TY - JOUR
T1 - Nectin/PRR
T2 - An immunoglobulin-like cell adhesion molecule recruited to cadherin-based adherens junctions through interaction with afadin, a PDZ domain-containing protein
AU - Takahashi, Kenichi
AU - Nakanishi, Hiroyuki
AU - Miyahara, Masako
AU - Mandai, Kenji
AU - Satoh, Keiko
AU - Satoh, Ayako
AU - Nishioka, Hideo
AU - Aoki, Junken
AU - Nomoto, Akio
AU - Mizoguchi, Akira
AU - Takai, Yoshimi
PY - 1999/5/3
Y1 - 1999/5/3
N2 - We have isolated a novel actin filament-binding protein, named afadin, localized at cadherin-based cell-cell adherens junctions (AJs) in various tissues and cell lines. Afadin has one PDZ domain, three proline-rich regions, and one actin filament-binding domain. We found here that afadin directly interacted with a family of the immunoglobulin superfamily, which was isolated originally as the poliovirus receptor-related protein (PRR) family consisting of PRR1 and -2, and has been identified recently to be the alphaherpes virus receptor. PRR has a COOH-terminal consensus motif to which the PDZ domain of afadin binds. PRR and afadin were colocalized at cadherin- based cell-cell AJs in various tissues and cell lines. In E-cadherin- expressing EL cells, PRR was recruited to cadherin-based cell-cell AJs through interaction with afadin. PRR showed Ca2+-independent cell-cell adhesion activity. These results indicate that PRR is a cell-cell adhesion molecule of the immunoglobulin superfamily which is recruited to cadherin- based cell-cell AJs through interaction with afadin. We rename PRR as nectin (taken from the Latin word 'necto' meaning 'to connect').
AB - We have isolated a novel actin filament-binding protein, named afadin, localized at cadherin-based cell-cell adherens junctions (AJs) in various tissues and cell lines. Afadin has one PDZ domain, three proline-rich regions, and one actin filament-binding domain. We found here that afadin directly interacted with a family of the immunoglobulin superfamily, which was isolated originally as the poliovirus receptor-related protein (PRR) family consisting of PRR1 and -2, and has been identified recently to be the alphaherpes virus receptor. PRR has a COOH-terminal consensus motif to which the PDZ domain of afadin binds. PRR and afadin were colocalized at cadherin- based cell-cell AJs in various tissues and cell lines. In E-cadherin- expressing EL cells, PRR was recruited to cadherin-based cell-cell AJs through interaction with afadin. PRR showed Ca2+-independent cell-cell adhesion activity. These results indicate that PRR is a cell-cell adhesion molecule of the immunoglobulin superfamily which is recruited to cadherin- based cell-cell AJs through interaction with afadin. We rename PRR as nectin (taken from the Latin word 'necto' meaning 'to connect').
KW - Afadin
KW - Cadherin
KW - Immunoglobulin superfamily
KW - Poliovirus receptor-related protein
KW - Zonula adherens
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U2 - 10.1083/jcb.145.3.539
DO - 10.1083/jcb.145.3.539
M3 - Article
C2 - 10225955
AN - SCOPUS:0033519211
VL - 145
SP - 539
EP - 549
JO - Journal of Cell Biology
JF - Journal of Cell Biology
SN - 0021-9525
IS - 3
ER -