The four collagen-binding αI domain integrins form their own subgroup among cell adhesion receptors. The signaling functions of α1β1 and α2β1 integrins have been analyzed in many experimental models, whereas less studies are available about the more recently found α10β1 and α11β1 heterodimers. Interestingly, collagen binding by α1β1 and α2β1 often generates opposite cellular responses. For example α1β1 has often been reported to promote cell proliferation and to suppress collagen synthesis, whereas α2β1 can in many model systems inhibit growth and promote collagen synthesis. There are obviously cell type dependent factors modifying the signaling. Additionally the structure and the organization of collagenous matrix play a critic role. Many recent studies have also stressed the importance of the crosstalk between the integrins and other cell surface receptors.