| Primary Identifier | IPR042694 | Type | Domain |
| Short Name | PSTPIP2_F-BAR |
| description | F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization []. Proline-Serine-Threonine Phosphatase-Interacting Protein 2 (PSTPIP2) is mostly expressed in hematopoietic cells but is also expressed in the brain. It is involvedin regulating cell adhesion and motility []. Mutations in the gene encoding murine PSTPIP2 can cause autoinflammatory disorders such as chronic multifocal osteomyelitis and macrophage autoinflammatory disease []. PSTPIP2 contains an N-terminal F-BAR domain and lacks the PEST motifs and SH3 domain that are found in PSTPIP1. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules []. |
