v5.1.0.3
Cicer data from the Legume Information System
| Type | Domain |
| 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 involved in 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 []. |
| Short Name | PSTPIP2_F-BAR |