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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

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Regulated Protein Degradation02:58

Regulated Protein Degradation

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...
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence the...
Conservative Site-specific Recombination and Phase Variation02:53

Conservative Site-specific Recombination and Phase Variation

Because the DNA segments are cut and reorganized in a direction-specific manner, site-specific recombination has emerged as an efficient genetic engineering technique. Flippase and Cyclization recombinases or Flp and Cre, respectively, are two members of the tyrosine recombinase family derived from bacteriophages, that are used to mediate site-specific DNA insertions, deletions, and targeted expression of proteins in mammalian cell lines.
The recognition sites for Cre recombinase called LoxP...
Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

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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SUMO-Binding Entities (SUBEs) as Tools for the Enrichment, Isolation, Identification, and Characterization of the SUMO Proteome in Liver Cancer
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Small ubiquitin-related modifier (SUMO) binding determines substrate recognition and paralog-selective SUMO

Jianmei Zhu1, Shanshan Zhu, Catherine M Guzzo

  • 1Bloomberg School of Public Health, Department of Biochemistry and Molecular Biology, The Johns Hopkins University, Baltimore, Maryland 21205, USA.

The Journal of Biological Chemistry
|August 19, 2008
PubMed
Summary

Small ubiquitin-related modifiers (SUMOs) regulate cells by attaching to proteins. This study shows SUMO-2/3 preferentially binds to BLM protein, revealing a mechanism for selective protein modification.

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SUMO-Binding Entities (SUBEs) as Tools for the Enrichment, Isolation, Identification, and Characterization of the SUMO Proteome in Liver Cancer
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In Vivo Detection and Analysis of Rb Protein SUMOylation in Human Cells

Published on: November 2, 2017

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • Small ubiquitin-related modifiers (SUMOs) are crucial for regulating cellular processes via covalent attachment to target proteins.
  • Vertebrates have three SUMO paralogs (SUMO-1, SUMO-2, SUMO-3), with SUMO-2 and SUMO-3 being highly similar (SUMO-2/3).
  • SUMO-1 and SUMO-2/3 modify distinct protein subsets, regulating separate cellular pathways, but the mechanism for this selectivity is unclear.

Purpose of the Study:

  • To investigate the mechanism of selective protein modification by different SUMO paralogs.
  • To determine how proteins are selectively modified by SUMO-1 versus SUMO-2/3.
  • To explore the role of non-covalent interactions in SUMO-target protein recognition.

Main Methods:

  • In vitro and in vivo assays to assess SUMO modification of BLM (Bloom syndrome protein).
  • Analysis of non-covalent interactions between SUMO paralogs and target proteins.
  • Investigating SUMOylation of a HIPK2 C-terminal fragment.

Main Results:

  • BLM, a RecQ DNA helicase, is preferentially modified by SUMO-2/3.
  • Non-covalent SUMO-BLM interactions are essential for modification at non-consensus sites.
  • Preferential SUMO-2/3 modification of BLM is driven by selective binding of SUMO-2/3.
  • SUMOylation of a HIPK2 fragment depends on SUMO binding, suggesting a general mechanism.

Conclusions:

  • Non-covalent interactions between SUMO paralogs and target proteins are a key mechanism for SUMO substrate selection.
  • This interaction mechanism facilitates paralog-selective SUMO modification.
  • Findings provide insights into the regulation of cellular processes by SUMOylation.