The flatworm features a duo-gland adhesive system that allows it to repeatedly attach to and release from substrates in seawater within a minute. However， little is known about the molecules involved in this temporary adhesion. In this study， we show that the attachment of relies on the secretion of two large adhesive proteins， adhesion protein 1 (Mlig-ap1) and Mlig-ap2. We revealed that both proteins are expressed in the adhesive gland cells and that their distribution within the adhesive footprints was spatially restricted. RNA interference knockdown experiments demonstrated the essential function of these two proteins in flatworm adhesion. Negatively charged modified sugars in the surrounding water inhibited flatworm attachment， while positively charged molecules impeded detachment. In addition， we found that could not adhere to strongly hydrated surfaces. We propose an attachment-release model where Mlig-ap2 attaches to the substrate and Mlig-ap1 exhibits a cohesive function. A small negatively charged molecule is secreted that interferes with Mlig-ap1， inducing detachment. These findings are of relevance for fundamental adhesion science and efforts to mitigate biofouling. Further， this model of flatworm temporary adhesion may serve as the starting point for the development of synthetic reversible adhesion systems for medicinal and industrial applications.