CELL BIOLOGY OF THE NEURON Polarity ... - Tavernarakis Lab

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Cell Biology of the Neuron: <strong>Polarity</strong>, Plasticity and Regeneration, Crete 2011 Mek2 and Pin1 Regulate BNIP-H (Caytaxin) Ability to Promote Axonal and Dendritic Growth by Trafficking Glutaminase KGA on Kinesin Heavy Chain KIF5B Catherine Qiurong Pan, Boon Chuan Low National University of Singapore, Mechanobiology Institute BNIP-H (or Caytaxin) is a brain-specific BNIP-2 family member implicated in Cayman cerebellar ataxia. Its overexpression potentiates neurite outgrowth in PC12 cells by acting as an adaptor to traffic glutaminase KGA on kinesin KIF5B towards neurite termini and regulates the production of glutamate. However, nothing is known about how formation and functions of such KGA/BNIP- H/KIF5B complex and their trafficking can be regulated and their physiologic outcomes perturbed. We recently showed that nerve growth factor stimulates interaction of BNIP-H with peptidyl-prolyl isomerase Pin1 in differentiating neurons. Here by co-immunoprecipitation studies, we further showed that constitutively active Mek2, but not the kinase-dead Mek2, strongly enhanced the interaction between BNIP-H with KGA as well as BNIP-H with KIF5B. However, the presence of Pin1 could disrupt the ability of BNIP-H to act as the adaptor that linked KGA to KIF5B. Consequently, co-expressing wildtype Pin1 (but not the catalytic mutant Pin1, H157A) with BNIP-H and KGA attenuates the ability of BNIP-H to potentiate PC12 cells differentiation. These results therefore reveal a novel duet role of Mek2 and Pin1 in activating and suppressing the functional ternary interaction of BNIP-H with KIF5B and KGA, and together they represent a novel feedforward and feedback determinant loop in regulating neuronal maturation and differentiation. Presented by: Pan, Catherine Qiurong Poster No 082 Red Session 164
Cell Biology of the Neuron: <strong>Polarity</strong>, Plasticity and Regeneration, Crete 2011 Developmental Stabilization and Activity-Dependent Regulation of Gephyrin Scaffolds at Hippocampal GABAergic Postsynapses Andreas Vlachos 1 , Suneel Reddy-Alla 2 , Theofilos Papadopoulos 2 , Thomas Deller 1 , Heinrich Betz 2 1 Goethe-University, Neuroscience Center, Institute of Clinical Neuroanatomy, Frankfurt a.M., Germany 2 MPI for Brain Research, Department of Neurochemistry, Frankfurt a.M., Germany Gephyrin is a scaffolding protein essential for synaptic clustering of inhibitory glycine and GABA(A) receptors. Here, we investigated the dynamics of gephyrin at individual synapses in organotypic entorhino-hippocampal slice cultures prepared from a newly generated mouse line, which expresses green fluorescent protein-tagged gephyrin under the control of the Thy1.2 promoter. Fluorescence recovery after photobleaching indicates that gephyrin clusters are stabilized at GABAergic postsynapses upon developmental maturation. This stabilization is accompanied by an increase in gephyrin scaffold size and inhibitory synaptic strength. Furthermore, by pharmacologically modulating GABA(A) receptor function we provide evidence for an activity-dependent regulation of gephyrin scaffold stability and size. We conclude that the maturation and plasticity of inhibitory synapses entail changes in the size of the synaptic gephyrin scaffold and its ability to undergo dynamic structural rearrangements. We are currently investigating the underlying molecular mechanisms controlling activitydependent stabilization of gephyrin scaffolds at GABAergic Synapses. Presented by: Papadopoulos, Theofilos 165 Poster No 083 Green Session
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CYFIP1, a Neuronal eIF4E‐BP, Link
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POSTER ABSTRACTS Poster # [‐R(ed)
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030‐B Paracrine Pax6 Activity Reg
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SESSION 10 SYNAPTOGENESIS Chairpers
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da F. Costa, L. 119 D'Adamo, P. 108
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Lewallen, K. 145 Li, Y.‐H. 201 Li
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Teuling, E. 141 Thiebes, K. 87 Thom
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Dr. Bernhard Lohkamp Karolinska Ins
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Mr. Abhishek Shrikant Sahasrabudhe
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CELL BIOLOGY OF THE NEURON Polarity ... - Tavernarakis Lab

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