Two types of transmembrane homomeric interactions in the integrin receptor family are evolutionarily conserved
Identifieur interne : 002146 ( Main/Exploration ); précédent : 002145; suivant : 002147Two types of transmembrane homomeric interactions in the integrin receptor family are evolutionarily conserved
Auteurs : Xin Lin ; Suet Mien Tan ; S. K. Alex Law ; Jaume TorresSource :
- Proteins [ 0887-3585 ] ; 2006.
Abstract
Integrins are heterodimers, but recent in vitro and in vivo experiments suggest that they are also able to associate through their transmembrane domains to form homomeric interactions. Two fundamental questions are the biological relevance of these aggregates and their form of interaction in the membrane domain. Although in vitro experiments have shown the involvement of a GxxxG‐like motif, several crosslinking in vivo data are consistent with an almost opposite form of interaction between the transmembrane α‐helices. In the present work, we have explored these two questions using molecular dynamics simulations for all available integrin types. We have tested the hypothesis that homomeric interactions are evolutionary conserved, and essential for the cell, using conservative substitutions to filter out nonnative interactions. Our results show that two models, one involving a GxxxG‐like motif (model I) and an almost opposite form of interaction (model II) are conserved across all α and β integrin types, both in homodimers and homotrimers, with different specificities. No conserved interaction was found for homotetramers. Our results are completely independent from experimental data, both during molecular dynamics simulations and in the selection of the correct models. We rationalize previous seemingly conflicting findings regarding the nature of integrin interhelical homomeric interactions. Proteins 2006. © 2006 Wiley‐Liss, Inc.
Url:
DOI: 10.1002/prot.20882
PubMed: 16444740
PubMed Central: 7168044
Affiliations:
Links toward previous steps (curation, corpus...)
- to stream Pmc, to step Corpus: 000796
- to stream Pmc, to step Curation: 000796
- to stream Pmc, to step Checkpoint: 000932
- to stream Ncbi, to step Merge: 000186
- to stream Ncbi, to step Curation: 000186
- to stream Ncbi, to step Checkpoint: 000186
- to stream Main, to step Merge: 002151
- to stream Main, to step Curation: 002146
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Two types of transmembrane homomeric interactions in the integrin receptor family are evolutionarily conserved</title><author><name sortKey="Lin, Xin" sort="Lin, Xin" uniqKey="Lin X" first="Xin" last="Lin">Xin Lin</name><affiliation><nlm:aff id="af1"></nlm:aff></affiliation></author><author><name sortKey="Tan, Suet Mien" sort="Tan, Suet Mien" uniqKey="Tan S" first="Suet Mien" last="Tan">Suet Mien Tan</name><affiliation><nlm:aff id="af1"></nlm:aff></affiliation></author><author><name sortKey="Law, S K Alex" sort="Law, S K Alex" uniqKey="Law S" first="S. K. Alex" last="Law">S. K. Alex Law</name><affiliation><nlm:aff id="af1"></nlm:aff></affiliation></author><author><name sortKey="Torres, Jaume" sort="Torres, Jaume" uniqKey="Torres J" first="Jaume" last="Torres">Jaume Torres</name><affiliation><nlm:aff id="af1"></nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">16444740</idno><idno type="pmc">7168044</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7168044</idno><idno type="RBID">PMC:7168044</idno><idno type="doi">10.1002/prot.20882</idno><date when="2006">2006</date><idno type="wicri:Area/Pmc/Corpus">000796</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000796</idno><idno type="wicri:Area/Pmc/Curation">000796</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">000796</idno><idno type="wicri:Area/Pmc/Checkpoint">000932</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Checkpoint">000932</idno><idno type="wicri:Area/Ncbi/Merge">000186</idno><idno type="wicri:Area/Ncbi/Curation">000186</idno><idno type="wicri:Area/Ncbi/Checkpoint">000186</idno><idno type="wicri:doubleKey">0887-3585:2006:Lin X:two:types:of</idno><idno type="wicri:Area/Main/Merge">002151</idno><idno type="wicri:Area/Main/Curation">002146</idno><idno type="wicri:Area/Main/Exploration">002146</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Two types of transmembrane homomeric interactions in the integrin receptor family are evolutionarily conserved</title><author><name sortKey="Lin, Xin" sort="Lin, Xin" uniqKey="Lin X" first="Xin" last="Lin">Xin Lin</name><affiliation><nlm:aff id="af1"></nlm:aff></affiliation></author><author><name sortKey="Tan, Suet Mien" sort="Tan, Suet Mien" uniqKey="Tan S" first="Suet Mien" last="Tan">Suet Mien Tan</name><affiliation><nlm:aff id="af1"></nlm:aff></affiliation></author><author><name sortKey="Law, S K Alex" sort="Law, S K Alex" uniqKey="Law S" first="S. K. Alex" last="Law">S. K. Alex Law</name><affiliation><nlm:aff id="af1"></nlm:aff></affiliation></author><author><name sortKey="Torres, Jaume" sort="Torres, Jaume" uniqKey="Torres J" first="Jaume" last="Torres">Jaume Torres</name><affiliation><nlm:aff id="af1"></nlm:aff></affiliation></author></analytic><series><title level="j">Proteins</title><idno type="ISSN">0887-3585</idno><idno type="eISSN">1097-0134</idno><imprint><date when="2006">2006</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><title>Abstract</title><p>Integrins are heterodimers, but recent in vitro and in vivo experiments suggest that they are also able to associate through their transmembrane domains to form homomeric interactions. Two fundamental questions are the biological relevance of these aggregates and their form of interaction in the membrane domain. Although in vitro experiments have shown the involvement of a GxxxG‐like motif, several crosslinking in vivo data are consistent with an almost opposite form of interaction between the transmembrane α‐helices. In the present work, we have explored these two questions using molecular dynamics simulations for all available integrin types. We have tested the hypothesis that homomeric interactions are evolutionary conserved, and essential for the cell, using conservative substitutions to filter out nonnative interactions. Our results show that two models, one involving a GxxxG‐like motif (model I) and an almost opposite form of interaction (model II) are conserved across all α and β integrin types, both in homodimers and homotrimers, with different specificities. No conserved interaction was found for homotetramers. Our results are completely independent from experimental data, both during molecular dynamics simulations and in the selection of the correct models. We rationalize previous seemingly conflicting findings regarding the nature of integrin interhelical homomeric interactions. Proteins 2006. © 2006 Wiley‐Liss, Inc.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct></biblStruct><biblStruct><analytic><author><name sortKey="Kreis, T" uniqKey="Kreis T">T Kreis</name></author></analytic></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct></listBibl></div1></back></TEI><affiliations><list></list><tree><noCountry><name sortKey="Law, S K Alex" sort="Law, S K Alex" uniqKey="Law S" first="S. K. Alex" last="Law">S. K. Alex Law</name><name sortKey="Lin, Xin" sort="Lin, Xin" uniqKey="Lin X" first="Xin" last="Lin">Xin Lin</name><name sortKey="Tan, Suet Mien" sort="Tan, Suet Mien" uniqKey="Tan S" first="Suet Mien" last="Tan">Suet Mien Tan</name><name sortKey="Torres, Jaume" sort="Torres, Jaume" uniqKey="Torres J" first="Jaume" last="Torres">Jaume Torres</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/StressCovidV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 002146 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 002146 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Sante
|area= StressCovidV1
|flux= Main
|étape= Exploration
|type= RBID
|clé= PMC:7168044
|texte= Two types of transmembrane homomeric interactions in the integrin receptor family are evolutionarily conserved
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:16444740" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a StressCovidV1
| This area was generated with Dilib version V0.6.33. |  |