Bledzka K.,Joseph cobs Center For Thrombosis And Vascular Biology Nb |
Liu J.,Joseph cobs Center For Thrombosis And Vascular Biology Nb |
Xu Z.,Blood Research Institute |
Dhanuja Perera H.,Joseph cobs Center For Thrombosis And Vascular Biology Nb |
And 5 more authors.
Journal of Biological Chemistry
Both talin head domain and kindlin-2 interact with integrin β cytoplasmic tails, and they function in concert to induce integrin activation. Binding of talin head domain to β cytoplasmic tails has been characterized extensively, but information on the interaction of kindin-2 with this integrin segment is limited. In this study, we systematically examine the interactions of kindlin-2 with integrin β tails. Kindlin-2 interacted well with β1 and β3 tails but poorly with the β2 cytoplasmic tail. This binding selectivity was determined by the non-conserved residues, primarily the three amino acids at the extreme C terminus of the β3tail, and the sequence in β2 was non-permissive. The region at the C termini of integrin β1 and β3 tails recognized by kindlin-2 was a binding core of 12 amino acids. Kindlin-2 and talin head do not interact with one another but can bind simultaneously to the integrin β3 tail without enhancing or inhibiting the interaction of the other binding partner. Kindlin-2 itself failed to directly unclasp integrin α/β tail complex, indicating that kindlin-2 must cooperate with talin to support the integrin activation mechanism. © 2012 by The American Society for Biochemistry and Molecular Biology, Inc. Source