Class I and class II hydrophobins are small secreted fungal proteins that play a role in a broad range of processes in the growth and development of filamentous fungi. For instance, they are involved in the formation of aerial structures and in the attachment of hyphae to hydrophobic surfaces. The mechanisms by which hydrophobins fulfill these functions are based on their property to self-assemble at hydrophilic-hydrophobic interfaces into a 10 nm-thin highly amphipathic film. Complementation studies have shown that class I hydrophobins belong to a closely related group of morphogenetic proteins, but that they have evolved to function at specific interfaces. Recent evidence indicates that hydrophobins do not only function by self-assembly. Monomeric hydrophobin has been implicated in cell-wall assembly, but the underlying mechanism is not yet clear. In addition, hydrophobin monomers could act as toxins and elicitors.