMeM5CFJ8ToXXqPYuBG-an4EwyA8pciajFPkhRYKQUUrMHP1-yU_i20IEztaAif-5tMbLoK3ptKmtN7qXtbP_1L8DXDKa3A</recordid><startdate>20111014</startdate><enddate>20111014</enddate><creator>Moen, Rebecca J.</creator><creator>Johnsrud, Daniel O.</creator><creator>Thomas, David D.</creator><creator>Titus, Margaret A.</creator><general>Elsevier Ltd</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>7S9</scope><scope>L.6</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20111014</creationdate><title>Characterization of a Myosin VII MyTH/FERM Domain</title><author>Moen, Rebecca J. ; Johnsrud, Daniel O. ; Thomas, David D. ; Titus, Margaret A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c483t-37c804791f5c5679d56dc87265133bba6bf7cd97bc58bfed64c3e578044460953</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>actin</topic><topic>Actins</topic><topic>Actins - metabolism</topic><topic>chemistry</topic><topic>Chromatography, Gel</topic><topic>deafness</topic><topic>Dictyostelium</topic><topic>Dictyostelium - chemistry</topic><topic>Dictyostelium - metabolism</topic><topic>dissociation</topic><topic>FERM</topic><topic>gel chromatography</topic><topic>isolation & purification</topic><topic>Kinetics</topic><topic>metabolism</topic><topic>microfilaments</topic><topic>microtubules</topic><topic>Microtubules - metabolism</topic><topic>mutation</topic><topic>myosin</topic><topic>myosin VII</topic><topic>Myosins</topic><topic>Myosins - chemistry</topic><topic>Myosins - isolation & purification</topic><topic>Myosins - metabolism</topic><topic>MyTH4</topic><topic>Protein Binding</topic><topic>Protein Conformation</topic><topic>Protein Structure, Tertiary</topic><topic>Protozoan Proteins</topic><topic>Protozoan Proteins - chemistry</topic><topic>Protozoan Proteins - isolation & purification</topic><topic>Protozoan Proteins - metabolism</topic><topic>Spectrum Analysis</topic><topic>ultraviolet-visible spectroscopy</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Moen, Rebecca J.</creatorcontrib><creatorcontrib>Johnsrud, Daniel O.</creatorcontrib><creatorcontrib>Thomas, David D.</creatorcontrib><creatorcontrib>Titus, Margaret A.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>AGRICOLA</collection><collection>AGRICOLA - Academic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Journal of molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Moen, Rebecca J.</au><au>Johnsrud, Daniel O.</au><au>Thomas, David D.</au><au>Titus, Margaret A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of a Myosin VII MyTH/FERM Domain</atitle><jtitle>Journal of molecular biology</jtitle><addtitle>J Mol Biol</addtitle><date>2011-10-14</date><risdate>2011</risdate><volume>413</volume><issue>1</issue><spage>17</spage><epage>23</epage><pages>17-23</pages><issn>0022-2836</issn><eissn>1089-8638</eissn><abstract>A group of closely related myosins is characterized by the presence of at least one MyTH/FERM (
myosin
tail
homology; band
4.1,
ezrin,
radixin,
moesin) domain in their C-terminal tails. This domain interacts with a variety of binding partners, and mutations in either the MyTH4 or the FERM domain of myosin VII and myosin XV result in deafness, highlighting the functional importance of each domain. The N-terminal MyTH/FERM region of
Dictyostelium myosin VII (M7) has been isolated as a first step toward gaining insight into the function of this domain and its interaction with binding partners. The M7 MyTH4/FERM domain (MF1) binds to both actin and microtubules
in vitro, with dissociation constants of 13.7 and 1.7 μM, respectively. Gel filtration and UV spectroscopy reveal that MF1 exists as a monomer in solution and forms a well-folded, compact conformation with a high degree of secondary structure. These results indicate that MF1 forms an integrated structural domain that serves to couple actin filaments and microtubules in specific regions of the cytoskeleton.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>21875595</pmid><doi>10.1016/j.jmb.2011.08.036</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | actin Actins Actins - metabolism chemistry Chromatography, Gel deafness Dictyostelium Dictyostelium - chemistry Dictyostelium - metabolism dissociation FERM gel chromatography isolation & purification Kinetics metabolism microfilaments microtubules Microtubules - metabolism mutation myosin myosin VII Myosins Myosins - chemistry Myosins - isolation & purification Myosins - metabolism MyTH4 Protein Binding Protein Conformation Protein Structure, Tertiary Protozoan Proteins Protozoan Proteins - chemistry Protozoan Proteins - isolation & purification Protozoan Proteins - metabolism Spectrum Analysis ultraviolet-visible spectroscopy |
| title | Characterization of a Myosin VII MyTH/FERM Domain |
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