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Related Concept Videos

Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

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.
Protein Complexes with Interchangeable Parts01:57

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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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Ribosome Profiling

Ribosome profiling or ribo-sequencing is a deep sequencing technique that produces a snapshot of active translation in a cell. It selectively sequences the mRNAs protected by ribosomes to get an insight into a cell’s translation landscape at any given point in time.
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The technique helps...

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Detection of Protein Ubiquitination Sites by Peptide Enrichment and Mass Spectrometry
11:54

Detection of Protein Ubiquitination Sites by Peptide Enrichment and Mass Spectrometry

Published on: March 23, 2020

Poly-small ubiquitin-like modifier (PolySUMO)-binding proteins identified through a string search.

Huaiyu Sun1, Tony Hunter

  • 1Molecular and Cell Biology Laboratory, Salk Institute for Biological Studies, La Jolla, California 92037, USA. hsun@salk.edu

The Journal of Biological Chemistry
|October 23, 2012
PubMed
Summary
This summary is machine-generated.

Researchers identified novel proteins with clustered SUMO-interacting motifs (SIMs) that bind to polySUMOylated proteins. These clustered SIMs, particularly the VIDLT motif, are key for recognizing SUMOylation, impacting cellular stress responses.

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Area of Science:

  • Molecular Biology
  • Cellular Biology
  • Biochemistry

Background:

  • Polysumoylation is a critical cellular process responding to genomic stress and proteostasis.
  • Proteins with clustered SUMO-interacting motifs (SIMs), like RNF4, act as signal transducers in polysumoylation pathways.

Purpose of the Study:

  • To identify novel proteins that bind to polysumoylated targets.
  • To investigate the structural basis of SUMO recognition by clustered SIMs.

Main Methods:

  • Computational string search using a custom Python script.
  • Biochemical analysis of identified proteins and their SIMs.
  • Sequence analysis to identify conserved SUMO-binding motifs.

Main Results:

  • Discovered clustered SIMs in Arkadia/RNF111, suggesting its role in polysumoylation.
  • Identified a dominant pentameric VIDLT motif within SIM clusters, crucial for SUMO binding.
  • Found novel SIM clusters in FLASH/CASP8AP2, C5orf25, and SOBP/JXC1.

Conclusions:

  • Clustered SIMs function as distinct SUMO binding domains.
  • The VIDLT motif represents an optimal structure for SUMO recognition.
  • These findings expand the understanding of proteins involved in polysumoylation and cellular stress response.