TAILIEUCHUNG - Báo cáo khoa học: Structure–function analysis of the filamentous actin binding domain of the neuronal scaffolding protein spinophilin

Spinophilin, a neuronal scaffolding protein, is essential for synaptic trans-mission, and functions to target protein phosphatase-1 to distinct subcellu-lar 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. | ỊFEBS Journal Structure-function analysis of the filamentous actin binding domain of the neuronal scaffolding protein spinophilin Herwig Schùler1 and Wolfgang Peti2 1 Max Delbruck Center for Molecular Medicine Berlin-Buch Germany 2 Department of Molecular Pharmacology Physiology and Biotechnology Brown University Providence RI USA Keywords F-actin intrinsically unstructured protein pointed-end capping protein spinal plasticity spinophilin Correspondence H. Schuler Max Delbruck Center for Molecular Medicine 13125 Berlin-Buch Germany Fax 0049-6221-564643 Tel 0049-6221-568284 E-mail W. Peti Department of Molecular Pharmacology Physiology and Biotechnology Brown University Box G-E3 Providence RI 02912 USA Fax 001-401-8636087 Tel 001-401-8636084 E-mail wolfgang_peti@ Present address Department of Parasitology Heidelberg University MedicalSchool Germany Received 21 June 2007 revised 25 October 2007 accepted 31 October 2007 doi Spinophilin a neuronal scaffolding protein is essential for synaptic transmission and functions to target protein phosphatase-1 to distinct subcellu-lar 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. Dendritic spines globular protrusions from neuronal dendrites in the .

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