The endoplasmic reticulum, while crucial to protein synthesis, is also an intracellular calcium storage organelle, and calcium can be released in response to signaling cascades as needed. None of the other organelles listed participates in storage of calcium.

The Golgi apparatus is a complex organelle with many various functions. These functions are primarily dedicated to protein modification, protein packaging, and protein sorting. Some of post-translational modifications that take place in this organelle include glycosylation and phosphorylation. The Golgi apparatus is an important relay in the secretory pathway, as it produces the vesicles that contain most secreted peptides.

The correct answer is ADP ribosylation factors (ARFs). ARFs are active when bound by GTP, and inactive when bound by GDP. The active GTP-bound form of ARF binds the vesicle coat protein 1 (COPI), to faciliate vesicle budding from the cis-Golgi face.

The Golgi apparatus is considered the post office of the cell; proteins are received, sorted, modified, and sent to their final cellular destination. The proteins required for the electron transport chain are localized to the mitochondria, and are not within the Golgi apparatus, thus this is the correct selection. 

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 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.

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. 

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. 

One of the most likely explanations for why intermediate filaments have no known motor proteins is because they are nonpolar. What this means is that there are no distinct ends to the filament. Motor proteins have ways of detecting which direction they are moving along actin or microtubules because they have distinct ends (polarization). Size should not affect the ability of a motor protein to function, especially because actin is smaller than intermediate filaments and microtubules are larger (hence the name "intermediate").

Eukaryotic flagella are composed of nine pairs of microtubules. In contrast, prokaryotic flagella are composed of the protein flagellin.