Related Experiment Video

Updated: Aug 9, 2026

Spheroid Assay to Measure TGF-β-induced Invasion
09:18

Spheroid Assay to Measure TGF-β-induced Invasion

Published on: November 16, 2011

Cellular distribution of type I and type II receptors for transforming growth factor-beta

S Cheifetz, B Like, J Massagué

    The Journal of Biological Chemistry
    |July 25, 1986
    PubMed

    Insights

    Researchers identified multiple transforming growth factor-beta (TGF beta) receptor forms using affinity labeling. These receptors, classified as Type I and Type II, exhibit distinct molecular weights and binding affinities for TGF beta.

    Area of Science:

    • Cell Biology
    • Molecular Biology
    • Biochemistry

    Background:

    • Transforming growth factor-beta (TGF beta) is a crucial signaling molecule.
    • Understanding TGF beta receptors is key to deciphering its cellular functions.
    • Previous studies indicated a TGF beta receptor complex.

    Purpose of the Study:

    • To identify and characterize diverse TGF beta receptor forms.
    • To distinguish between different types of TGF beta receptors based on structure and binding.
    • To investigate the presence and distribution of these receptors across various cell types.

    Main Methods:

    • Affinity labeling of target cells using iodinated TGF beta (125I-TGF beta).
    • Cross-linking with disuccinimidyl suberate or a photoreactive analogue (4-azidobenzoyl-125I-TGF beta).
    • Structural analysis of labeled receptor species via peptide mapping.

    Main Results:

    • Two distinct TGF beta receptor types (Type I and Type II) were identified.
    • Type I receptors include 280-kDa, 65-kDa, and 130-140-kDa forms with varying cell-type specificity and Kd (50-500 pM).
    • Type II receptors include 85-kDa and 110-kDa forms with high affinity (Kd ~50 pM).

    Conclusions:

    • Multiple TGF beta receptor forms exist, differing in size and binding characteristics.
    • These receptors are intrinsic membrane proteins located on the cell surface.
    • The 280-kDa Type I receptor is part of a disulfide-linked complex, unlike other identified forms.

    More Related Videos

    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

    Studying TGF-β Signaling and TGF-β-induced Epithelial-to-mesenchymal Transition in Breast Cancer and Normal Cells06:54

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

    Published on: October 27, 2020

    Related Concept Videos

    Intracellular Hormone Receptors01:08

    Intracellular Hormone Receptors

    Lipid-soluble hormones diffuse across the plasma and nuclear membrane of target cells to bind to their specific intracellular receptors. These receptors act as transcription factors that regulate gene expression and protein synthesis in the target cell
    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...
    Receptor Downregulation in MVBs01:15

    Receptor Downregulation in MVBs

    Multivesicular bodies (MVBs) are mature endosomes that sort ubiquitinated proteins and then fuse with lysosomes to degrade the sorted proteins. Epidermal growth factor (EGF) and its receptor (EGFR) form a complex that can be internalized through endocytosis, sorted into an MVB, and later degraded.
    The EGFR can initiate signaling pathways that  lead to cell proliferation, migration, and differentiation. Overexpression of EGFR  stimulates cells to proliferate. Excessive  EGFR activation may...
    Receptor Tyrosine Kinases01:26

    Receptor Tyrosine Kinases

    Receptor tyrosine kinases or RTKs are membrane-bound receptors that phosphorylate specific tyrosine on protein substrates. RTKs regulate cellular growth, differentiation, survival, and migration. They contain an extracellular ligand binding domain, a transmembrane domain, and a cytosolic tail with intrinsic kinase activity. Several extracellular signaling molecules activate RTKs in one or more ways and relay the signal downstream. Ligands such as platelet-derived growth factor (PDGF) or...
    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...
    Transducer Mechanism: Enzyme-Linked Receptors01:27

    Transducer Mechanism: Enzyme-Linked Receptors

    Enzyme-linked receptors are cell-surface receptors acting as an enzyme or associating with an enzyme intracellularly. They make excellent drug targets. Drugs can bind to the extracellular ligand-binding domain or directly affect their enzymatic domain and alter their activity.
    Major types that are helpful drug targets include: