Poliovirus receptor-related 1

Poliovirus receptor-related 1 (PVRL1), also known as Nectin-1, is a protein that in humans is encoded by the PVRL1 gene. It is a cell adhesion molecule involved in the formation of adherens junctions, and plays a crucial role in the pathogenesis of several diseases, including poliomyelitis and herpes simplex infection.

Structure

PVRL1 is a member of the nectin and nectin-like (Necl) family of proteins, which are related to the immunoglobulin superfamily. It is a type I transmembrane protein with three extracellular immunoglobulin-like domains, a single transmembrane domain, and a cytoplasmic tail. The extracellular domains are involved in cell adhesion and virus binding, while the cytoplasmic tail interacts with the actin cytoskeleton through afadin, a PDZ domain-containing protein.

Function

PVRL1 functions as a cell adhesion molecule, mediating cell-cell interactions and regulating cell polarity and tissue architecture. It is involved in the formation of adherens junctions, a type of cell junction that connects the actin cytoskeletons of neighboring cells. PVRL1 also serves as a receptor for certain viruses, including poliovirus and herpes simplex virus.

Clinical significance

Mutations in the PVRL1 gene are associated with Cleft lip and palate/ectodermal dysplasia syndrome, a rare genetic disorder characterized by cleft lip and/or palate, ectodermal dysplasia, and other abnormalities. PVRL1 is also implicated in the pathogenesis of several viral diseases. It serves as a receptor for poliovirus, facilitating the virus's entry into cells. In addition, PVRL1 is a receptor for herpes simplex virus, and its expression is upregulated in herpes simplex virus-infected cells.

See also

• Nectin
• Cell adhesion
• Poliomyelitis
• Herpes simplex

References

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