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Mena binds α5 integrin directly and modulates α5β1 function.
Stephanie L Gupton1, Daisy Riquelme, Shannon K Hughes-Alford
1The David H. Koch Institute for Integrative Cancer Research, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
The Journal of Cell Biology
|August 22, 2012
Summary
Mena protein regulates cell migration and adhesion by forming a complex with α5β1 integrin. This interaction is crucial for cell-matrix communication and controlling cell movement.
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- Mena (Ena/VASP family) is an actin regulator involved in cell migration and adhesion.
- Mena localizes to focal adhesions but its function there is unknown.
- α5β1 integrin is a fibronectin receptor mediating cell adhesion and motility.
Purpose of the Study:
- To investigate the function of Mena in focal adhesions.
- To determine the relationship between Mena and α5β1 integrin.
Main Methods:
- Co-immunoprecipitation to identify Mena-binding partners.
- In vitro binding assays to map Mena interaction domains.
- Analysis of cell behavior (migration, adhesion, spreading) in fibroblasts lacking Mena or α5β1 integrin function.
Main Results:
- Mena forms an adhesion-regulated complex with the α5 cytoplasmic tail.
- Mena directly binds α5 via a region rich in LERER repeats.
- The Mena-α5 complex is essential for outside-in α5β1 signaling, including FAK/paxillin phosphorylation.
- This complex regulates fibrillar adhesion formation, fibronectin fibrillogenesis, cell spreading, and migration speed.
Conclusions:
- Mena plays a critical role in α5β1 integrin-mediated cell functions.
- The Mena-α5 complex is a key mediator of bidirectional communication between the extracellular matrix and focal adhesions.
- Mena is essential for fibroblast adhesion, spreading, and migration through its interaction with α5β1 integrin.
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