The endoplasmic reticulum resident chaperone HSP47 is essential for proper formation of the collagen triple helix. HSP47 has a number of unique properties: It is specific for collagens (or at least was thought to be); its client binding and release cycle is not governed by ATP binding/hydrolysis but rather by the pH shift occurring on the travel from the ER to the Golgi compartment; and its expression levels parallel the amount of collagen being synthesized, thus meaning it is upregulated in all kinds of fibrotic diseases. The talk will cover structure-function relationships of HSP47: the molecular details of its interaction with its clients, its mechanism of pH-mediated client release, a closer examination of the client repertoire, an attempt to identify specific small-molecule inhibitors, and the effects of a keratinocyte-specific knockout.