Mitochondria are surrounded by two biological membranes. The outer mitochondrial membrane contains two major translocators, the TOM40 (TOM) and TOB/SAM complexes for protein translocation across and/or insertion into the outer membrane. The TOM40 complex functions as an entry gate for most mitochondrial proteins, and the TOB/SAM complex as a specialized insertion machinery for β-barrel membrane proteins. In order to handle loosely folded or unfolded precursor polypeptides, those translocators cooperate with chaperones in the cytosol and intermembrane space, and also exhibit chaperone-like functions on their own. Several α-helical membrane proteins take ‘non-standard’ routes to be inserted into the outer membrane. Here we review the current view on a remarkable variety of mechanisms of protein transport taking place at the mitochondrial outer membrane.