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Related Concept Videos

Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

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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.
These groups modify specific amino acids in a protein....
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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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Regulation of Expression at Multiple Steps01:23

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The gene expression in cells is regulated at different stages: (i) transcription, (ii) RNA processing, (iii) RNA localization, and (iv) translation. Transcriptional regulation is mediated by regulatory proteins such as transcription factors, activators, or repressors—these control gene expression by initiating or inhibiting the transcription of genes. Once a precursor or pre-mRNA is produced, it undergoes post-transcriptional modification, including 5' capping, splicing, and the...
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Proteins are involved in several cellular processes and biochemical reactions. Analyzing a specific protein of interest requires it to be isolated from the other proteins in the cell. This is achieved by overexpressing the specific gene in a suitable host to produce large quantities of the target protein. A tag or label is recombined with the gene to produce a fusion protein containing the target protein and the tag. The tags on these fusion proteins can then be used for easy detection and...
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Protein Folding Quality Check in the RER01:29

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ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
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Pre-mRNA Processing: Modification of pre-mRNA Ends01:35

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In eukaryotic cells, transcripts made by RNA polymerase are modified and processed before exiting the nucleus. Unprocessed RNA is called precursor mRNA or pre-mRNA to distinguish it from mature mRNA.
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Related Experiment Video

Updated: Aug 13, 2025

Utilizing a Comprehensive Immunoprecipitation Enrichment System to Identify an Endogenous Post-translational Modification Profile for Target Proteins
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A guide to UFMylation, an emerging posttranslational modification.

David Millrine1, Joshua J Peter1, Yogesh Kulathu1

  • 1Medical Research Council Protein Phosphorylation & Ubiquitylation Unit (MRC-PPU), School of Life Sciences, University of Dundee, UK.

The FEBS Journal
|January 21, 2023
PubMed
Summary
This summary is machine-generated.

Ubiquitin Fold Modifier-1 (UFM1) is a ubiquitin-like modifier crucial for cell health. Its dysregulation links to diseases via endoplasmic reticulum stress, highlighting UFM1

Keywords:
UFM1endoplasmic reticulumligaseproteaseproteostasisubiquitin-like modifier

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Ubiquitin Fold Modifier-1 (UFM1) is a ubiquitin-like modifier (UBL) essential for eukaryotic cell function.
  • UFM1 conjugation involves a unique enzymatic system ensuring substrate fidelity.
  • Defects in the UFM1 pathway are linked to human diseases, including musculoskeletal and neurodevelopmental disorders.

Purpose of the Study:

  • To provide a comprehensive overview of UFM1 biogenesis, conjugation, and function.
  • To elucidate the mechanisms underlying UFM1's role in cellular processes.
  • To highlight the therapeutic potential of targeting the UFM1 pathway.

Main Methods:

  • Review of existing literature on UFM1 pathway mechanics.
  • Analysis of UFM1's involvement in endoplasmic reticulum (ER) stress and translational homeostasis.
  • Exploration of UFM1's roles in DNA damage response and telomere maintenance.

Main Results:

  • UFM1 plays a critical role at the ER, where it modifies ribosomes in response to translational stalling.
  • Loss of UFMylation leads to increased ER stress and disrupted translational homeostasis.
  • UFM1 is implicated in DNA damage response and telomere maintenance, underscoring its broad cellular functions.

Conclusions:

  • Understanding UFM1 pathway mechanics is vital for comprehending fundamental cell biology.
  • The UFM1 pathway represents a promising target for therapeutic interventions in human diseases.
  • Further research into UFM1 function will yield significant insights into cell biology and human health.