Nectin/PRR: an immunoglobulin-like cell adhesion molecule recruited to cadherin-based adherens junctions through interaction with Afadin, a PDZ domain-containing protein.
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").
Takahashi
K
K
Takai Biotimer Project, ERATO, Japan Science and Technology Corp., c/o JCR Pharmaceuticals Co., Ltd., Kobe 651-2241, Japan.
Nakanishi
H
H
Miyahara
M
M
Mandai
K
K
Satoh
K
K
Satoh
A
A
Nishioka
H
H
Aoki
J
J
Nomoto
A
A
Mizoguchi
A
A
Takai
Y
Y
D017398:Alternative Splicing / Q000235:genetics; D000595:Amino Acid Sequence; D000818:Animals; D019556:COS Cells / Q000737:chemistry / Q000378:metabolism; D015820:Cadherins / Q000378:metabolism*; D002118:Calcium / Q000378:metabolism; D015815:Cell Adhesion Molecules / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D002449:Cell Aggregation / Q000502:physiology; D004847:Epithelial Cells / Q000737:chemistry / Q000166:cytology / Q000378:metabolism; D007365:Intercellular Junctions / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure; D016547:Kinesins; D008562:Membrane Glycoproteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D051379:Mice; D008840:Microfilament Proteins / Q000737:chemistry / Q000378:metabolism*; D008854:Microscopy, Electron; D009206:Myocardium / Q000737:chemistry / Q000166:cytology / Q000378:metabolism; D009218:Myosins; D000075983:Nectins; D017434:Protein Structure, Tertiary; D011817:Rabbits; D018124:Receptors, Tumor Necrosis Factor; D053240:Receptors, Tumor Necrosis Factor, Member 14; D011991:Receptors, Virus; D016596:Vinculin / Q000378:metabolism
C095516:AFDN protein, human; C490657:Afdn protein, mouse; D015820:Cadherins; D015815:Cell Adhesion Molecules; D008562:Membrane Glycoproteins; D008840:Microfilament Proteins; D000075983:Nectins; D018124:Receptors, Tumor Necrosis Factor; D053240:Receptors, Tumor Necrosis Factor, Member 14; D011991:Receptors, Virus; C506028:TNFRSF14 protein, human; C506029:Tnfrsf14 protein, mouse; C108835:afadin; D016596:Vinculin; D009218:Myosins; D016547:Kinesins; D002118:Calcium