PAK6 Phosphorylates 14-3-3γ to Regulate Steady State Phosphorylation of LRRK2-Reference-Cited by-同舟云学术

PAK6 Phosphorylates 14-3-3γ to Regulate Steady State Phosphorylation of LRRK2

Published:2017-12-14 Issue: Volume:10 Page:
ISSN:1662-5099
Container-title:Frontiers in Molecular Neuroscience
language:
Short-container-title:Front. Mol. Neurosci.

Author:

Civiero Laura,Cogo Susanna,Kiekens Anneleen,Morganti Claudia,Tessari Isabella,Lobbestael Evy,Baekelandt Veerle,Taymans Jean-Marc,Chartier-Harlin Marie-Christine,Franchin Cinzia,Arrigoni Giorgio,Lewis Patrick A.,Piccoli Giovanni,Bubacco Luigi,Cookson Mark R.,Pinton Paolo,Greggio Elisa

Publisher

Frontiers Media SA

Subject

Cellular and Molecular Neuroscience,Molecular Biology

Reference57 articles.

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3. Protein kinase D-mediated phosphorylation at Ser 99 regulates localization of p21-activated kinase 4;Bastea;Biochem. J.,2013

4. LRRK2 overexpression alters glutamatergic presynaptic plasticity, striatal dopamine tone, postsynaptic signal transduction, motor activity and memory;Beccano-Kelly;Hum. Mol. Genet,2015

5. LRRK2 phosphorylates pre-synaptic N-ethylmaleimide sensitive fusion (NSF) protein enhancing its ATPase activity and SNARE complex disassembling rate;Belluzzi;Mol. Neurodegener,2016

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