The heterogeneity of peroxisomal matrix proteins which are imported in a folded, even oligomeric state, requires adaptive and dynamic properties of the translocation machinery. Dynamic multicompartmental subcellular distribution of peroxisomal proteins is governed by the accessibility of targeting signals. Conformational changes of peroxisomal targeting receptors upon cargo-binding might serve as a docking 'quality control'. Although the mechanisms are not understood in detail, recent work suggests the existence of a transient translocon within the peroxisomal membrane. Rapid formation and disassembly of the transient import pore ensures the integrity of the peroxisomal membrane barrier for small metabolites. In this review, we will focus on the regulatory aspects of peroxisomal matrix protein import.