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  Protein Synthesis in the Developing Neocortex at Near-Atomic Resolution Reveals Ebp1-Mediated Neuronal Proteostasis at the 60S Tunnel Exit

Kraushar, M. L., Krupp, F., Harnett, D., Turko, P., Ambrozkiewicz, M. C., Sprink, T., et al. (2021). Protein Synthesis in the Developing Neocortex at Near-Atomic Resolution Reveals Ebp1-Mediated Neuronal Proteostasis at the 60S Tunnel Exit. Molecular Cell, 81(2): e16, pp. 304-322. doi:10.1016/j.molcel.2020.11.037.

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 Creators:
Kraushar, Matthew L., Author
Krupp, Ferdinand , Author
Harnett, Dermot , Author
Turko, Paul, Author
Ambrozkiewicz, Mateusz C. , Author
Sprink, Thiemo, Author
Imami, Koshi , Author
Günnigmann, Manuel , Author
Zinnall, Ulrike, Author
Vieira-Vieira, Carlos H. , Author
Schaub, Theres, Author
Münster-Wandowski, Agnieszka , Author
Bürger, Jörg1, Author              
Borisova, Ekaterina , Author
Yamamot, Hiroshi , Author
Rasin, Mladen-Roko , Author
Ohlen, Uwe, Author
Beule, Dieter, Author
Mielke, Thorsten1, Author              
Tarabykin, Victor , Author
Landthaler, Markus, AuthorKramer, Günter, AuthorVida, Imre, AuthorSelbach, Matthias , AuthorSpahn, Christian M. T., Author more..
Affiliations:
1Microscopy and Cryo-Electron Microscopy (Head: Thorsten Mielke), Scientific Service (Head: Christoph Krukenkamp), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1479668              

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Free keywords: Ebp1; cryo-EM; development; neocortex; neurons; pSILAC/BONCAT mass spectrometry; proteostasis; ribosome; ribosome profiling; selective ribosome profiling
 Abstract: Protein synthesis must be finely tuned in the developing nervous system as the final essential step of gene expression. This study investigates the architecture of ribosomes from the neocortex during neurogenesis, revealing Ebp1 as a high-occupancy 60S peptide tunnel exit (TE) factor during protein synthesis at near-atomic resolution by cryoelectron microscopy (cryo-EM). Ribosome profiling demonstrated Ebp1-60S binding is highest during start codon initiation and N-terminal peptide elongation, regulating ribosome occupancy of these codons. Membrane-targeting domains emerging from the 60S tunnel, which recruit SRP/Sec61 to the shared binding site, displace Ebp1. Ebp1 is particularly abundant in the early-born neural stem cell (NSC) lineage and regulates neuronal morphology. Ebp1 especially impacts the synthesis of membrane-targeted cell adhesion molecules (CAMs), measured by pulsed stable isotope labeling by amino acids in cell culture (pSILAC)/bioorthogonal noncanonical amino acid tagging (BONCAT) mass spectrometry (MS). Therefore, Ebp1 is a central component of protein synthesis, and the ribosome TE is a focal point of gene expression control in the molecular specification of neuronal morphology during development.

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Language(s): eng - English
 Dates: 2020-11-192020-12-222021-01-21
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: DOI: 10.1016/j.molcel.2020.11.037
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Title: Molecular Cell
Source Genre: Journal
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Publ. Info: Cambridge, Mass. : Cell Press
Pages: 19 Volume / Issue: 81 (2) Sequence Number: e16 Start / End Page: 304 - 322 Identifier: ISSN: 1097-2765
CoNE: https://pure.mpg.de/cone/journals/resource/954925610929