Proteomic Analysis of Integrin a5 Associated Complexes Dependent upon Integrin Activation State in Zebrafish

Integrins are a major class of heterodimeric adhesion receptors composed of an a and b subunit that link the extracellular matrix (ECM) and the cytoskeleton across the cell membrane. When activated by either the intracellular (inside-out signaling) or extracellular (outside-in signaling) environment, integrins undergo a conformational change that increases the ligand binding affinity. As the primary receptor for ECM protein fibronectin, Integrin a5 plays a critical role in zebrafish somitogenesis. To better understand integrin activation in this context, we performed co-immunoprecipitation and Mass Spectrometry (MS) based proteomics using FLAG-tagged Integrin a5 alleles that alter it activation state: constitutive active mutant a5GAAKR and inactive ligand binding deficient mutant a5FYLDD, expressed in maternal zygotic a5 mutant (MZa5-/-) embryos. Our data provide an overview of Integrin associated proteins according to the activation state of the Integrin.