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Structure–function analysis of the filamentous actin binding domain of the neuronal scaffolding protein spinophilin
Author(s) -
Schüler Herwig,
Peti Wolfgang
Publication year - 2008
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2007.06171.x
Subject(s) - scaffold protein , actin binding protein , microbiology and biotechnology , dendritic spine , actin remodeling of neurons , cytoskeleton , actin , actin cytoskeleton , biology , chemistry , actin remodeling , biophysics , biochemistry , neuroscience , signal transduction , cell , hippocampal formation
Spinophilin, a neuronal scaffolding protein, is essential for synaptic transmission, and functions to target protein phosphatase‐1 to distinct subcellular locations in dendritic spines. It is vital for the regulation of dendritic spine formation and motility, and functions by regulating glutamatergic receptors and binding to filamentous actin. To investigate its role in regulating actin cytoskeletal structure, we initiated structural studies of the actin binding domain of spinophilin. We demonstrate that the spinophilin actin binding domain is intrinsically unstructured, and that, with increasing C‐terminal length, the domain shows augmented secondary structure content. Further characterization confirmed the previously known crosslinking activity and uncovered a novel filamentous actin pointed‐end capping activity. Both of these functions seem to be fully contained within residues 1–154 of spinophilin.