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PACSIN1

Domain

The F-BAR domain forms a coiled coil and mediates membrane-binding and membrane tubulation. In the autoinhibited conformation, interaction with the SH3 domain inhibits membrane tubulation mediated by the F-BAR domain. DNM1 binding abolishes autoinhibition (By similarity).

Function

Plays a role in the reorganization of the microtubule cytoskeleton via its interaction with MAPT; this decreases microtubule stability and inhibits MAPT-induced microtubule polymerization. Plays a role in cellular transport processes by recruiting DNM1, DNM2 and DNM3 to membranes. Plays a role in the reorganization of the actin cytoskeleton and in neuron morphogenesis via its interaction with COBL and WASL, and by recruiting COBL to the cell cortex. Plays a role in the regulation of neurite formation, neurite branching and the regulation of neurite length. Required for normal synaptic vesicle endocytosis; this process retrieves previously released neurotransmitters to accommodate multiple cycles of neurotransmission. Required for normal excitatory and inhibitory synaptic transmission (By similarity). Binds to membranes via its F-BAR domain and mediates membrane tubulation.

Post-translational modifications

Phosphorylated by casein kinase 2 (CK2) and protein kinase C (PKC).

Sequence Similarities

Belongs to the PACSIN family.

Tissue Specificity

Highly expressed in brain and, at much lower levels, in heart and pancreas.

Cellular localization

Alternative names

KIAA1379, PACSIN1, Protein kinase C and casein kinase substrate in neurons protein 1, Syndapin-1

swissprot:Q9BY11 omim:606512 entrezGene:29993