Poliovirus receptor-related 1

Last updated

NECTIN1
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases NECTIN1 , CD111, CLPED1, ED4, HIgR, HV1S, HVEC, OFC7, PRR, PRR1, PVRR, PVRR1, SK-12, nectin-1, PVRL1, nectin cell adhesion molecule 1
External IDs OMIM: 600644 MGI: 1926483 HomoloGene: 2138 GeneCards: NECTIN1
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_203286
NM_002855
NM_032767
NM_203285

NM_021424

RefSeq (protein)

NP_002846
NP_976030
NP_976031

NP_067399

Location (UCSC) Chr 11: 119.62 – 119.73 Mb Chr 9: 43.66 – 43.74 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

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).

Contents

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]

See also

Interactions

PVRL1 has been shown to interact with MLLT4. [7]

Related Research Articles

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<span class="mw-page-title-main">Herpes simplex virus</span> Species of virus

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CD155, also known as the poliovirus receptor, is a protein that in humans is encoded by the PVR gene. It is a transmembrane protein that is involved in forming junctions between neighboring cells. It is also the molecule that poliovirus uses to enter cells. The gene is specific to the primate lineage.

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<span class="mw-page-title-main">Afadin</span> Protein-coding gene in the species Homo sapiens

Afadin is a protein that in humans is encoded by the AFDN gene.

<span class="mw-page-title-main">Poliovirus receptor-related 2</span> Protein-coding gene in the species Homo sapiens

Poliovirus receptor-related 2 (PVRL2), also known as nectin-2 and CD112, is a human plasma membrane glycoprotein.

<span class="mw-page-title-main">Herpesvirus entry mediator</span> Protein-coding gene in the species Homo sapiens

Herpesvirus entry mediator (HVEM), also known as tumor necrosis factor receptor superfamily member 14 (TNFRSF14), is a human cell surface receptor of the TNF-receptor superfamily.

<span class="mw-page-title-main">CREB3</span> Protein-coding gene in the species Homo sapiens

Cyclic AMP-responsive element-binding protein 3 is a protein that in humans is encoded by the CREB3 gene.

<span class="mw-page-title-main">EIF3M</span> Protein-coding gene in the species Homo sapiens

Eukaryotic translation initiation factor 3, subunit M (eIF3m) also known as PCI domain containing 1 (herpesvirus entry mediator) (PCID1), is a protein that in humans is encoded by the EIF3M gene.

Nectins and Nectin-like molecules (Necl) are families of cellular adhesion molecules involved in Ca2+-independent cellular adhesion.

<span class="mw-page-title-main">Herpesvirus glycoprotein B</span> Viral glycoprotein

Herpesvirus glycoprotein B is a viral glycoprotein that is involved in the viral cell entry of Herpes simplex virus (HSV). Herpesviruses have a lipid bilayer, called the envelope, which contains twelve surface glycoproteins. For infectivity to be attained, the double stranded DNA genome of HSV must enter the host cell through means of fusion of its envelope with the cellular membrane or via endocytosis. Other viral glycoproteins involved in the process of viral cell entry include gC, gB, gD, gH, and gL, but only gC, gB, gD, and gH are required for the fusion of the HSV's envelope with the cellular membrane. It can be noted that all herpesviruses have glycoproteins gB, gH, and gL.

Gabriella Campadelli-Fiume is a virologist with a primary research focus on herpes simplex virus, fusion and viral entry. She is a retired professor of virology from the University of Bologna, Italy.

<span class="mw-page-title-main">PILRA</span> Protein-coding gene in the species Homo sapiens

Paired immunoglobin like type 2 receptor alpha is a protein that in humans is encoded by the PILRA gene.

Patricia Gail Spear is an American virologist. She is a professor emeritus of microbiology and immunology at Northwestern University in Evanston, Illinois. She is best known for her pioneering work studying the herpes simplex virus. Spear is a past president of the American Society for Virology and an elected member of the National Academy of Sciences.

<span class="mw-page-title-main">Nectin-3</span>

Nectin-3, also known as nectin cell adhesion molecule 3, is a protein that in humans is encoded by the NECTIN3 gene.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000110400 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000032012 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. "Entrez Gene: PVRL1 poliovirus receptor-related 1 (herpesvirus entry mediator C; nectin)".
  6. Cocchi F, Lopez M, Menotti L, Aoubala M, Dubreuil P, Campadelli-Fiume G (1999). "The V domain of herpesvirus Ig-like receptor (HIgR) contains a major functional region in herpes simplex virus-1 entry into cells and interacts physically with the viral glycoprotein D". Proc. Natl. Acad. Sci. U.S.A. 95 (26): 15700–5. doi: 10.1073/pnas.95.26.15700 . PMC   28107 . PMID   9861033.
  7. Takahashi K, Nakanishi H, Miyahara M, Mandai K, Satoh K, Satoh A, Nishioka H, Aoki J, Nomoto A, Mizoguchi A, Takai Y (May 1999). "Nectin/PRR: An Immunoglobulin-like Cell Adhesion Molecule Recruited to Cadherin-based Adherens Junctions through Interaction with Afadin, a PDZ Domain–containing Protein". J. Cell Biol. 145 (3): 539–49. doi:10.1083/jcb.145.3.539. PMC   2185068 . PMID   10225955.

Further reading

This article incorporates text from the United States National Library of Medicine, which is in the public domain.