Publication
ZBP1 phosphorylation at serine 181 regulates its dendritic transport and the development of dendritic trees of hippocampal neurons.
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- Last modified
- 03/03/2025
- Type of Material
- Authors
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Anna S. Urbanska, International Institute of Molecular and Cell BiologyAleksandra Janusz-Kaminska, International Institute of Molecular and Cell BiologyKatarzyna Switon, International Institute of Molecular and Cell BiologyAlicia L. Hawthorne, Emory UniversityMalgorzata Perycz, International Institute of Molecular and Cell Biology
- Language
- English
- Date
- 2017-05-12
- Publisher
- Nature Publishing Group
- Publication Version
- Copyright Statement
- © The Author(s) 2017
- License
- Final Published Version (URL)
- Title of Journal or Parent Work
- ISSN
- 2045-2322
- Volume
- 7
- Issue
- 1
- Start Page
- 1876
- End Page
- 1876
- Grant/Funding Information
- This research was supported by the Polish National Science Centre (2011/01/N/NZ3/05405) to A.S.U. and an ICEGB grant to J.J., A.J.-K. and K.S. were supported by a National Science Centre Sonata-Bis grant (2012/07/E/NZ3/00503).
- M.U. was supported by a Polish Ministry of Science and Higher Education Iuventus Plus grant (IP2012 037872).
- J.J., K.S., and M.U. are also recipients of the Foundation for Polish Science “Mistrz” Professorial Subsidy and Fellowship, respectively.
- Supplemental Material (URL)
- Abstract
- Local protein synthesis occurs in axons and dendrites of neurons, enabling fast and spatially restricted responses to a dynamically changing extracellular environment. Prior to local translation, mRNA that is to be translated is packed into ribonucleoprotein particles (RNPs) where RNA binding proteins ensure mRNA silencing and provide a link to molecular motors. ZBP1 is a component of RNP transport particles and is known for its role in the local translation of β-actin mRNA. Its binding to mRNA is regulated by tyrosine 396 phosphorylation, and this particular modification was shown to be vital for axonal growth and dendritic branching. Recently, additional phosphorylation of ZBP1 at serine 181 (Ser181) was described in non-neuronal cells. In the present study, we found that ZBP1 is also phosphorylated at Ser181 in neurons in a mammalian/mechanistic target of rapamycin complex 2-, Src kinase-, and mRNA binding-dependent manner. Furthermore, Ser181 ZBP1 phosphorylation was essential for the proper dendritic branching of hippocampal neurons that were cultured in vitro and for the proper ZBP1 dendritic distribution and motility.
- Author Notes
- Keywords
- Research Categories
- Biology, Cell
- Biology, Neuroscience
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