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

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Cell Biology of the Neuron: Polarity, Plasticity and Regeneration, Crete 2011 The Actin Nucleator Cobl Plays a Role in Neuronal Differentiation and Cerebellar Development and Relies on Association with Abp1 Natja Haag 1 , Lukas Schwintzer 1 , Rashmi Ahuja 1 , Julia Grimm 1 , Nicole Koch 1 , Heike Heuer 2 , Britta Qualmann 1 , Michael Kessels 1 1 Institute for Biochemistry I, University Hospital Jena, Friedrich-Schiller- University Jena 2 Research Group Neuroendocrinology; Leibniz Institute for Age Research Neuromorphogenesis relies on actin cytoskeletal forces to initiate, promote and maintain the underlying cell shape changes. This requires a careful control of actin nucleation at the cell cortex in time and space. Here we describe that the Factin binding protein Abp1, interacts with the novel actin nucleator Cobl. Both heterologous and endogenous coimmunoprecipitations from rat brain demonstrate that Abp1/Cobl interactions exist in vivo. Further analyses revealed that Abp1/Cobl complexes form by the thus far uncharacterized Cobl-Homology domain and are associated with the cell cortex. Immunohistochemistry revealed that Cobl is especially highly expressed in Purkinje cells – cells that constitute the sole source for all motor coordination in the cerebellar cortex. Gene gun experiments with developing cerebellar slices showed that Cobl-deficient Purkinje cells have a strongly impaired arborization. Lack of Abp1 caused a similar phenotype. Thus both Cobl and Abp1 are crucial for proper development of the elaborate dendritic arbor of Purkinje cells. To explicitly prove that Cobl and Abp1 play important roles in dendritogenesis in form of Abp1/Cobl complexes, we demonstrated that Abp1 RNAi suppressed the effects of Cobl on dendritic arborization. Likewise, interfering with Cobl/Abp1 complex formation suppressed Cobl-mediated effects. Thus, Abp1 is an integral part of the Cobl-actin nucleation machinery and together Abp1 and Cobl are important for proper neuromorphogenesis. Presented by: Kessels, Michael Poster No 056 Green Session 138
Cell Biology of the Neuron: Polarity, Plasticity and Regeneration, Crete 2011 Proper Synaptic Vesicle Formation and Neuronal Network Activity Critically Rely on Syndapin I Dennis Koch 1 , Isabella Spiwoks-Becker 2 , Victor Sabanov 3 , Tamar Dugladze 4 , Anne Stellmacher 5 , Rashmi Ahuja 6 , Julia Grimm 1 , Susann Schüler 1 , Anke Müller 7 , Frank Angenstein 8 1 Institute for Biochemistry I, University Hospital Jena - Friedrich Schiller University of Jena, 07743 Jena, Germany 2 Institute for Microanatomy and Neurobiology, Johannes Gutenberg-University of Mainz, 55128 Mainz, Germany 3 Laboratory of Biological Psychology, Department of Psychology, Katholieke Universiteit Leuven, Leuven, 3000, Belgium 4 Cellular and Network Physiology Group, Institute of Neurophysiology, Charité Universitätsmedizin Berlin, 10117 Berlin, Germany 5 Dpt. of Neurochemistry, Leibniz-Institut for Neurobiology, Brenneckestr. 6, 39118 Magdeburg, Germany 6 Massachusetts General Hospital Cancer Ctr 149-7205 149 13th Street Charlestown, MA 02129 7 RG Neuralomics, Leibniz-Institut for Neurobiology, Brenneckestr. 6, 39118 Magdeburg, Germany 8 Non-invasive brain imaging, Leibniz Institute for Neurobiology, 39118 Magdeburg, Germany Synaptic transmission relies on effective and accurate compensatory endocytosis. F-BAR proteins are predestined to serve as membrane curvature sensors and/or inducers and may thereby support membrane remodeling processes, yet, their in vivo functions urgently await disclosure. We demonstrate that the F-BAR protein syndapin I is crucial for proper brain function. Syndapin I knock-out mice suffer from seizures, a phenotype consistent with excessive hippocampal network activity. Loss of syndapin I causes defects in presynaptic membrane trafficking processes evident by loss of synaptic vesicle size control and defects in synaptic activity. Upon high-capacity retrieval accumulation of endocytic intermediates are observed in the ribbon synapses of the retina. Detailed molecular analyses demonstrate that syndapin I plays an important role in the recruitment of all dynamin isoforms, central players in vesicle fission reactions, to the membrane. Consistently, syndapin I KO mice share phenotypes with dynamin I KO mice, whereas their seizure phenotype is very reminiscent of fitful mice expressing a mutant dynamin. Syndapin I thus acts as pivotal membrane anchoring factor for dynamins during regeneration of synaptic vesicles. Presented by: Koch, Dennis 139 Poster No 057 Blue Session
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The meeting was funded in part by E
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These abstracts should not be cited
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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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058‐R Dynein Light Chain LC8 is a
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088‐R Spectraplakins ‐ Cytoskel
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121‐R Calmyrin1 Binds to SCG10 Pr
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18.00 ‐ 18.15 Non Hyperpolarizing
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10.00 ‐ 10.30 Neurotrophin Regula
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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. Christian Alfano INSERM U636, N
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Prof. Graeme W. Davis University of
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Prof. Zhigang He Harvard Medical Sc
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Dr. Bernhard Lohkamp Karolinska Ins
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Mr. Abhishek Shrikant Sahasrabudhe
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Dr. Med. Andreas Vlachos Goethe‐U
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