Poliovirus receptor-related 1 (PVRL1), also known as nectin-1 and CD111 (formerly herpesvirus entry mediator C, HVEC) is a human protein of the
immunoglobulin superfamily (IgSF), also considered a member of the
nectins.[5] It is a membrane protein with three extracellular immunoglobulin domains, a single transmembrane helix and a cytoplasmic tail. The protein can mediate
Ca2+-independent
cellular adhesion further characterizing it as IgSF cell adhesion molecule (IgSF CAM).
Function
PVRL1 is an adhesion molecule found in a wide range of tissues where it localizes in various junctions such as the
adherens junction of
epithelial tissue or the
chemical synapse of
neurons. The cytoplasmic tail of PVRL1 can bind the protein
afadin which is a scaffolding protein that binds
actin.
In the chemical synapse PVRL1 interacts with
PVRL3 (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 the
axonal side and PVRL3 on the
dendritic side.
The protein has been revealed as one of the key players in mediating cellular entry of the
Herpes simplex virus by interacting with the viral glycoprotein D (gD).[6]
Bustos T, Simosa V, Pinto-Cisternas J, Abramovits W, Jolay L, Rodriguez L, Fernandez L, Ramela M (1992). "Autosomal recessive ectodermal dysplasia: I. An undescribed dysplasia/malformation syndrome". Am. J. Med. Genet. 41 (4): 398–404.
doi:
10.1002/ajmg.1320410403.
PMID1776626.
Lopez M, Eberlé F, Mattei MG, Gabert J, Birg F, Bardin F, Maroc C, Dubreuil P (1995). "Complementary DNA characterization and chromosomal localization of a human gene related to the poliovirus receptor-encoding gene". Gene. 155 (2): 261–5.
doi:
10.1016/0378-1119(94)00842-G.
PMID7721102.
Poliovirus receptor-related 1 (PVRL1), also known as nectin-1 and CD111 (formerly herpesvirus entry mediator C, HVEC) is a human protein of the
immunoglobulin superfamily (IgSF), also considered a member of the
nectins.[5] It is a membrane protein with three extracellular immunoglobulin domains, a single transmembrane helix and a cytoplasmic tail. The protein can mediate
Ca2+-independent
cellular adhesion further characterizing it as IgSF cell adhesion molecule (IgSF CAM).
Function
PVRL1 is an adhesion molecule found in a wide range of tissues where it localizes in various junctions such as the
adherens junction of
epithelial tissue or the
chemical synapse of
neurons. The cytoplasmic tail of PVRL1 can bind the protein
afadin which is a scaffolding protein that binds
actin.
In the chemical synapse PVRL1 interacts with
PVRL3 (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 the
axonal side and PVRL3 on the
dendritic side.
The protein has been revealed as one of the key players in mediating cellular entry of the
Herpes simplex virus by interacting with the viral glycoprotein D (gD).[6]
Bustos T, Simosa V, Pinto-Cisternas J, Abramovits W, Jolay L, Rodriguez L, Fernandez L, Ramela M (1992). "Autosomal recessive ectodermal dysplasia: I. An undescribed dysplasia/malformation syndrome". Am. J. Med. Genet. 41 (4): 398–404.
doi:
10.1002/ajmg.1320410403.
PMID1776626.
Lopez M, Eberlé F, Mattei MG, Gabert J, Birg F, Bardin F, Maroc C, Dubreuil P (1995). "Complementary DNA characterization and chromosomal localization of a human gene related to the poliovirus receptor-encoding gene". Gene. 155 (2): 261–5.
doi:
10.1016/0378-1119(94)00842-G.
PMID7721102.