Interaction between actin and the effector peptide of MARCKS-related protein. Identification of functional amino acid segments
| Autor: | F, Wohnsland, A A, Schmitz, M O, Steinmetz, U, Aebi, G, Vergéres |
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| Rok vydání: | 2000 |
| Předmět: |
Molecular Sequence Data
Intracellular Signaling Peptides and Proteins Membrane Proteins Muscle Proteins Proteins Actins Peptide Fragments Iodoacetamide Actin Cytoskeleton Microscopy Electron Spectrometry Fluorescence Calmodulin Mutation Animals ATP-Binding Cassette Transporters Amino Acid Sequence Rabbits Multidrug Resistance-Associated Proteins Phosphorylation Muscle Skeletal Myristoylated Alanine-Rich C Kinase Substrate Protein Kinase C Protein Binding |
| Zdroj: | The Journal of biological chemistry. 275(27) |
| ISSN: | 0021-9258 |
| Popis: | It is widely assumed that the members of the MARCKS protein family, MARCKS (an acronym for myristoylated alanine-rich C kinase substrate) and MARCKS-related protein (MRP), interact with actin via their effector domain, a highly basic segment composed of 24-25 amino acid residues. To clarify the mechanisms by which this interaction takes place, we have examined the effect of a peptide corresponding to the effector domain of MRP, the so-called effector peptide, on both the dynamic and the structural properties of actin. We show that in the absence of cations the effector peptide polymerizes monomeric actin and causes the alignment of the formed filaments into bundle-like structures. Moreover, we document that binding of calmodulin or phosphorylation by protein kinase C both inhibit the actin polymerizing activity of the MRP effector peptide. Finally, several effector peptides were synthesized in which positively charged or hydrophobic segments were deleted or replaced by alanines. Our data suggest that a group of six positively charged amino acid residues at the N-terminus of the peptide is crucial for its interaction with actin. While its actin polymerizing activity critically depends on the presence of all three positively charged segments of the peptide, hydrophobic amino acid residues rather modulate the polymerization velocity. |
| Databáze: | OpenAIRE |
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