Poliovirus receptor-related 1 (PVRL1), also known asnectin-1 andCD111 (formerlyherpesvirus entry mediator C,HVEC) is a human protein of theimmunoglobulin superfamily (IgSF), also considered a member of thenectins.[5] It is a membrane protein with three extracellular immunoglobulin domains, a single transmembrane helix and a cytoplasmic tail. The protein can mediateCa2+-independentcellular adhesion further characterizing it as IgSF cell adhesion molecule (IgSF CAM).
PVRL1 is an adhesion molecule found in a wide range of tissues where it localizes in various junctions such as theadherens junction ofepithelial tissue or thechemical synapse ofneurons. The cytoplasmic tail of PVRL1 can bind the proteinafadin which is a scaffolding protein that bindsactin.
In the chemical synapse PVRL1 interacts withPVRL3 (nectin-3) and both proteins can be found in neuronal tissue already in early stages of brain development as well as in aging brains. The two proteins have been found to localize asymmetrically along the chemical synapse, with PVRL1 primarily on theaxonal side and PVRL3 on thedendritic side.
The protein has been revealed as one of the key players in mediating cellular entry of theHerpes simplex virus by interacting with the viral glycoprotein D (gD).[6]
PVRL1 has been shown tointeract withMLLT4.[7]
This article incorporates text from theUnited States National Library of Medicine, which is in thepublic domain.
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