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Related Concept Videos

Tagging and Fusion Proteins01:24

Tagging and Fusion Proteins

Proteins are involved in several cellular processes and biochemical reactions. Analyzing a specific protein of interest requires it to be isolated from the other proteins in the cell. This is achieved by overexpressing the specific gene in a suitable host to produce large quantities of the target protein. A tag or label is recombined with the gene to produce a fusion protein containing the target protein and the tag. The tags on these fusion proteins can then be used for easy detection and...
Golgi Matrix Proteins01:12

Golgi Matrix Proteins

Golgi matrix proteins are a group of highly dynamic proteins that maintain the stacked structure of Golgi. These proteins adapt to rapid morphological changes of the Golgi during the cell cycle. During cell division, mild proteolysis removes these connections resulting in Golgi unstacking. In The daughter cells, these proteins help reassemble the unstacked Golgi.
One of the first identified Golgi matrix proteins was GM130, a rod-like protein located in the cis-Golgi. Subsequently, many Golgi...
Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the translocon complex.
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
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...
Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

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
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...

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Related Experiment Video

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Spectrophotometric Screening for Potential Inhibitors of Cytosolic Glutathione S-Transferases
14:57

Spectrophotometric Screening for Potential Inhibitors of Cytosolic Glutathione S-Transferases

Published on: October 10, 2020

Transglutaminase 2: a multi-functional protein in multiple subcellular compartments.

Donghyun Park1, Sun Shim Choi, Kwon-Soo Ha

  • 1Department of Molecular and Cellular Biochemistry, Vascular System Research Center, Kangwon National University School of Medicine, Chuncheon, Kangwon-do, 200-701, Republic of Korea.

Amino Acids
|February 12, 2010
PubMed
Summary

Transglutaminase 2 (TG2) is a versatile protein involved in many cell functions. Its activity and interactions are dictated by its location within the cell and the surrounding microenvironment.

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Background:

  • Transglutaminase 2 (TG2) exhibits diverse enzymatic and non-enzymatic functions.
  • TG2's roles span critical cellular processes including differentiation, apoptosis, inflammation, migration, and healing.
  • Its activity is modulated by cellular factors like calcium, nucleotides, and redox potential.

Purpose of the Study:

  • To review the biological functions of TG2.
  • To explore TG2's molecular interactions.
  • To contextualize TG2's activities within its subcellular localization and microenvironment.

Main Methods:

  • Literature review and synthesis of existing research on TG2.
  • Analysis of TG2's biochemical activities and regulatory mechanisms.
  • Examination of TG2's protein interactions and substrate specificity.

Main Results:

  • TG2 possesses multiple biochemical activities: transglutaminase, G protein, kinase, protein disulfide isomerase, and adaptor protein.
  • Cellular location (cytosol, plasma membrane, nucleus, mitochondria, extracellular space) significantly influences TG2's biochemical activities.
  • TG2 interacts with different protein subsets based on its subcellular localization.

Conclusions:

  • Subcellular microenvironments are critical determinants of TG2's specific biochemical activities.
  • TG2's localization dictates its functional outcomes and molecular partnerships.
  • Understanding TG2's context-dependent functions is key to elucidating its role in cellular processes.