α Integrin cytoplasmic tails have tissue-specific roles during C. elegans development.
Christopher M Meighan1, Jean E Schwarzbauer
1Department of Molecular Biology and Chemistry, Christopher Newport University, Newport News, VA, USA.
The International Journal of Developmental Biology
|October 31, 2014
Summary
The alpha integrin cytoplasmic tails dictate distinct cellular functions during development. Tail swapping experiments in C. elegans reveal tissue-specific roles for integrin signaling in development.
Area of Science:
- Cell Biology
- Developmental Biology
- Genetics
Background:
- Integrin signaling is crucial for development, with complexity arising from multiple integrin heterodimers.
- Separation of signals from different integrin types is essential within cells.
Purpose of the Study:
- To investigate the role of alpha integrin cytoplasmic tails in developmental processes.
- To determine how distinct alpha integrin tails influence cellular behaviors in a tissue-specific manner.
Main Methods:
- Utilized chimeric alpha integrins in C. elegans to swap cytoplasmic tails between INA-1 and PAT-2.
- Assessed the functional rescue of developmental defects in integrin mutants by chimeric integrins.
- Examined the effects of chimeric integrins in a wild-type background.
Main Results:
- A chimeric INA-1 integrin with the PAT-2 tail rescued lethality and neuron fasciculation but not all developmental processes.
- A chimeric PAT-2 integrin with the INA-1 tail showed limited rescue of a PAT-2 mutation and induced defects in wild-type animals.
- Alpha integrin cytoplasmic tails demonstrated distinct and context-dependent roles in cell migration, muscle organization, and survival.
Conclusions:
- Alpha integrin cytoplasmic tails are key determinants of specific cellular functions during development.
- The impact of integrin tails is modulated by tissue type and genetic background.
- Understanding integrin tail function is vital for deciphering complex developmental signaling pathways.
More Related Videos
Related Concept Videos
01:10Integrins
4.7K
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,...
4.7K
01:17Intracellular Signaling Affects Focal Adhesions
2.7K
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...
2.7K
01:15Activation of Integrins
4.2K
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...
4.2K
01:23Catenins
2.2K
Catenins are characterized by multiple binding domains and dynamic structures that allow them to function as linker proteins in cell junction complexes. All catenins, except α-catenin, contain a characteristic protein sequence called the armadillo repeat and are therefore also called armadillo proteins.
Catenins in Cell Junctions
Catenins bind to cell adhesion molecules such as cadherins and link them to different cytoskeletal proteins depending on the type of cell junction. At the...
Catenins in Cell Junctions
Catenins bind to cell adhesion molecules such as cadherins and link them to different cytoskeletal proteins depending on the type of cell junction. At the...
2.2K
01:03Anchoring Junctions
4.2K
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:...
4.2K
01:26Tension Response at Adherens Junctions
3.1K
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...
α-Catenin as a Mechanosensory Protein
The α-catenin of adherens junctions is an allosteric protein with three VH (vinculin...
3.1K