Palladin

Palladin protein is a cytoskeletal protein coded by the palladin gene (KIAA0992).

Palladin was characterised independently by two research groups, first in the lab of Carol Otey (in 2000) and then in the lab of Olli Carpén (in 2001). It is a part of the myotilin-myopalladin-palladin family and may play an important role in modulating the actin cytoskeleton. Palladin, in contrast to myotilin and myopalladin, which are expressed only in striated muscle, is expressed ubiquitously in cells of mesenchymal origin.

Three major isoforms of palladin arise from a single gene. These isoforms contain between three and five copies (depending on the isoform) of an Ig-like domain and between one and two copies of a polyproline domain. Its precise biological role is yet poorly understood, but it has been shown to play a role in cytoskeletal organization, embryonic development, cell motility, scar formation in the skin, and nerve cell development.

Recently, it has been demonstrated that palladin RNA is overexpressed in patients with pancreatic neoplasia, and that palladin is both overexpressed and mutated in an inherited form of pancreatic cancer. More research is required before this protein and its role in neoplasia can be fully understood.

Palladin was named after the Renaissance architect Andrea Palladio, reflecting its localization to architectural elements of the cell.