| Primary Identifier | IPR037454 | Type | Domain |
| Short Name | PACSIN1_F-BAR |
| description | PACSIN1 (protein kinase C and casein kinase substrate in neurons protein 1, also known as SYNDAPIN1) belongs to the PACSIN family that contains a N-terminal F-BAR (FCH-BAR) domain and a C-terminal SH3 domain []. There are three tissue-specific isoforms of PACSIN1 found in mammals: PACSIN11 is enriched in neurons, PACSIN12 is ubiquitously expressed, and PACSIN13 is found mainly in muscle []. They are cytoplasmic phosphoproteins that play a role in vesicle formation and transport [].PACSIN1 is upregulated upon differentiation into neuronal cells []. The SH3 domain of PACSIN1 mediates activation of neural WASP (N-WASP), which is required to regulate actin polymerisation and is essential for proper neuromorphogenesis and cellular motility []. Two phosphorylation sites within the F-BAR domain of PACSIN1 are used for membrane tubulation regulation []. This entry represents the F-BAR domain of PACSIN1. F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization []. |
