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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.
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It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
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Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
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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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In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones
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Expanding the ubiquitin code through post-translational modification.

Lina Herhaus1, Ivan Dikic2

  • 1Institute of Biochemistry II Goethe University, Frankfurt am Main, Germany.

EMBO Reports
|August 14, 2015
PubMed
Summary
This summary is machine-generated.

Post-translational modifications of ubiquitin (Ub) and its receptors expand its regulatory functions. Phosphorylation by PINK1 and TBK1 impacts cellular processes and is linked to neurodegenerative diseases like Parkinson's disease.

Keywords:
mitophagyphosphorylationpost‐translational modificationubiquitin

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Detection of Protein Ubiquitination Sites by Peptide Enrichment and Mass Spectrometry
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Detection of Protein Ubiquitination Sites by Peptide Enrichment and Mass Spectrometry

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Background:

  • Ubiquitylation is a key post-translational modification regulating cellular functions.
  • Ubiquitin itself can be modified by other post-translational modifications, including acetylation and phosphorylation.
  • These modifications alter ubiquitin chain formation and signaling pathways.

Purpose of the Study:

  • To explore the role of ubiquitin and autophagy receptor post-translational modifications in cellular signaling.
  • To investigate the impact of specific phosphorylation events on disease development.
  • To understand how ubiquitin modifications expand the ubiquitin code.

Main Methods:

  • Literature review on ubiquitin post-translational modifications.
  • Analysis of signaling pathways involving PINK1, TBK1, and autophagy receptors.
  • Examination of the link between these modifications and neurodegenerative diseases.

Main Results:

  • Ubiquitin acetylation on K6 and K48 represses ubiquitin chain formation.
  • Phosphorylation of ubiquitin at S65 by PINK1 activates Parkin, crucial for mitophagy.
  • TBK1-mediated phosphorylation of OPTN and p62 regulates the removal of various cellular components.

Conclusions:

  • Post-translational modification of ubiquitin and its receptors significantly expands the ubiquitin code.
  • PINK1- and TBK1-mediated phosphorylation events are implicated in Parkinson's disease and amyotrophic lateral sclerosis.
  • Understanding these modifications is vital for comprehending cellular regulation in health and disease.