Structural characterization of the interactions between palladin and ?-actinin.

ABSTRACT: The interaction between ?-actinin and palladin, two actin-cross-linking proteins, is essential for proper bidirectional targeting of these proteins. As a first step toward understanding the role of this complex in organizing cytoskeletal actin, we have characterized binding interactions between the EF-hand domain of ?-actinin (Act-EF34) and peptides derived from palladin and generated an NMR-derived structural model for the Act-EF34/palladin peptide complex. The critical binding site residues are similar to an ?-actinin binding motif previously suggested for the complex between Act-EF34 and titin Z-repeats. The structure-based model of the Act-EF34/palladin peptide complex expands our understanding of binding specificity between the scaffold protein ?-actinin and various ligands, which appears to require an ?-helical motif containing four hydrophobic residues, common to many ?-actinin ligands. We also provide evidence that the Family X mutation in palladin, associated with a highly penetrant form of pancreatic cancer, does not interfere with ?-actinin binding.

SUBMITTER: Beck MR 

PROVIDER: S-EPMC3226707 | biostudies-literature | 2011 Oct

REPOSITORIES: biostudies-literature