Integrin Trafficking in Cell Migration Dynamics

Integrins are transmembrane heterodimeric receptors that anchor cells to the extracellular matrix and transduce mechanical and chemical signals essential for migration. Migration relies on the finely tuned balance between integrin endocytosis, recycling and degradation to remodel adhesions and direct protrusive activity. Internalisation of ligand-bound integrins at the cell rear and sides facilitates adhesion disassembly, while targeted recycling to the leading edge supports the formation of new contact points and directional force generation. This trafficking is orchestrated by small GTPases, adaptor proteins and SNARE-mediated vesicle fusion, integrating cues from growth factors, matrix composition and mechanical stress. Cross-talk between integrin trafficking and nutrient-sensing pathways further couples metabolic state to migratory capacity. Dysregulation of these routes underpins pathological processes such as tumour invasion, angiogenesis and inflammatory disorders, making integrin traffic a focal point for therapeutic intervention.

Research from Nature Portfolio

Recent studies have identified the GTPase-activating protein p120RasGAP as a central regulator of α5 integrin recycling in vascular endothelial cells. Proteomic mapping revealed that neuropilin 1 and neuropilin 2 co-associate with α5 integrin in endosomal compartments, directing its transit to Rab11-positive recycling endosomes. This pathway promotes polarised fibronectin fibrillogenesis and endothelial sprouting in vivo, emphasising the coordinated trafficking of integrin-ligand complexes during angiogenesis. These findings underline how adaptor proteins and co-receptors integrate to control adhesion receptor localisation and drive morphogenetic processes.

Integrin Trafficking in Cell Migration Dynamics publication trend

The graph below shows the total number of articles in integrin trafficking in cell migration dynamics across all publications each year (not limited to Nature Index journals).

Technical terms

Integrin: Transmembrane heterodimeric receptor that mediates cell–extracellular matrix adhesion and bidirectional signalling.

Endocytosis: Cellular process by which plasma membrane receptors are internalised into endosomal vesicles.

Recycling endosome: Intracellular compartment marked by Rab11 that returns internalised receptors to the cell surface.

Focal adhesion: Dynamic multiprotein complex linking integrins to the actin cytoskeleton to mediate adhesion and signalling.

Extracellular matrix (ECM): Network of proteins and polysaccharides providing structural support and biochemical cues to cells.

References

1. Enhanced Tumor‐Targeted Delivery of Arginine‐Rich Peptides via a Positive Feedback Loop Orchestrated by Piezo1/integrin β1 Signaling Axis. Advanced Science (2024).
2. Tetraspanin 3 promotes NSCLC cell proliferation via regulation of β1 integrin intracellular recycling. Cellular & Molecular Biology Letters (2024).
3. A proteomics approach to isolating neuropilin-dependent α5 integrin trafficking pathways: neuropilin 1 and 2 co-traffic α5 integrin through endosomal p120RasGAP to promote polarised fibronectin fibrillogenesis in endothelial cells. Communications Biology (2024).
4. Integrin traffic – the update. Journal of Cell Science (2015).
5. Ligand-Occupied Integrin Internalization Links Nutrient Signaling to Invasive Migration. Cell Reports (2015).