Dia-Interacting Protein Modulates Formin-Mediated Actin Assembly at the Cell Cortex

Mammalian Diaphanous (mDia)-related formins and the N-WASP-activated Arp2/3 complex initiate the assembly of filamentous actin. Dia-interacting protein (DIP) binds via its amino-terminal SH3 domain to the proline-rich formin homology 1 (FH1) domain of mDia1 and mDia2 and to the N-WASp proline-rich r...

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Veröffentlicht in:	Current biology 2007-04, Vol.17 (7), p.579-591
Hauptverfasser:	Eisenmann, Kathryn M., Harris, Elizabeth S., Kitchen, Susan M., Holman, Holly A., Higgs, Henry N., Alberts, Arthur S.
Format:	Artikel
Sprache:	eng
Schlagworte:	Actin Cytoskeleton - metabolism Actin-Related Protein 2-3 Complex - metabolism Actins - metabolism Adaptor Proteins, Signal Transducing - chemistry Adaptor Proteins, Signal Transducing - genetics Adaptor Proteins, Signal Transducing - metabolism Amino Acid Sequence Carrier Proteins - metabolism cdc42 GTP-Binding Protein - metabolism Cell Line Cell Membrane - metabolism CELLBIO Green Fluorescent Proteins - metabolism HeLa Cells Humans Molecular Sequence Data Muscle Proteins - chemistry Muscle Proteins - genetics Muscle Proteins - metabolism Mutation Protein Structure, Tertiary Pseudopodia - metabolism Pseudopodia - ultrastructure Recombinant Fusion Proteins - metabolism Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism RNA, Small Interfering - genetics Sequence Alignment
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