Paralemmin, also called Paralemmin-1 or PALM, is a widely expressed peripheral membrane protein that is involved in cell structure and shape. A hydrophobic protein, Paralemmin is anchored to the cytoplasmic side of the cell membrane via di-palmitoylation and prenylation of its C-terminal cysteine cluster. Functioning at the synapse to regulate neuronal plasticity and plasma membrane dynamics, Paralemmin can bind to the dopamine receptor D3, thereby reducing D3 expression and subsequent adenylate cyclase activity. Overexpression of Paralemmin induces fibroblasts to extend long filopodia and to assume extreme cell shapes, suggesting involvement in the formation and stabilization of the plasma membrane. Two isoforms of Paralemmin exists due to alternative splicing events.