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Related Concept Videos

Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

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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
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
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The Sarcomere01:08

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A sarcomere is a microscopic segment repeating in a myofibril. The sarcomere fundamentally consists of two main myofilaments: thick filaments called myosin and thin filaments called actin. These filaments interact by sliding past each other in response to stimulus. In addition to myosin and actin, several other proteins, such as tropomyosin, troponin, titin, nebulin, myomesin, α-actinin, and dystrophin, play crucial roles in regulating, structuring, and functioning of the sarcomere.
Each...
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Protein Modifications in the RER01:26

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Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
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Translation01:31

Translation

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Lesson: Translation
Translation is the process of synthesizing proteins from the genetic information carried by messenger RNA (mRNA). Following transcription, it constitutes the final step in the expression of genes. This process is carried out by ribosomes, complexes of protein and specialized RNA molecules. Ribosomes, transfer RNA (tRNA), and other proteins produce a chain of amino acids—the polypeptide—as the end product of translation.
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Histone Modification02:32

Histone Modification

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The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
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Initiation of Translation

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Initiating translation is complex because it involves multiple molecules. Initiator tRNA, ribosomal subunits, and eukaryotic initiation factors (eIFs) are all required to assemble on the initiation codon of mRNA. This process consists of several steps that are mediated by different eIFs.
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Related Experiment Video

Updated: Feb 7, 2026

Identification of Post-translational Modifications of Plant Protein Complexes
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Temperature-sensitive sarcomeric protein post-translational modifications revealed by top-down proteomics.

Wenxuan Cai1, Zachary L Hite2, Beini Lyu2

  • 1Molecular and Cellular Pharmacology Training Program, University of Wisconsin-Madison, Madison, WI 53705, USA; Department of Cell and Regenerative Biology, University of Wisconsin-Madison, Madison, WI 53705, USA.

Journal of Molecular and Cellular Cardiology
|July 27, 2018
PubMed
Summary

Temperature significantly impacts post-translational modifications (PTMs) of sarcomeric proteins in human heart tissue. Careful handling is crucial to prevent artefactual changes during sample processing and shipment for accurate heart failure research.

Keywords:
PhosphorylationPost-translational modificationSarcomeresTop-down mass spectrometry

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A Fast and Quantitative Method for Post-translational Modification and Variant Enabled Mapping of Peptides to Genomes
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Area of Science:

  • Biochemistry
  • Proteomics
  • Cardiovascular Research

Background:

  • Heart failure (HF) remains a leading cause of death globally, necessitating research on human cardiac tissue.
  • Animal models have limitations due to physiological differences with humans.
  • Artefactual changes in tissue samples due to temperature variations are a concern in research.

Purpose of the Study:

  • To investigate the effects of temperature on post-translational modifications (PTMs) of sarcomeric proteins.
  • To understand how temperature variations during tissue handling affect sample integrity.
  • To evaluate the utility of top-down proteomics for assessing cardiac tissue quality.

Main Methods:

  • Utilized a top-down proteomics approach.
  • Examined human heart tissue samples under simulated shipment/processing temperatures (4°C and 22°C).
  • Analyzed changes in post-translational modifications (PTMs) of sarcomeric proteins.

Main Results:

  • Temperature significantly altered sarcomeric protein PTMs, with differential effects observed.
  • Increased phosphorylation of cardiac troponin I and enigma homolog isoform 2 occurred at 4°C and 22°C.
  • Decreased phosphorylation of cardiac troponin T and myosin regulatory light chain was noted at these temperatures.
  • Significant protein degradation was observed after incubation at 4°C and 22°C.

Conclusions:

  • Temperature has diverse effects on sarcomeric protein PTMs in human heart tissue.
  • Meticulous tissue handling protocols are essential to avoid temperature-induced artefacts.
  • Top-down proteomics is a powerful tool for evaluating the integrity of cardiac tissue samples.