Proline-rich protein 14 (PRR14)

Proline-rich protein 14 (PRR14) is a 64 kDa nuclear protein that functions as a structural tether between heterochromatin and the nuclear lamina during interphase, via dual modular domains: an N-terminal HP1-heterochromatin binding domain and a C-terminal nuclear lamina binding domain[1][4]. PRR14 dynamically associates with chromatin and the nuclear periphery through the cell cycle, supporting chromatin organization, nuclear lamina association, and mitotic chromatin “bookmarking” roles[1]. It is regulated via phosphorylation, mediates nuclear structure, promotes myoblast differentiation by stimulating MyoD activity, and positively regulates the PI3K-Akt pathway, possibly through interacting with Grb2[2][3][5]. PRR14 is overexpressed in several cancers and linked to increased proliferation; however, it is not currently a direct therapeutic target[2][5]. Its closest paralog, PRR14L, is implicated in hematologic neoplasia.

Other names

PRR14MGC3121Proline-rich protein 14proline rich 14Proline rich 14

No direct mechanism of action for drugs is described, as PRR14 is not a current pharmacological target.