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Updated: May 4, 2026
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Analyzing Cell Surface Adhesion Remodeling in Response to Mechanical Tension Using Magnetic Beads
Published on: March 8, 2017
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Dynamic control of β1 integrin adhesion by the plexinD1-sema3E axis
Young I Choi1, Jonathan S Duke-Cohan, Wei Chen
1Laboratory of Immunobiology and Department of Medical Oncology, Dana-Farber Cancer Institute and Department of Medicine, Harvard Medical School, Boston, MA 02115.
Summary
PlexinD1 and semaphorin 3E control thymocyte movement by regulating beta1 integrin adhesion. This finding reveals how cell guidance molecules fine-tune integrin function for immune cell trafficking and selection.
Area of Science:
- Cell Biology
- Immunology
- Neuroscience
Background:
- Plexins and semaphorins are key regulators of cell guidance across multiple biological systems.
- The precise mechanisms linking plexin function to integrin activity in directed cell movement are not fully understood.
Purpose of the Study:
- To investigate how plexin D1 and semaphorin 3E influence beta1 integrin function during thymocyte development and trafficking.
- To elucidate the molecular basis of plexin-integrin interactions in cellular guidance.
Main Methods:
- Utilized developing thymocytes to examine plexin D1's role in beta1 integrin adhesion domain organization.
- Investigated the effect of semaphorin 3E ligation on individual beta1 integrin bond stability and lifetime under force.
Main Results:
- Plexin D1 regulates the nanoscale topology of beta1 integrin adhesion domains in cis.
- Semaphorin 3E ligation in trans alters individual beta1 integrin bond lifetimes, reducing stability.
- Loss of plexin D1 diminishes beta1 integrin clustering and avidity, while semaphorin 3E reduces bond stability.
Conclusions:
- Decreased plexin D1 expression and semaphorin 3E gradients promote thymocyte migration towards the medulla.
- These plexin-mediated modulations of integrin adhesion are crucial for orchestrated lymphoid trafficking and immune repertoire selection.
- The study reveals plexin-tunable molecular features of integrin adhesion with broad implications for cellular processes.
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