WorldCat Identities

Windscheid, Vanessa (1980-....).

Overview
Works: 1 works in 3 publications in 1 language and 3 library holdings
Roles: Author
Publication Timeline
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Most widely held works by Vanessa Windscheid
Caractérisation d'une nouvelle protéine associée aux microtubules, SL21 by Vanessa Windscheid( Book )

3 editions published between 2008 and 2009 in French and held by 3 WorldCat member libraries worldwide

The Early and adult neuronal microtubule-associated protein STOP (Stable Tubule Only Polypeptide) is the main effectors responsible for neuronal microtubules stability. STOP null mice exhibit synaptic plasticity defects with depleted synaptic vesicles pools. Mature neurons also contain a 21-kDa STOP like protein, SL21, which shares micro tubule binding and stabilizing domain and a amino-terminal part of 35 amino acids with STOP proteins. SL21 decorates micro tubules but is otherwise localized at the Golgi apparatus. The first part of this study is focused on the functional characterisation of this amino-terminal domain. It contains three cysteine residues in position 5, 10 and 11 wich sus tain palmitoylation. Palmitoylation is often required for protein association with membrane. We find that SL21's cysteine 5 and 11 is palmitoylated and that only cysteine 5 is necessary for Golgi localization of this protein. We also find that STOP protein, in addition to decorate microtubules, could stain the Golgi apparatus. This target depends on the conserved amino-terminal domain, shared by STOP and SL21 proteins. STOP protein could also be palmitoylated. ln the second part of this work, to understand the function of SL21, we have chosen to study the partners of SL21. A Two- Hybrid screen, using pro teins known as being partners of STOP as target, was realized in the laboratory. Three potential partners were schown to interact with SL21: the protein Tctexl, one of the light chains of the dynein molecular motor, proteins SL21 and STOPs. We confirmed the interaction of these proteins with SL21 by co-immunoprecipitation after over expression in cells and also, from brain extract for the SL21 and STOP's interaction. We also characterise their site of interaction on SL21. The protein Tctexl interacts with SL21 on its module of binding microtubules, the multimerisation domain of SL21 is located on its amino-terminal domain and could implicated palmitoylation. These results let us to imagine the involvement of SL21 and STOPs pro teins in the regulation of synaptic vesicles pool
 
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Languages
French (3)