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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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Phosphorylation01:02

Phosphorylation

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The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
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Regulated Protein Degradation02:58

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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.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
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Regulated Protein Degradation02:58

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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
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Author Spotlight: Fluorescence-Based Quantification of Mitochondrial Membrane Potential and Superoxide Levels Using Live Imaging in HeLa Cells
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Post translational modification of Parkin.

Joy Chakraborty1, Valentina Basso1, Elena Ziviani2,3

  • 1Department of Biology, University of Padova, Via Ugo Bassi 58b, 35131, Padova, Italy.

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|February 23, 2017
PubMed
Summary

Parkin protein mutations cause Parkinsonism. This review explores how post-translational modifications regulate Parkin activity, impacting its roles in cell health and disease.

Keywords:
ParkinParkinson’s diseasePhosphorylationPost translational modificationsUbiquitination

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Neuroscience

Background:

  • Mutations in the E3 ubiquitin ligase Parkin gene are linked to familial Parkinsonism.
  • Parkin's structure is known, but activation pathways remain unclear.
  • Parkin regulates mitochondria quality, tumor suppression, and stress protection.

Purpose of the Study:

  • To review post-translational modifications (PTMs) affecting Parkin activity and stability.
  • To understand how PTMs control Parkin's diverse cellular functions.

Main Methods:

  • Comparative sequence alignment of Parkin orthologs across species.
  • Identification of conserved amino acid residues critical for Parkin function.

Main Results:

  • Conserved domains and residues across species suggest functional importance.
  • PTMs are hypothesized to mediate Parkin's broad cellular impact.
  • Specific PTMs directly influence Parkin activity and protein stability.

Conclusions:

  • Post-translational modifications are key regulators of Parkin function.
  • Understanding Parkin PTMs is crucial for deciphering its role in Parkinsonism and other cellular processes.