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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. Binds to membranes via its F-BAR domain and mediates membrane tubulation.
Gene References into Functions
Specifically, CKS1B and MAP2K5 significantly inhibited hepatitis C viral RNA replication. PACSIN1, by contrast, inhibited hepatitis C virus infection by decreasing the level of viral protein p7. PMID: 24205826
Data indicate that the structural capacity of N17 to fold back toward distal regions within huntingtin requires an interacting protein, protein kinase C and casein kinase 2 substrate in neurons 1 (PACSIN1). PMID: 23898200
Pacsin-1 plays a versatile role in sculpting cellular membranes that is likely dependent both on protein structure and membrane properties. PMID: 23236520
PACSIN1 represents a pDC-specific adaptor molecule that plays an important role in the TLR7/9-mediated type I IFN responses by pDCs in vitro and in vivo. PMID: 22488361
Phosphorylation of syndapin I F-BAR domain at two helix-capping motifs regulates membrane tubulation PMID: 22355135
PACSIN 1 (1-344) was crystallized & diffracted to resolution of 3.0 A. The crystal belonged to space group C2, with unit-cell parameters a=158.65, b=87.38, c=91.76 A, alpha=90.00, beta=113.61, gamma=90.00 degrees. There are 2 molecules in asymmetric unit. PMID: 20057076