Paralemmin-1 (PALM1) is an alternatively spliced phosphoprotein of the paralemmin family, defined by a conserved paralemmin motif and a C-terminal prenylation/di-palmitoylation cysteine cluster (CaaX-like anchor) that targets the protein to the cytoplasmic face of membranes.
Paralemmin1 belongs to the Paralemmin family comprising four members (paralemmin1, ‑2, ‑3 and palmdelphin), which share a conserved domain structure. Palmdelphin is lacking the C‑terminal lipid anchor (3).
Functionally, Paralemmin-1 acts as a membrane-shape regulator linked to plasma-membrane dynamics, filopodia/process formation, dendritic spine maturation, and receptor-associated signaling (1, 2, 4). It localizes in discontinuous patches at the plasma membrane and endomembranes, prominently in neuronal perikarya, axons, dendrites, dendritic spines, and also in glial processes. Polarized membrane localization is seen in kidney and adrenal epithelia (1, 3). Paralemmin-1 expression is highest in brain, but also occurs in kidney, adrenal gland, lens fiber cells, retina, and lymphatic endothelial cells (1, 3, 5). Pathologically, increased paralemmin-1 is associated with breast cancer and contributes to tumor lymphangiogenesis (4, 5).