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In 2004, he joined a Marie Curie Research Training Network of the European Commission, studying the sugar-protein interactions that mediate cell-cell recognition.
Interaction of integrins with other proteins, including cadherins and Ig-CAMs allow transmission of signals across the plasma membrane in both directions and mediate cell-cell and cell-matrix interactions and communication (Hynes, 2002).
While it is well known that the extracellular repeats of cadherin proteins mediate cell-cell adhesion in a calcium-dependent manner, the molecular mechanisms behind the influence of calcium in adhesion dynamics and cadherin's mechanical response are not well understood.
Matrix proteoglycans mediate cell-cell and cell-matrix interactions and play key roles in tissue remodeling.
Integrins are a family of heterodimeric transmembrane receptors that mediate cell-cell and cell-ECM interactions.
Normally CAMs tightly orchestrate tissue structure by their ability to mediate cell-cell interaction and contact inhibition.
Cadherins are essential components of the adherens junction complexes that mediate cell-cell adhesion and regulate cell motility.
Classical cadherins are transmembrane proteins that mediate cell-cell adhesion through Ca+2-dependent homophilic interactions of their ectodomains.
Classical cadherins mediate cell-cell adhesion and induce adhesion-related signaling via their interaction with p120 catenin (p120) and β-catenin [8] [10].
Integrins are heterodimeric cell surface adhesion receptors expressed on most cells throughout the body where they mediate cell-cell and cell-extracellular matrix interactions [1].
In addition, it is speculated that STIM1 in the plasma membrane may mediate cell-cell interactions through its extracellular facing N-terminal domain [32], [33].
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