Binding of alphaII spectrin to 14-3-3beta is involved in NCAM-dependent neurite outgrowth.
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Binding of alphaII spectrin to 14-3-3beta is involved in NCAM-dependent neurite outgrowth. / Ramser, Elisa; Buck, Friedrich; Schachner, Melitta; Tilling, Thomas.
In: MOL CELL NEUROSCI, Vol. 45, No. 1, 1, 2010, p. 66-74.Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review
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T1 - Binding of alphaII spectrin to 14-3-3beta is involved in NCAM-dependent neurite outgrowth.
AU - Ramser, Elisa
AU - Buck, Friedrich
AU - Schachner, Melitta
AU - Tilling, Thomas
PY - 2010
Y1 - 2010
N2 - Members of the 14-3-3 protein family have been implicated in neuronal migration, synaptic plasticity and learning. Using affinity chromatography followed by mass spectrometry analysis, we show here that the cytoskeletal protein alphaII spectrin is a novel ligand of 14-3-3beta. We found that 14-3-3beta interacts with alphaII spectrin via the mode 2 14-3-3 binding motif RLIQS(1302)HP. Binding required phosphorylation of Ser(1302) by casein kinase II and was enhanced in the presence of calmodulin. Co-immunoprecipitation of alphaII spectrin and 14-3-3beta with the neural cell adhesion molecule NCAM suggested that the 14-3-3-spectrin-interaction affects NCAM function. Indeed, disruption of the 14-3-3beta/alphaII spectrin interaction by mutating Ser(1302) to Ala enhanced NCAM-dependent neurite outgrowth. Our results indicate that the phosphorylation-dependent interaction between 14-3-3beta and alphaII spectrin acts as a switch between positive and negative regulation of neurite outgrowth stimulated by NCAM, representing a novel and acute mechanism preventing uncontrolled elongation of neuronal processes.
AB - Members of the 14-3-3 protein family have been implicated in neuronal migration, synaptic plasticity and learning. Using affinity chromatography followed by mass spectrometry analysis, we show here that the cytoskeletal protein alphaII spectrin is a novel ligand of 14-3-3beta. We found that 14-3-3beta interacts with alphaII spectrin via the mode 2 14-3-3 binding motif RLIQS(1302)HP. Binding required phosphorylation of Ser(1302) by casein kinase II and was enhanced in the presence of calmodulin. Co-immunoprecipitation of alphaII spectrin and 14-3-3beta with the neural cell adhesion molecule NCAM suggested that the 14-3-3-spectrin-interaction affects NCAM function. Indeed, disruption of the 14-3-3beta/alphaII spectrin interaction by mutating Ser(1302) to Ala enhanced NCAM-dependent neurite outgrowth. Our results indicate that the phosphorylation-dependent interaction between 14-3-3beta and alphaII spectrin acts as a switch between positive and negative regulation of neurite outgrowth stimulated by NCAM, representing a novel and acute mechanism preventing uncontrolled elongation of neuronal processes.
M3 - SCORING: Zeitschriftenaufsatz
VL - 45
SP - 66
EP - 74
JO - MOL CELL NEUROSCI
JF - MOL CELL NEUROSCI
SN - 1044-7431
IS - 1
M1 - 1
ER -