Actin and tubulin, which forms microtubules, are components of the cytoskeleton. While the extracellular matrix is linked to the cytoskeleton, these proteins are not large components of the matrix. Myosin is a motor protein that largely interacts with actin in muscle tissue. Collagens are the most abundant proteins in the extracellular matrix and have many important functions, including helping maintain cell and tissue structure.

The correct answer is that integrins anchor the cell to the extracellular matrix (ECM) and relay signals from the ECM to the cell. Integrins are transmembrane receptors that bind ECM ligands such as fibronectin, vitronectin, collagen, and laminin to relay messages to the cell, ultimately regulating transcription of genes involved in the cell cycle, cell shape, and motility.

The only choice that is actually a transmembrane protein is "integrins." This class of protein has several important functions, including anchoring the extracellular matrix to the cell. Integrins serve as the connection between the actin cytoskeleton and the extracellular matrix. Integrins directly interact with fibronectins to help hold important proteins, such as collagens and laminins, in place. These proteins, however, are located outside of the cell and are not embedded in the membrane.

Type IV collagen is the major component of the basal lamina, which is a crucial sub-foundation for many tissue types and epithelia. Laminins and entactin are found in the basal lamina, but there is more Type IV collagen. Integrins and microfilaments are proteins with important structural functions in other contexts.