Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Directing Proteins to the Rough Endoplasmic Reticulum

Directing Proteins to the Rough Endoplasmic Reticulum

The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...

Rab Proteins

Rab Proteins

Rab proteins constitute the largest family of monomeric GTPases, of which 70 members are present in humans. Rab proteins and their effectors regulate consecutive stages of vesicle transport such as vesicle transport, docking, and fusion to the correct recipient membrane.
Rab proteins switch between a cytosolic, GDP-bound inactive state and a membrane-anchored, GTP-bound active state. By themselves, Rabs show slow rates of GDP/GTP exchange and GTP hydrolysis. Thus, Rab proteins are considered...

Rab Cascades

Rab Cascades

Rab GTPases act in a regulated cascade during membrane fusion, helping the lipid bilayers mix. The Rab family of proteins are active when bound to GTP, and inactive when bound to GDP. Hence, they act as guanine nucleotide-dependent molecular switches. Rab-GTP recognizes and binds to long or short-range tethering proteins to capture the target vesicle. These tethers coordinate with SNAREs on the vesicle and the target membrane to assemble the trans SNARE complex that locks the mixing bilayers.

Post-translational Translocation of Proteins to the RER

Post-translational Translocation of Proteins to the RER

A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...

Cotranslational Protein Translocation

Cotranslational Protein Translocation

Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...

Regulation of Nuclear Protein Sorting

Regulation of Nuclear Protein Sorting

Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Facilitation of hippocampal long-term potentiation by astrocytic Gq signaling is compromised in an advanced Alzheimer's disease model.

Scientific reports·2026

Same author

Dual role of 3' UTR length in modulating translation termination efficiency.

RNA (New York, N.Y.)·2026

Same author

Eukaryotic initiation factor eIF3 facilitates loading of eukaryotic release factor eRF1 or suppressor tRNA to the ribosome.

Nucleic acids research·2026

Same author

Eukaryotic translation initiation factor 4F: functional properties and physiological role.

Nucleic acids research·2025

Same author

A Duality of Function: An Integrative Model of RACK1 as a Switch Between Translational and Signaling Hubs.

International journal of molecular sciences·2025

Same author

Eukaryotic initiation factors eIF4F and eIF4B promote translation termination upon closed-loop formation.

Nucleic acids research·2025

Search research articles

Related Experiment Video

Updated: Jun 27, 2026

Study of Protein-protein Interactions in Autophagy Research

Study of Protein-protein Interactions in Autophagy Research

Published on: September 9, 2017

PKCβII Activation Promotes Membrane-Proximal Enrichment of Ribosome-Bound RACK1.

Ekaterina Shuvalova¹, Polina Fortygina², Gulnur Smirnova^1,2

¹Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, 119991 Moscow, Russia.

International Journal of Molecular Sciences

|June 26, 2026

Summary

This summary is machine-generated.

Receptor for Activated C Kinase 1 (RACK1) links cell signaling and protein synthesis. Activated Protein Kinase C (PKC) recruits ribosome-bound RACK1 to the cell membrane, enabling localized translation near signaling sites.

Keywords:

PKCβII RACK1 local translation ribosome

More Related Videos

Studying RNA Interactors of Protein Kinase RNA-Activated during the Mammalian Cell Cycle

Studying RNA Interactors of Protein Kinase RNA-Activated during the Mammalian Cell Cycle

Published on: March 5, 2019

Oligopeptide Competition Assay for Phosphorylation Site Determination

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

Related Experiment Videos

Last Updated: Jun 27, 2026

Study of Protein-protein Interactions in Autophagy Research

Study of Protein-protein Interactions in Autophagy Research

Published on: September 9, 2017

Studying RNA Interactors of Protein Kinase RNA-Activated during the Mammalian Cell Cycle

Studying RNA Interactors of Protein Kinase RNA-Activated during the Mammalian Cell Cycle

Published on: March 5, 2019

Oligopeptide Competition Assay for Phosphorylation Site Determination

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

Area of Science:

Molecular Biology
Cell Biology
Biochemistry

Background:

Receptor for Activated C Kinase 1 (RACK1) is a scaffold protein integral to the 40S ribosomal subunit.
RACK1 facilitates the integration of signaling pathways and protein translation.
It interacts with activated Protein Kinase C (PKC) isoforms and membrane receptors.

Purpose of the Study:

To investigate the dynamic interaction between RACK1 and PKCβII at the cellular membrane.
To elucidate the role of ribosome-bound RACK1 in membrane-proximal translation.
To understand the spatial organization of translation in response to cellular signaling.

Main Methods:

Utilized an auxin-inducible degron (AID2) system in human HAP1 cells for selective depletion of cytoplasmic RACK1.
Engineered a RACK1-mAID-mClover3 fusion protein to track RACK1 dynamics.
Employed live-cell imaging to monitor PKCβII membrane recruitment and RACK1 localization upon PKC activation.

Main Results:

Selective depletion of cytoplasmic RACK1 confirmed ribosome association confers resistance to proteolysis.
Activated PKCβII rapidly recruited to the cell membrane, closely followed by enrichment of ribosome-bound RACK1 at membrane-proximal sites.
Kinetics of PKCβII membrane recruitment and RACK1 enrichment peaked around 10 minutes.

Conclusions:

Activated PKCβII engages ribosome-bound RACK1 at membrane-proximal locations.
A diffusion-capture model explains PKCβII membrane accumulation and subsequent capture of ribosome-bound RACK1.
This mechanism recruits the translational machinery to signal input sites, facilitating membrane-proximal translation and providing insights into translation's spatial organization.