PACSIN1 and EHD1 assemble membrane tubules from the developing intracellular cilium that attach to the plasma membrane creating an extracellular membrane channel to the outside of the cell.
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.
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).
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.
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.
The regulated deformation of membranes and promotion of tubule constrictions by Pacsin suggests a more versatile function of these proteins in vesiculation and endocytosis.
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