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The Calcium Integrin Binding protein (CIB) has been identified as interacting specifically with the cytoplasmic tail of the integrin α IIb domain to induce receptor activation and integrin α IIb β 3 mediated cell adhesion to extracellular proteins. In K562 cells stably expressing mutated integrin α V β 3 , or chimeric α V β 3 carrying α IIb cytoplasmic tail, we report that the interaction of CIB with β 3 integrins is not α IIb β 3 specific but binds α IIb as well as α V cytoplasmic tail domains. A double mutation of two proline residues to alanine residues in the α IIb cytoplasmic domain, previously shown to disturb its conformation, inhibits chimeric α V /α IIb β 3 -CIB interaction. This demonstrates that α IIb cytoplasmic domain loop-like conformation is required for interaction with CIB. Moreover, mutations of β 3 cytoplasmic domain residues Tyr-747 and/or Tyr-759 to phenylalanine residues (Y747F, Y759F, and Y747,759F) as well as residues Ser-752 to proline or alanine (S752P and S752A), do not affect the α IIb β 3 or α V β 3 interaction with CIB. Since tyrosine residues Tyr-747 and/or Tyr-759 are the sites of tyrosine phosphorylation of β 3 subunit, these results suggest that the β 3 integrin-CIB interaction occurs through a β 3 -phosphorylation independent mechanism. Likewise, ablation of conformation-dependent affinity change in β 3 Ser752Pro mutation had no affect on CIB-β 3 interaction. In summary, our results demonstrate that the α IIb -subunit integrin and CIB interaction is non-exclusive and requires the loop-like α IIb -cytoplasmic domain conformation. An interaction of CIB with α V -containing integrins provides an additional role for this molecule in keeping with its expression outside of platelets.

cellbio

Calcium Integrin Binding Protein Associates with Integrins &amp;lt;i&amp;gt;α&amp;lt;sub&amp;gt;V&amp;lt;/sub&amp;gt;β&amp;lt;sub&amp;gt;3&amp;lt;/sub&amp;gt;&amp;lt;/i&amp;gt; and &amp;lt;i&amp;gt;α&amp;lt;sub&amp;gt;IIb&amp;lt;/sub&amp;gt;β&amp;lt;sub&amp;gt;3&amp;lt;/sub&amp;gt;&amp;lt;/i&amp;gt; Independent of &amp;lt;i&amp;gt;β&amp;lt;sub&amp;gt;3&amp;lt;/sub&amp;gt;&amp;lt;/i&amp;gt; Activation Motifs