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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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Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
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Nuclear Protein Sorting01:34

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Nuclear protein sorting is the selective trafficking of histones, polymerases, gene regulatory proteins into the nucleus and exporting RNAs and ribosomes to the cytosol. It is a tightly controlled process that regulates gene expression within a cell.
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The nucleus restricts several proteins within and allows others to pass. The restricted proteins possess a nuclear retention sequence or NRS, anchoring them to the nuclear lamins and preventing their transport to the cytosol. The non-restricted proteins, after their synthesis, are transported to their site of action, such as the cytosol or other organelles, with the help of nuclear export signals or NES.
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Proteins targeted to the nucleus carry short stretches of amino acid sequences called the nuclear localization signal or NLS. Classical nuclear localization signals are of two types: monopartite and bipartite NLS. Monopartite classical NLS (cNLS) consists of a single cluster of 4-8 amino acids. Bipartite cNLS consists of two clusters of  2-3 amino acids and a 9-12 residue long proline-rich linker bridging the two clusters. Signal clusters are rich in positively charged amino acids such as...
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Before mRNAs are exported to the cytoplasm, it is crucial to check each mRNA for structural and functional integrity. Eukaryotic cells use several different mechanisms, collectively known as mRNA surveillance, to look for irregularities in mRNAs. Irregular or aberrant mRNA are rapidly degraded by various enzymes. If a defective mRNA escapes the surveillance, it would be translated into a protein which would either be non-functional or not function properly. One of the primary irregularities in...
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Related Experiment Video

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In Vitro SUMOylation Assay to Study SUMO E3 Ligase Activity
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Non-nuclear function of sumoylated proteins.

Urszula Wasik1, Anna Filipek1

  • 1Nencki Institute of Experimental Biology, Warsaw, Poland.

Biochimica Et Biophysica Acta
|August 12, 2014
PubMed
Summary

The review highlights the growing evidence for SUMOylation, a key regulatory modification, outside the cell nucleus. It details the non-nuclear roles of SUMO substrates in diverse cellular functions.

Keywords:
AutophagyCytoskeletal functionEnzyme activityExocytosisMitochondrial dynamicsReceptor function

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Post-translational modification by SUMOylation is a critical regulatory mechanism in eukaryotic cells.
  • Sumoylated proteins are traditionally known for their roles in nuclear processes like transcription and DNA repair.
  • Emerging research reveals significant functions of sumoylated proteins beyond the nucleus.

Approach:

  • This review synthesizes current literature on the non-nuclear functions of SUMO substrates.
  • It specifically focuses on experimental evidence detailing SUMOylation's impact on various cellular processes outside the nucleus.
  • The compilation aims to provide a comprehensive overview of this expanding research area.

Key Points:

  • Sumoylation regulates diverse non-nuclear cellular functions, including channel activity and receptor signaling.
  • It plays a role in the activity of enzymes, cytoskeletal organization, and exocytosis.
  • The modification is also implicated in fundamental processes such as autophagy and mitochondrial dynamics.

Conclusions:

  • The non-nuclear roles of SUMOylation are increasingly recognized as vital for cellular homeostasis and function.
  • Further research into extranuclear SUMOylation will likely uncover new therapeutic targets.
  • Understanding these extranuclear functions is crucial for a complete picture of SUMOylation's regulatory impact.