Platelets function physiologically in mediating hemostasis, but are also associated with many pathological conditions, such as thrombosis, which can lead to myocardial infarction and/or stroke. Therefore, the study of platelet regulation and signaling has been of great interest and is necessary for generating effective antiplatelet therapeutics. One platelet signaling molecule of particular interest is the integrin alpha(IIb)beta(3), which binds Fg and mediates platelet cross-linking. The integrin itself as well as cytoplasmic proteins that interact with alpha(IIb)beta(3) have become potential targets for anti-platelet therapies. One such protein that has been shown to directly regulate alpha(IIb)beta(3) function is calcium-and integrin-binding protein 1 ( CIB1). CIB1 has been implicated in alpha(IIb)beta(3) activation and outside-in signaling through the integrin. By increasing our understanding of CIB1 and other proteins that like it, associate with integrin alpha(IIb)beta(3), and the signaling events that result from those interactions, we may bring ourselves closer to more effective therapies. In the present work, we explore known cytoplasmic binding partners of the integrin alpha(IIb)beta(3) and their effect on alpha(IIb)beta(3), focusing on CIB1.