Autoinhibition of the formin Cappuccino in the absence of canonical autoinhibitory domains
| Autor: | Christina L. Vizcarra, Margot E. Quinlan, Martin L. Phillips, Batbileg Bor |
|---|---|
| Přispěvatelé: | Pollard, Thomas D |
| Rok vydání: | 2012 |
| Předmět: |
Circular dichroism
animal structures Amino Acid Motifs macromolecular substances Biology Peptide Mapping Medical and Health Sciences Cell Line 03 medical and health sciences 0302 clinical medicine Drosophila Proteins Site-Directed Protein Interaction Domains and Motifs Molecular Biology Cytoskeleton Actin 030304 developmental biology 0303 health sciences Microfilament Proteins fungi Mutagenesis Amino acid substitution Articles Cell Biology Biological Sciences Protein multimerization Actins Peptide Fragments Cell biology Kinetics A-site Amino Acid Substitution Biochemistry Formins Mutagenesis Site-Directed biology.protein Generic health relevance Protein Multimerization 030217 neurology & neurosurgery Developmental Biology |
| Zdroj: | Molecular biology of the cell, vol 23, iss 19 Molecular Biology of the Cell |
| ISSN: | 1939-4586 1059-1524 |
| Popis: | The Fmn-family formin Cappuccino does not contain classical autoihibitory domains but is autoinhibited. The N-terminus inhibits actin nucleation and competes with elongation. Formins are a conserved family of proteins known to enhance actin polymerization. Most formins are regulated by an intramolecular interaction. The Drosophila formin, Cappuccino (Capu), was believed to be an exception. Capu does not contain conserved autoinhibitory domains and can be regulated by a second protein, Spire. We report here that Capu is, in fact, autoinhibited. The N-terminal half of Capu (Capu-NT) potently inhibits nucleation and binding to the barbed end of elongating filaments by the C-terminal half of Capu (Capu-CT). Hydrodynamic analysis indicates that Capu-NT is a dimer, similar to the N-termini of other formins. These data, combined with those from circular dichroism, suggest, however, that it is structurally distinct from previously described formin inhibitory domains. Finally, we find that Capu-NT binds to a site within Capu-CT that overlaps with the Spire-binding site, the Capu-tail. We propose models for the interaction between Spire and Capu in light of the fact that Capu can be regulated by autoinhibition. |
| Databáze: | OpenAIRE |
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