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Current Research on Structure and Functions of Ribosomal Proteins

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Biology".

Deadline for manuscript submissions: 20 September 2026 | Viewed by 611

Editor

Special Issue Information

Dear Colleagues,

Ribosomal proteins are among the most ancient and intriguing biomolecules in the cell. As essential components of the ribosome—often considered a molecular fossil—they provide a unique window into the earliest forms of life. Many ribosomal proteins exhibit unusual structural features: a large number are fully or partially intrinsically disordered outside the ribosome, raising fundamental questions about their folding, assembly, function, and transport.

In recent years, their roles have proven to be far more complex than initially thought. Emerging studies suggest that the network organization within the ribosome contributes to the control of ribosome dynamics during translation. Moreover, several ribosomal proteins have been implicated in extra-ribosomal functions, with growing evidence of their involvement in diverse cellular processes and diseases, including cancer and developmental disorders.

Another fascinating frontier is ribosome heterogeneity—the concept that ribosomes can vary in protein composition, potentially leading to specialized functions or adaptive responses. This paradigm shift opens new avenues for understanding translational regulation and cellular plasticity.

We warmly invite researchers exploring any aspect of ribosomal proteins—from structure and evolution to dynamics, function, and pathology—to contribute to this Special Issue. Let us together deepen our understanding of these enigmatic molecular players.

Dr. Youri Timsit
Guest Editor

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Keywords

  • protein synthesis
  • translation
  • translocation
  • dynamics
  • folding
  • network
  • assembly
  • evolution

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Published Papers (1 paper)

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Research

13 pages, 1385 KB  
Communication
PKCβII Activation Promotes Membrane-Proximal Enrichment of Ribosome-Bound RACK1
by Ekaterina Shuvalova, Polina Fortygina, Gulnur Smirnova, Natialia Bal, Elena Alkalaeva and Peter Kolosov
Int. J. Mol. Sci. 2026, 27(12), 5310; https://doi.org/10.3390/ijms27125310 - 11 Jun 2026
Viewed by 237
Abstract
The scaffold protein RACK1 (Receptor for Activated C Kinase 1) integrates signaling and translation, acting as a core component of the 40S ribosomal subunit. It binds activated Protein Kinase C (PKC) isoforms and membrane receptors. We used an auxin-inducible degron (AID2) system in [...] Read more.
The scaffold protein RACK1 (Receptor for Activated C Kinase 1) integrates signaling and translation, acting as a core component of the 40S ribosomal subunit. It binds activated Protein Kinase C (PKC) isoforms and membrane receptors. We used an auxin-inducible degron (AID2) system in human HAP1 cells to selectively deplete the free (cytoplasmic) pool of RACK1. The engineered RACK1–mAID–mClover3 fusion was rapidly degraded in the cytoplasm upon addition of 5-phenyl-indole-3-acetic acid (5-Ph-IAA), while the ribosome-bound pool remained detectable in ribosomal fractions, indicating that ribosome association makes RACK1 relatively less accessible to AID2-mediated proteolysis. Upon activation of PKCβII with phorbol-12-myristate-13-acetate (PMA), imaging at defined time points revealed closely matched kinetics of PKCβII membrane recruitment and membrane-proximal enrichment of ribosome-bound RACK1, peaking at ~10 min. Our data support a model in which activated PKCβII engages ribosome-bound RACK1 at membrane-proximal sites, consistent with a diffusion–capture mechanism in which PKCβII first accumulates at the membrane and then captures ribosome-bound RACK1, thereby recruiting the translational machinery to sites of signal input for membrane-proximal translation. These findings provide new insights into the spatial organization of translation. Full article
(This article belongs to the Special Issue Current Research on Structure and Functions of Ribosomal Proteins)
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