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 Dynein Light Chain LC8 is a Dimerization Hub for the Memory-Related KIBRA Protein Joachim Kremerskothen, Kerstin Duning, Bernd Ribbrock, Hermann Pavenstaedt Department for Molecular Nephrology, University Hospital Muenster, Muenster, Germany Memory formation in the mammalian brain is based on a dynamic remodelling of synaptic contacts in concert with the constant turnover of neuroreceptors at postsynaptic sites. These processes are achieved through highly regulated intra- and interneuronal transport mechanisms and a dynamic cytoskeleton network in axons and dendrites. Recent studies have shown that the expression of the KIBRA scaffolding protein is crucial for memory formation and the development of neurodegenerative diseases. In neurons, KIBRA is enriched at postsynaptic sites where it interacts with the actin-binding proteins Synaptopodin and Dendrin. Additional KIBRA binding partners include protein kinase M (PKM) zeta as well as the dynein light chain LC8. LC8 was initially discovered as part of the dynein motor complex and was thought to act mainly as a cargo adapter. However, recent findings suggest that LC8 is also able to stabilize multiprotein complexes by promoting dimerization of its binding partners. Because the intracellular transport of KIBRA is mainly dynein-independent, we examined the functional role of the interaction with LC8 in more detail. Using in vitro binding assays and yeast two-hybrid experiments we were able to map two distinct LC8 binding motifs within the KIBRA molecule. Mutation analysis revealed that only dimeric LC8 is able to associate with KIBRA and that this association is controlled by LC8 phosphorylation. Interestingly, binding of LC8 facilitates KIBRA dimerization and regulates the interaction with its other binding proteins. In summary, our data indicate that LC8 is a molecular hub for KIBRA dimerization. Thus, LC8 could serve as a regulatory element in neurons mediating assembly/disassembly of structural protein networks containing the KIBRA dimer. Presented by: Kremerskothen, Joachim Poster No 058 Red Session 140
Cell Biology of the Neuron: <strong>Polarity</strong>, Plasticity and Regeneration, Crete 2011 The Amyotrophic Lateral Sclerosis 8 Protein VAPB Disrupts the Early Secretory Pathway Marijn Kuijpers, Ka Lou Yu, Eva Teuling, Dick Jaarsma, Casper Hoogenraad Department of Neuroscience, Erasmus Medical Center, Rotterdam, The Netherlands The vesicle-associated membrane protein (VAMP) associated protein B (VAPB) is an ubiquitously expressed integral membrane protein localized to the ER. A missense mutation (P56S) in de gene encoding for VAPB has been linked to motor neuron degeneration in amyotrophic lateral scleroses (ALS) affected patients. In the central nervous system VAPB is abundant in motor neurons and when mutated VAPB-P56S proteins accumulate in ER-like subcompartments. To understand the physiological and pathological functions of VAPB in causing neurodegenerative diseases, we searched for potential in vivo binding partners of VAPB protein. Via pull-down assays and mass spectrometry we identified interacting factor of YIP1 (YIF1A) as a VAPB binding partner and found that VAPB and YIF1A interact via their transmembrane regions. By immunofluorescent labeling of cultured hippocampal neurons we demonstrate that YIF1A is localized to the endoplasmic reticulum - Golgi intermediate compartments (ERGIC), which is involved in ER-to-Golgi trafficking. We show that VAPB knockdown affects the distribution of YIF1A localization in neurons. We also found that YIF1A is recruited to VAPB-P56S structures and thereby loses its ERGIC localization. These data suggest that YIF1A missorting and disruptions in the early secretory pathway might play an important role in VAPB associated motor neuron disease. Presented by: Kuijpers, Marijn 141 Poster No 059 Green Session
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Abstracts of papers presented at th
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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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