Drebrin-like protein (DBNL)

Drebrin-like protein (DBNL) is a multifunctional actin-binding adaptor protein encoded by the DBNL gene in humans[1][5]. DBNL integrates cytoskeletal reorganization with diverse signaling processes, acting as a molecular bridge between actin dynamics and signal transduction pathways[1][2][3]. It binds actin filaments and localizes to the cytoplasm, intracellular organelles, and the plasma membrane; its localization is sensitive to the state of actin polymerization[2][4]. Phosphorylation of DBNL modulates stem-cell characteristics and supports cancer cell invasiveness, while its post-transcriptional regulation can influence metastatic potential and cell adhesion[1]. DBNL is critical in processes such as nervous system development, podosome assembly, sarcomere organization in muscle, and cell migration[1][4]. Dysregulation has been implicated in cancer proliferation, migration, and metastasis[1]. DBNL exists mainly as a dimer under physiological conditions and features distinct protein domains, including an ADF-H (actin depolymerizing factor-homology) domain, a coiled-coil region, a proline-rich region, and an SH3 domain[2][4].

Other names

HIP-55HIP55SH3P7mAbp1ABP1Cervical SH3P7Cervical mucin-associated proteinDrebrin-FHPK1-interacting protein of 55 kDaSH3 domain-containing protein 7actin-binding protein 1