Role of the second immunoglobulin-like loop of nectin in cell-cell adhesion

Biochemical and Biophysical Research Communications

Volumn 293, Issue 1, 2002, Pages 45-49

  Momose, Yumiko ^a   Honda, Tomoyuki ^a   Inagaki, Maiko ^a   Shimizu, Kazuya ^a   Irie, Kenji ^a   Nakanishi, Hiroyuki ^a   Takai, Yoshimi ^a  

^a OSAKA UNIVERSITY GRADUATE SCHOOL OF MEDICINE   (Japan)

Author keywords

Adherens junctions; Cell cell adhesion; cis Dimers; Ig like cell adhesion molecule; Nectin; trans Dimers

Indexed keywords

CELL ADHESION MOLECULE; DIMER; IMMUNOGLOBULIN; NECTIN 2; UNCLASSIFIED DRUG; UVOMORULIN;

ANIMAL CELL; ARTICLE; CELL ADHESION; CELL AGGREGATION; CELL JUNCTION; CIS ISOMER; CONTROLLED STUDY; DIMERIZATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; TRANS ISOMER;

ANIMALS; CELL ADHESION; CELL ADHESION MOLECULES; CELL AGGREGATION; CERCOPITHECUS AETHIOPS; COS CELLS; DIMERIZATION; IMMUNOGLOBULINS; MICE; PROTEIN STRUCTURE, SECONDARY; TRANSFECTION;

EID: 0036293996     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-291X(02)00183-3     Document Type: Article

References (21)

1. Mouse homolog of poliovirus receptor-related gene 2 product, mPRR2, mediates homophilic cell aggregation
2. The human poliovirus receptor related 2 protein is a new hematopoietic/endothelial homophilic adhesion molecule
3. Nectin/PRR: An immunoglobulin-like cell adhesion molecule recruited to cadherin-based adherens junctions through interaction with afadin, a PDZ domain-containing protein
4. Interaction of nectin with afadin is necessary for its clustering at cell-cell contact sites but not for its cis dimerization or trans interaction
5. Nectin-3, a new member of immunoglobulin-like cell adhesion molecules that shows homophilic and heterophilic cell-cell adhesion activities
6. Two cell adhesion molecules, nectin and cadherin, interact through their cytoplasmic domain-associated proteins
7. Nectin4/PRR4: A new afadin-associated member of the nectin family that trans-interacts with nectin1/PRR1 through V domain interaction
8. Nectin: An adhesion molecule involved in formation of synapses
9. Molecular cloning and expression of a murine homolog of the human poliovirus receptor gene
10. Amino acid residues on human poliovirus receptor involved in interaction with poliovirus
11. The human PRR2 gene, related to the human poliovirus receptor gene (PVR), is the true homolog of the murine MPH gene
12. Complementary DNA characterization and chromosomal localization of a human gene related to the poliovirus receptor-encoding gene
13. 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
14. Entry of alphaherpesviruses mediated by poliovirus receptor-related protein 1 and poliovirus receptor
15. A cell surface protein with herpesvirus entry activity (HveB) confers susceptibility to infection by mutants of herpes simplex virus type 1, herpes simplex virus type 2, and pseudorabies virus
16. Cell-to-cell spread of wild-type herpes simplex virus type 1, but not of syncytial strains, is mediated by the immunoglobulin-like receptors that mediate virion entry, nectin1 (PRR1/HveC/ HIgR) and nectin2 (PRR2/HveB)
17. Requirement of interaction of nectin-1alpha/HveC with afadin for efficient cell-cell spread of herpes simplex virus type 1
18. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
19. Cleavage of structural proteins during the assembly of the head of bacteriophage T4
20. Effects of herpes simplex virus on structure and function of necin-1/HveC