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 [].
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 [].
PACSIN1 and PACSIN2 belong to the PACSIN family that contains a N-terminal F-BAR (FCH-BAR) domain and a C-terminal SH3 domain []. They are cytoplasmic phosphoproteins that play a role in vesicle formation and transport [].PACSIN1 (also known as Syndapin-1) 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 []. PACSIN2 interacts with several proteins such as Rac1, dynamin, Neuronal Wiskott-Aldrich Syndrome Protein (N-WASP), and synaptojanin via its C-terminal SH3 domain []. PACSIN2 negatively regulates the EGF (epidermal growth factor) receptor activation and signaling [, ]. It plays an important role in caveolae membrane sculpting []. This entry represents the SH3 domain of PACSINs 1 and 2.
