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rdf:type |
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lifeskim:mentions |
umls-concept:C0086418,
umls-concept:C0678594,
umls-concept:C1425164,
umls-concept:C1426592,
umls-concept:C1514562,
umls-concept:C1514873,
umls-concept:C1546857,
umls-concept:C1549781,
umls-concept:C1556066,
umls-concept:C1619636,
umls-concept:C1863551,
umls-concept:C1879547,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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pubmed:issue |
9
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pubmed:dateCreated |
2008-9-12
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pubmed:abstractText |
Formins induce the nucleation and polymerization of unbranched actin filaments. They share three homology domains required for profilin binding, actin polymerization, and regulation. Diaphanous-related formins (DRFs) are activated by GTPases of the Rho/Rac family, whose interaction with the N-terminal formin domain is thought to displace a C-terminal Diaphanous-autoregulatory domain (DAD). We have determined the structure of the N-terminal domains of FHOD1 consisting of a GTPase-binding domain (GBD) and the DAD-recognition domain FH3. In contrast to the formin mDia1, the FHOD1-GBD reveals a ubiquitin superfold as found similarly in c-Raf1 or PI3 kinase. This GBD is recruited by Rac and Ras GTPases in cells and plays an essential role for FHOD1-mediated actin remodeling. The FHOD1-FH3 domain is composed of five armadillo repeats, similarly to other formins. Mutation of one residue in the predicted DAD-interaction surface efficiently activates FHOD1 in cells. These results demonstrate that DRFs have evolved different molecular solutions to govern their autoregulation and GTPase specificity.
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0969-2126
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
16
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1313-23
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pubmed:meshHeading |
pubmed-meshheading:18786395-Amino Acid Motifs,
pubmed-meshheading:18786395-Amino Acid Sequence,
pubmed-meshheading:18786395-Animals,
pubmed-meshheading:18786395-Armadillo Domain Proteins,
pubmed-meshheading:18786395-Conserved Sequence,
pubmed-meshheading:18786395-Enzyme Activation,
pubmed-meshheading:18786395-Fetal Proteins,
pubmed-meshheading:18786395-GTP Phosphohydrolases,
pubmed-meshheading:18786395-Humans,
pubmed-meshheading:18786395-Mice,
pubmed-meshheading:18786395-Models, Biological,
pubmed-meshheading:18786395-Models, Molecular,
pubmed-meshheading:18786395-Molecular Sequence Data,
pubmed-meshheading:18786395-Mutation, Missense,
pubmed-meshheading:18786395-NIH 3T3 Cells,
pubmed-meshheading:18786395-Nuclear Proteins,
pubmed-meshheading:18786395-Protein Binding,
pubmed-meshheading:18786395-Protein Structure, Tertiary,
pubmed-meshheading:18786395-Sequence Homology, Amino Acid,
pubmed-meshheading:18786395-Transfection
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pubmed:year |
2008
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pubmed:articleTitle |
The human formin FHOD1 contains a bipartite structure of FH3 and GTPase-binding domains required for activation.
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pubmed:affiliation |
Abteilung Physikalische Biochemie, Max-Planck-Institut für Molekulare Physiologie, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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