Related Experiment Video

Updated: Jun 25, 2026

Studying TGF-β Signaling and TGF-β-induced Epithelial-to-mesenchymal Transition in Breast Cancer and Normal Cells
06:54

Studying TGF-β Signaling and TGF-β-induced Epithelial-to-mesenchymal Transition in Breast Cancer and Normal Cells

Published on: October 27, 2020

Transforming Growth Factor {beta} Can Stimulate Smad1 Phosphorylation Independently of Bone Morphogenic Protein

Katharine H Wrighton1, Xia Lin, Paul B Yu

  • 1Michael E. DeBakey Department of Surgery and Department of Molecular and Cellular Biology, Baylor College of Medicine, Houston, Texas 77030, USA.

The Journal of Biological Chemistry
|February 20, 2009
PubMed

Insights

Transforming growth factor-beta (TGFbeta) signaling can activate Smad1 phosphorylation in various cell types. This process occurs through different receptor complexes, depending on the specific cell, and is not always dependent on Bone Morphogenic Protein (BMP) receptors.

Area of Science:

  • Cellular signaling pathways
  • Molecular biology
  • Receptor kinase activation

Background:

  • Transforming growth factor-beta (TGFbeta) superfamily ligands regulate cellular processes via receptor kinases.
  • Canonical TGFbeta signaling involves TbetaRI/ALK5 and Smad2/3 phosphorylation.
  • Canonical Bone Morphogenic Protein (BMP) signaling involves ALK1/2/3/6 and Smad1/5/8 phosphorylation.

Purpose of the Study:

  • To investigate TGFbeta-induced Smad1 phosphorylation in non-endothelial cells.
  • To determine the receptor specificity of TGFbeta-mediated Smad1 phosphorylation.

Main Methods:

  • Treatment of various cell lineages with TGFbeta.
  • Analysis of Smad1 phosphorylation.
  • Use of chemical inhibitors specific for TGFbeta (ALK4/5/7) and BMP (ALK1/2/3/6) type I receptors.

Main Results:

  • TGFbeta significantly induces Smad1 phosphorylation in multiple non-endothelial cell types.
  • TGFbeta-mediated Smad1 phosphorylation can occur independently of BMP type I receptors in certain cell types.
  • The receptor complexes involved in TGFbeta-induced Smad1 phosphorylation are cell type-specific.

Conclusions:

  • TGFbeta can induce Smad1 phosphorylation beyond endothelial cells.
  • TGFbeta-mediated Smad1 phosphorylation utilizes diverse receptor complexes in a cell-specific manner.
  • This expands the understanding of TGFbeta superfamily signaling crosstalk.

More Related Videos

Visualization and Quantification of TGFβ/BMP/SMAD Signaling under Different Fluid Shear Stress Conditions using Proximity-Ligation-Assay11:38

Visualization and Quantification of TGFβ/BMP/SMAD Signaling under Different Fluid Shear Stress Conditions using Proximity-Ligation-Assay

Published on: September 14, 2021

Molecular Analysis of Endothelial-mesenchymal Transition Induced by Transforming Growth Factor-β Signaling07:49

Molecular Analysis of Endothelial-mesenchymal Transition Induced by Transforming Growth Factor-β Signaling

Published on: August 3, 2018

Related Concept Videos

TGF - β Signaling Pathway01:16

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...
Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze the...
PI3K/mTOR/AKT Signaling Pathway01:22

PI3K/mTOR/AKT Signaling Pathway

The mammalian target of rapamycin  (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1  (mTORC1) and mTOR complex 2  (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast,  mTORC2 consists of a rapamycin-insensitive companion...
The JAK-STAT Signaling Pathway01:20

The JAK-STAT Signaling Pathway

Several cytokine receptors have tightly bound Janus kinase or JAK proteins attached at their cytosolic tail. Small signaling molecules such as cytokines, growth hormones, or prolactins bind to the cytokine receptors and initiate their dimerization. The dimerization brings the cytosolic JAKs together that trans-phosphorylate and activates each other. The activated JAKs now phosphorylate cytosolic tails of the cytokine receptors, which serve as binding sites for adaptor proteins such as  SH2...
mTOR Signaling and Cancer Progression03:03

mTOR Signaling and Cancer Progression

The mammalian target of rapamycin or mTOR protein was discovered in 1994 due to its direct interaction with rapamycin. The protein gets its name from a yeast homolog called TOR. The mTOR protein complex in mammalian cells plays a major role in balancing anabolic processes such as the synthesis of proteins, lipids, and nucleotides and catabolic processes, such as autophagy in response to environmental cues, such as availability of nutrients and growth factors.
The mTOR pathway or the...
Mitogens and the Cell Cycle02:38

Mitogens and the Cell Cycle

Mitogens and their receptors play a crucial role in controlling the progression of the cell cycle. However, the loss of mitogenic control over cell division leads to tumor formation. Therefore, mitogens and mitogen receptors play an important role in cancer research. For instance, the epidermal growth factor (EGF) - a type of mitogen and its transmembrane receptor (EGFR), decides the fate of the cell's proliferation. When EGF binds to EGFR, a member of the ErbB family of tyrosine kinase...