alpha-Synuclein is a presynaptic protein that binds to phospholipid membranes and is involved in the pathogenesis of Parkinson's disease (PD). In this paper, we describe the effects of adding wild-type alpha-synuclein (WT) and three familial PD mutants (A53T, MOP, and E46K) to membranes containing 15-35 mol % anionic lipid. Tubules were observed to form in the membranes to an extent that depended on the alpha-synuclein variant, the anionic lipid content, and the protein concentration. For all four variants, tubule formation decreased with increasing anionic lipid content. Tubules were more readily observed with MOP and E46K than with WT or A53T. The results are consistent with a model wherein the helical content of alpha-synuclein increases with increasing anionic lipid content, and alpha-synuclein conformers with low helical content have a high propensity to induce tubule formation. This work, combined with previous work from our laboratory (Pandey et al. Biophys. J. 2009, 96, 540), shows that WT adsorption of the protein has deleterious effects on the membrane when the anionic lipid concentration is less than 30 mol % (tubule formation) or greater than 40 mol % (reorganization of the bilayer, clustering of protein).