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TGF - β Signaling Pathway

The TGF-β signaling pathway regulates cell growth, differentiation, adhesion, motility, and development. TGF-β ligands that induce TGF-β signaling are synthesized in their latent form. Several proteases or cell surface receptors such as integrins act upon the latent form, releasing the active ligand. There are three types of mammalian TGF-βs: (TGF-β1, TGF-β2, and TGF-β3) that bind as homodimers or heterodimers to TGF-β receptors. The TGF-β receptors are of three kinds RI, RII, and RIII. The RI...
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Heterotrimeric G proteins are guanine nucleotide-binding proteins. As the name suggests, heterotrimeric G proteins are composed of three subunits: alpha, beta, and gamma. They remain GDP-bound or GTP-bound inside the cells and switch between inactive/active states. The Gα subunit possesses the nucleotide-binding pocket that binds guanine nucleotides and switches between GDP or GTP-bound states. In contrast, the Gꞵ and Gγ subunits are always bound together with high affinity and are together...
Integrins01:10

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Updated: May 30, 2026

A Convenient and General Expression Platform for the Production of Secreted Proteins from Human Cells
07:09

A Convenient and General Expression Platform for the Production of Secreted Proteins from Human Cells

Published on: July 31, 2012

TG2, a novel extracellular protein with multiple functions.

Zhuo Wang1, Martin Griffin

  • 1School of Life and Health Sciences, Aston University, Aston Triangle, Birmingham, B47ET, UK.

Amino Acids
|August 6, 2011
PubMed
Summary

Tissue transglutaminase 2 (TG2) acts extracellularly as a scaffold and enzyme, influencing cell adhesion and behavior. Dysregulation of TG2 contributes to diseases like cancer and fibrosis, making it a key therapeutic target.

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Modified Yeast-Two-Hybrid System to Identify Proteins Interacting with the Growth Factor Progranulin
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Last Updated: May 30, 2026

A Convenient and General Expression Platform for the Production of Secreted Proteins from Human Cells
07:09

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Published on: July 31, 2012

Modified Yeast-Two-Hybrid System to Identify Proteins Interacting with the Growth Factor Progranulin
07:56

Modified Yeast-Two-Hybrid System to Identify Proteins Interacting with the Growth Factor Progranulin

Published on: January 17, 2012

Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Background:

  • Tissue transglutaminase 2 (TG2) is a multifunctional enzyme with known intracellular roles.
  • TG2 can be secreted to the cell surface via an unknown mechanism.
  • Extracellular TG2 activity is influenced by oxidation and nitric oxide (NO).

Purpose of the Study:

  • To review the novel roles of TG2 at the cell surface and in the extracellular matrix (ECM).
  • To explore TG2's functions as both a transamidating enzyme and an extracellular scaffold protein.
  • To discuss TG2's involvement in cell adhesion and associated signaling pathways.

Main Methods:

  • Literature review of TG2's extracellular functions.
  • Analysis of TG2's interactions with cell surface receptors (e.g., β integrins, syndecan-4).
  • Examination of TG2's role in physiological and pathological processes.

Main Results:

  • TG2 functions as an FN co-receptor for β integrins.
  • TG2 forms a heterocomplex with Fibronectin (FN) and syndecan-4, activating PKCα.
  • TG2's extracellular roles are transamidation-dependent and independent.

Conclusions:

  • TG2 plays diverse roles at the cell surface and in the ECM, impacting cell behavior and adhesion.
  • TG2's involvement in cell adhesion pathways highlights its significance in physiological processes.
  • Dysregulated TG2 contributes to diseases such as metastatic cancer, fibrosis, and coeliac disease, positioning it as a therapeutic and diagnostic target.