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Structure-function analysis of the filamentous actin binding domain of the neuronal scaffolding protein spinophilin

Item Type:Article
Title:Structure-function analysis of the filamentous actin binding domain of the neuronal scaffolding protein spinophilin
Creators Name:Schueler, H. and Peti, W.
Abstract: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.
Keywords:Pointed-End Capping Protein, Spinal Plasticity, Spinophilin, Animals, Rats
Source:FEBS Journal
ISSN:1742-464X
Publisher:Blackwell Publishing (U.K.)
Volume:275
Number:1
Page Range:59-68
Date:January 2008
Official Publication:https://doi.org/10.1111/j.1742-4658.2007.06171.x
PubMed:View item in PubMed

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