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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, Jahrgang 45, Nr. 1, 1, 2010, S. 66-74.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Ramser, E, Buck, F, Schachner, M & Tilling, T 2010, 'Binding of alphaII spectrin to 14-3-3beta is involved in NCAM-dependent neurite outgrowth.', MOL CELL NEUROSCI, Jg. 45, Nr. 1, 1, S. 66-74. <http://www.ncbi.nlm.nih.gov/pubmed/20598904?dopt=Citation>

APA

Ramser, E., Buck, F., Schachner, M., & Tilling, T. (2010). Binding of alphaII spectrin to 14-3-3beta is involved in NCAM-dependent neurite outgrowth. MOL CELL NEUROSCI, 45(1), 66-74. [1]. http://www.ncbi.nlm.nih.gov/pubmed/20598904?dopt=Citation

Vancouver

Ramser E, Buck F, Schachner M, Tilling T. Binding of alphaII spectrin to 14-3-3beta is involved in NCAM-dependent neurite outgrowth. MOL CELL NEUROSCI. 2010;45(1):66-74. 1.

Bibtex

@article{016e315e6ca7459b8255bf318abbf91c,
title = "Binding of alphaII spectrin to 14-3-3beta is involved in NCAM-dependent neurite outgrowth.",
abstract = "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.",
author = "Elisa Ramser and Friedrich Buck and Melitta Schachner and Thomas Tilling",
year = "2010",
language = "Deutsch",
volume = "45",
pages = "66--74",
journal = "MOL CELL NEUROSCI",
issn = "1044-7431",
publisher = "Academic Press Inc.",
number = "1",

}

RIS

TY - JOUR

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 -