Integrins are transmembrane adhesion receptors essential for cell communication with the environment and in particular with the extracellular matrix (ECM). ECM components can be processed by several enzymes; one of the largest families involved in this task being matrix metalloproteinases (MMPs). MT1-MMP (membrane type 1-matrix metalloproteinase) is a membrane-anchored MMP with important roles in processes such as tissue development, tumor invasion, and angiogenesis. In addition to its catalytic-dependent functions, MT1-MMP can interact, via its cytosolic tail, with intracellular components, and trigger signaling pathways that impact cell decisions. These features make MT1-MMP similar to integrins, because both are able to integrate events in the extracellular and intracellular milieus. Accordingly, it is probably no coincidence that MT1-MMP often associates and functionally cooperates with distinct integrins at specific cellular compartments. In this review, we discuss aspects of the molecular and functional interplay between MT1-MMP and integrins in distinct cellular and biological contexts.