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Directing Proteins to the Rough Endoplasmic Reticulum

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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...

Leaky Scanning

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During most eukaryotic translation processes, the small 40S ribosome subunit scans an mRNA from its 5' end until it encounters the first start AUG codon. The large 60S ribosomal subunit then joins the smaller one to initiate protein synthesis. The location of the translation initiation is largely determined by the nucleotides near the start codon as there may be multiple translation initiation sites present on the mRNA. Marilyn Kozak discovered that the sequence RCCAUGG (where R...

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Targeting proteins to the ER
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Translational Regulation

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Translational regulation in prokaryotes ensures efficient protein synthesis by controlling ribosome access to mRNA. This regulation is mediated by secondary RNA structures, including translational riboswitches, RNA thermometers, and small RNAs (sRNAs), which respond to intracellular and environmental signals to modulate gene expression.Translational RiboswitchesRiboswitches in the leader region of mRNAs can regulate translation by altering the accessibility of the Shine-Dalgarno (SD) sequence,...

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Related Experiment Video

Updated: Mar 19, 2026

Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins

Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins

Published on: August 9, 2019

Intrinsically disordered SERBP1 regulates translation through topology-driven G-quadruplex recognition.

Antoine Baudin^1,2,3,4, Hoang H Dinh^1,2, Kira Breunig¹

¹Greehey Children's Cancer Research Institute, University of Texas Health San Antonio, San Antonio, TX, United States.

Biorxiv : the Preprint Server for Biology

|March 18, 2026

Summary

This summary is machine-generated.

Serpine mRNA-binding protein 1 (SERBP1) binds G-quadruplexes via an encircling mechanism, with phosphorylation acting as a regulatory switch. This discovery offers a framework for targeting SERBP1-G4 interactions in cancer therapy.

Keywords:

G-quadruplex RNA-protein interactions SERBP1 glioblastoma intrinsically disordered protein mTOR phosphorylation translational regulation

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Last Updated: Mar 19, 2026

Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins

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Published on: August 9, 2019

Genome-wide Quantification of Translation in Budding Yeast by Ribosome Profiling

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Published on: December 21, 2017

Assessment of Selective mRNA Translation in Mammalian Cells by Polysome Profiling

Assessment of Selective mRNA Translation in Mammalian Cells by Polysome Profiling

Published on: October 28, 2014

Area of Science:

Molecular Biology
Structural Biology
Cancer Research

Background:

Serpine mRNA-binding protein 1 (SERBP1) is an intrinsically disordered protein implicated in cancer, but its RNA recognition mechanism is unclear.
Understanding SERBP1's interaction with RNA targets is crucial for elucidating its role in translation regulation and disease.

Purpose of the Study:

To characterize the G-quadruplex (G4)-binding properties of SERBP1.
To elucidate the molecular mechanism of SERBP1-G4 recognition.
To investigate the role of SERBP1-G4 interactions in glioblastoma and mTOR regulation.

Main Methods:

NMR spectroscopy and biophysical assays to determine SERBP1-G4 binding affinity and mechanism.
Molecular dynamics and docking simulations to visualize the interaction.
Phosphomimetic mutations to assess the role of serine phosphorylation.
Cell-based assays in glioblastoma to study SERBP1's role in mTOR expression.

Main Results:

SERBP1 binds parallel RNA and DNA G4s with low micromolar affinity via an encircling mechanism involving its RGG box and C-terminal serines.
Phosphorylation of key serines acts as a regulatory switch, modulating SERBP1 binding affinity.
G4 topology, not sequence, drives SERBP1 recognition, positioning it as a broad-specificity G4 adaptor.
SERBP1 regulates mTOR expression in glioblastoma through G4 elements in the mTOR 5' UTR, and its depletion synergizes with mTOR inhibition.

Conclusions:

SERBP1 is a G4 adaptor protein that recognizes G4 structures through a unique encircling mechanism.
Phosphorylation serves as a regulatory switch for SERBP1 activity.
SERBP1-G4 interactions are critical for mTOR regulation in glioblastoma, presenting a potential therapeutic target.