Related Experiment Video
Updated: May 21, 2026
07:55
Analyzing Cell Surface Adhesion Remodeling in Response to Mechanical Tension Using Magnetic Beads
Published on: March 8, 2017
Opening the floodgates: proteomics and the integrin adhesome
Tamar Geiger1, Ronen Zaidel-Bar
1Dept. of Human Molecular Genetics and Biochemistry, Tel Aviv University, Tel Aviv 69978, Israel. geiger@post.tau.ac.il
Current Opinion in Cell Biology
|June 26, 2012
Summary
The integrin adhesome, crucial for cell adhesion, is far more complex than previously known. New proteomic studies reveal a vast number of uncharacterized proteins and force-dependent variations in its composition.
Area of Science:
- Cell Biology
- Molecular Biology
- Proteomics
Background:
- Cell-extracellular matrix connections are mediated by integrin receptors.
- The integrin adhesome comprises adaptors, enzymes, and signaling proteins regulating adhesion dynamics.
- Existing knowledge of adhesome complexity is incomplete.
Purpose of the Study:
- To investigate the full complexity of the integrin adhesome.
- To identify novel components and functional categories within the adhesome.
- To explore integrin-specific variations and force-dependent recruitment.
Main Methods:
- Proteomic analysis of integrin adhesome components.
- Analysis of adhesion complexes under varying tension regimes.
Main Results:
- Recent proteomic studies reveal that known adhesome components represent only a fraction of the total.
- Candidate components in existing functional categories more than double known numbers, with new categories suggested.
- Integrin heterodimers exhibit specific compositional variations.
- Adhesion complex composition is force-dependent, notably recruiting LIM domain proteins.
Conclusions:
- The integrin adhesome is significantly more complex than currently understood.
- Proteomic and mechanical analyses are crucial for a comprehensive understanding of cell adhesion.
- Future research should focus on characterizing novel adhesome components and their functions.
Related Concept Videos
01:17Intracellular Signaling Affects Focal Adhesions
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...
01:15Activation of Integrins
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 events provide an effective stimulus.
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 events provide an effective stimulus.
01:10Integrins
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,...
01:30Assembly of Signaling Complexes
Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
01:26Tension Response at Adherens Junctions
The adherens junctions that anchor cells together are multi-protein complexes that dynamically adapt to mechanical stimuli such as tensile forces and shear stress. Mechanosensory proteins in these junctions can sense such mechanical stimuli and undergo a shift in their conformation, resulting in an altered function — a process called mechanotransduction.
α-Catenin as a Mechanosensory Protein
The α-catenin of adherens junctions is an allosteric protein with three VH (vinculin homology) domains...
α-Catenin as a Mechanosensory Protein
The α-catenin of adherens junctions is an allosteric protein with three VH (vinculin homology) domains...
01:24Overview of Cell-Matrix Interactions
The extracellular matrix or ECM holds cells together to form a tissue and allows the cells within the tissue to communicate. ECM comprises proteins such as fibronectin, collagen, laminin, etc. The most abundant protein in this space is collagen. Collagen fibers are interwoven with carbohydrate-containing protein molecules called proteoglycans. ECM allows cell migration and provides a structural scaffold at cell adhesion that anchors the cell when the extracellular matrix proteins interact with...