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Related Concept Videos

Translational Regulation01:29

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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Post-translational Translocation of Proteins to the RER01:27

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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
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Regulation of Expression Occurs at Multiple Steps02:24

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Gene expression can be regulated at almost every step from gene to protein. Transcription is the step that is most commonly regulated. This involves the binding of proteins to short regulatory sequences on the DNA. This association can either promote or inhibit the transcription of a gene associated with the respective sequence.
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Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
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Translation

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Lesson: Translation
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Detection of Post-translational Modifications on Native Intact Nucleosomes by ELISA
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RECK isoforms differentially regulate fibroblast migration by modulating tubulin post-translational modifications.

Ha Neul Lee1, Oye A Bosompra2, Hilary A Coller3

  • 1Molecular Biology Institute, University of California, Los Angeles, Los Angeles, CA, 90095, USA.

Biochemical and Biophysical Research Communications
|February 2, 2019
PubMed
Summary

RECK isoforms regulate cell migration by altering α-tubulin post-translational modifications (PTMs). These RECK-mediated changes in tubulin acetylation and detyrosination impact fibroblast migration rates and integrin-extracellular matrix interactions.

Keywords:
Fibroblast migrationIntegrinMMP9RECK isoformsTubulin PTM

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Cell migration is crucial for development and immunity.
  • RECK isoforms influence invasion by interacting with MMP9.
  • Previous work identified RECK isoform-mediated invasion pathways.

Purpose of the Study:

  • To elucidate the mechanism by which RECK isoforms affect cell migration.
  • To investigate the role of α-tubulin post-translational modifications (PTMs) in RECK-mediated cell migration.
  • To identify upstream regulators of RECK's effects on tubulin PTMs.

Main Methods:

  • Analysis of RECK isoform effects on α-tubulin acetylation and detyrosination.
  • Assessment of fibroblast migration rates under varying RECK isoform conditions.
  • Investigation of MMP9 and integrin activity in regulating tubulin PTMs.

Main Results:

  • Both canonical and short RECK isoforms modulate tubulin acetylation and detyrosination levels.
  • Altered tubulin PTMs are sufficient to modulate fibroblast migration rates.
  • MMP9 and integrin activity were identified as upstream regulators of tubulin acetylation and detyrosination.

Conclusions:

  • RECK isoforms impact cell migration through modulation of α-tubulin PTMs.
  • RECK isoforms exert opposing effects on cell migration via MMP9-dependent regulation of integrin-ECM interactions and microtubule PTMs.
  • This study defines a molecular pathway linking RECK, MMP9, integrin activity, and tubulin PTMs in regulating cell migration.