Related Experiment Video
Updated: Mar 11, 2026
11:38
Visualization and Quantification of TGFβ/BMP/SMAD Signaling under Different Fluid Shear Stress Conditions using Proximity-Ligation-Assay
Published on: September 14, 2021
3.9K
Modulation of BMP signalling by integrins.
1Faculty of Life Sciences, University of Manchester, Oxford Road, Manchester M13 9PT, U.K.
Biochemical Society Transactions
|December 3, 2016
Summary
Integrins, cell surface receptors, modulate the bone morphogenetic protein (BMP) pathway. This cross-talk can enhance or inhibit BMP signaling, depending on the cellular context and specific mechanisms involved.
Area of Science:
- Cell Biology
- Developmental Biology
- Signal Transduction
Background:
- The bone morphogenetic protein (BMP) pathway is crucial for development and homeostasis.
- Cells interact with their three-dimensional extracellular matrix via integrin receptors.
- Understanding BMP pathway regulation within complex cellular environments is essential.
Purpose of the Study:
- To review the modulation of the BMP pathway by integrins.
- To explore the diverse mechanisms of integrin-BMP cross-talk.
- To highlight the context-dependent nature of this interaction.
Main Methods:
- Literature review of studies on BMP pathway and integrin interactions.
- Analysis of examples from Drosophila embryos and cell line studies.
- Examination of mechanisms including ligand-receptor binding and Smad phosphorylation.
Main Results:
- Integrins can enhance BMP pathway responses through various mechanisms.
- BMP-dependent activation of integrins is frequently observed.
- Integrins can also inhibit the BMP pathway in specific contexts.
Conclusions:
- Integrin-BMP cross-talk is a significant regulatory mechanism for the BMP pathway.
- The outcome of integrin modulation is highly context-dependent.
- Further research is needed to fully elucidate these complex interactions.
Related Concept Videos
01:17Intracellular Signaling Affects Focal Adhesions
3.8K
Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...
Some...
3.8K
01:15Activation of Integrins
5.4K
Integrins bind ligands and transmit information from outside the cell to inside or vice-versa through an "outside-in signaling" or "inside-out signaling."
In "outside-in signaling," external factors in the extracellular space bind to exposed ligand binding sites on integrins. This causes the inactive protein to undergo a conformational change to become active. Integrins are often clustered on the cell membrane. Repetitive and regularly spaced ligand binding...
In "outside-in signaling," external factors in the extracellular space bind to exposed ligand binding sites on integrins. This causes the inactive protein to undergo a conformational change to become active. Integrins are often clustered on the cell membrane. Repetitive and regularly spaced ligand binding...
5.4K
01:10Integrins
5.9K
Animal and protozoan cells do not have cell walls to help maintain shape and provide structural stability. Instead, these eukaryotic cells secrete a sticky mass of carbohydrates and proteins into the spaces between adjacent cells. This network of proteins and molecules is called an extracellular matrix or ECM.
Some ECM proteins assemble into a basement membrane to which the remaining components adhere. Proteoglycans typically form the bulk of the ECM while fibrous proteins, like collagen,...
Some ECM proteins assemble into a basement membrane to which the remaining components adhere. Proteoglycans typically form the bulk of the ECM while fibrous proteins, like collagen,...
5.9K
01:16TGF - β Signaling Pathway
10.8K
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...
10.8K
01:20The JAK-STAT Signaling Pathway
13.5K
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...
13.5K
01:03Anchoring Junctions
5.4K
Anchoring junctions are multiprotein complexes that help cells connect to other cells and the extracellular matrix. Anchoring junctions are present on the lateral and basal surfaces of cells, providing strong and flexible connections. Focal adhesions are often formed due to cell interactions with the ECM substrata, which initiate signal transduction via kinase cascades and other mechanisms. Together, they provide stability and tissue integrity. There are three types of anchoring junctions:...
5.4K