Role of each immunoglobulin-like loop of nectin for its cell-cell adhesion activity

Biochemical and Biophysical Research Communications

Volumn 302, Issue 1, 2003, Pages 61-66

  Yasumi, Masato ^a   Shimizu, Kazuya ^a   Honda, Tomoyuki ^a   Takeuchi, Masakazu ^b   Takai, Yoshimi ^a  

^a OSAKA UNIVERSITY GRADUATE SCHOOL OF MEDICINE   (Japan)

^b KAN Research Institute Inc ^*  (Japan)

Author keywords

Adherens junctions; Cell cell adhesion molecule; Immunoglobulin like loop; Nectin

Indexed keywords

ALKALINE PHOSPHATASE; CELL ADHESION MOLECULE; DIMER; IMMUNOGLOBULIN FRAGMENT; IMMUNOGLOBULIN G; NECTIN 1; NECTIN 3; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; CELL ADHESION; CELL FUSION; CONTROLLED STUDY; DIMERIZATION; EXTRACELLULAR MATRIX; GENETIC RECOMBINATION; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION;

EID: 0037470536     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-291X(03)00106-2     Document Type: Article

References (18)

1. Takai Y., Nakanishi H. Nectin and afadin: novel organizers of intercellular junctions. J. Cell Sci. 116:2003;17-27.
2. Aoki J., Koike S., Asou H., Ise I., Suwa H., Tanaka T., Miyasaka M., Nomoto A. Mouse homolog of poliovirus receptor-related gene 2 product, mPRR2, mediates homophilic cell aggregation. Exp. Cell Res. 235:1997;374-384.
3. Lopez M., Aoubala M., Jordier F., Isnardon D., Gomez S., Dubreuil P. The human poliovirus receptor related 2 protein is a new hematopoietic/endothelial homophilic adhesion molecule. Blood. 92:1998;4602-4611.
4. Takahashi K., Nakanishi H., Miyahara M., Mandai K., Satoh K., Satoh A., Nishioka H., Aoki J., Nomoto A., Mizoguchi A., Takai Y. 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. 145:1999;539-549.
5. Miyahara M., Nakanishi H., Takahashi K., Satoh-Horikawa K., Tachibana K., Takai Y. Interaction of nectin with afadin is necessary for its clustering at cell-cell contact sites but not for its cis dimerization or trans interaction. J. Biol. Chem. 275:2000;613-618.
6. Satoh-Horikawa K., Nakanishi H., Takahashi K., Miyahara M., Nishimura M., Tachibana K., Mizoguchi A., Takai Y. Nectin-3, a new member of immunoglobulin-like cell adhesion molecules that shows homophilic and heterophilic cell-cell adhesion activities. J. Biol. Chem. 275:2000;10291-10299.
7. Tachibana K., Nakanishi H., Mandai K., Ozaki K., Ikeda W., Yamamoto Y., Nagafuchi A., Tsukita S., Takai Y. Two cell adhesion molecules, nectin and cadherin, interact through their cytoplasmic domain-associated proteins. J. Cell Biol. 150:2000;1161-1175.
8. Reymond N., Fabre S., Lecocq E., Adelaide J., Dubreuil P., Lopez M. Nectin4/PRR4: a new afadin-associated member of the nectin family that trans-interacts with nectin1/PRR1 through V domain interaction. J. Biol. Chem. 276:2001;43205-43215.
9. Mizoguchi A., Nakanishi H., Kimura K., Matsubara K., Ozaki-Kuroda K., Katata T., Honda T., Kiyohara Y., Heo K., Higashi M., Tsutsumi T., Sonoda S., Ide C., Takai Y. Nectin: an adhesion molecule involved in formation of synapses. J. Cell Biol. 156:2002;555-565.
10. Ozaki-Kuroda K., Nakanishi H., Ohta H., Tanaka H., Kurihara H., Mueller S., Irie K., Ikeda W., Sasaki T., Wimmer E., Nishimune Y., Takai Y. Nectin couples cell-cell adhesion and actin scaffold at heterotypic testicular junctions. Curr. Biol. 12:2002;1145-1150.
11. Sakisaka T., Taniguchi T., Nakanishi H., Takahashi K., Miyahara M., Ikeda W., Yokoyama S., Peng Y.F., Yamanishi K., Takai Y. Requirement of interaction of nectin-1α/HveC with afadin for efficient cell-cell spread of herpes simplex virus type 1. J. Virol. 75:2001;4734-4743.
12. Momose Y., Honda T., Inagaki M., Shimizu K., Irie K., Nakanishi H., Takai Y. Role of the second immunoglobulin-like loop of nectin in cell-cell adhesion. Biochem. Biophys. Res. Commun. 293:2002;45-49.
13. Honda T., Shimizu K., Kawakatsu T., Yasumi M., Shingai T., Fukuhara A., Ozaki-Kuroda K., Irie K., Nakanishi H., Takai Y. Antagonistic and agonistic effects of an extracellular fragment of nectin on formation of E-cadherin-based cell-cell adhesion. Genes Cells. 8:2003;51-63.
14. ′ C″ -D β-strands of the nectin 1 V domain J. Biol. Chem. 277:2002;27006-27013.
15. Imai T., Baba M., Nishimura M., Kakizaki M., Takagi S., Yoshie O. The T cell-directed CC chemokine TARC is a highly specific biological ligand for CC chemokine receptor 4. J. Biol. Chem. 272:1997;15036-15042.
16. Nagafuchi A., Shirayoshi Y., Okazaki K., Yasuda K., Takeichi M. Transformation of cell adhesion properties by exogenously introduced E-cadherin cDNA. Nature. 329:1987;341-343.
17. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
18. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.