PMID- 10225955
OWN - NLM
STAT- MEDLINE
DCOM- 19990601
LR  - 20191210
IS  - 0021-9525 (Print)
IS  - 0021-9525 (Linking)
VI  - 145
IP  - 3
DP  - 1999 May 3
TI  - Nectin/PRR: an immunoglobulin-like cell adhesion molecule recruited to
      cadherin-based adherens junctions through interaction with Afadin, a PDZ
      domain-containing protein.
PG  - 539-49
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").
FAU - Takahashi, K
AU  - Takahashi K
AD  - Takai Biotimer Project, ERATO, Japan Science and Technology Corp., c/o JCR
      Pharmaceuticals Co., Ltd., Kobe 651-2241, Japan.
FAU - Nakanishi, H
AU  - Nakanishi H
FAU - Miyahara, M
AU  - Miyahara M
FAU - Mandai, K
AU  - Mandai K
FAU - Satoh, K
AU  - Satoh K
FAU - Satoh, A
AU  - Satoh A
FAU - Nishioka, H
AU  - Nishioka H
FAU - Aoki, J
AU  - Aoki J
FAU - Nomoto, A
AU  - Nomoto A
FAU - Mizoguchi, A
AU  - Mizoguchi A
FAU - Takai, Y
AU  - Takai Y
LA  - eng
PT  - Journal Article
PL  - United States
TA  - J Cell Biol
JT  - The Journal of cell biology
JID - 0375356
RN  - 0 (AFDN protein, human)
RN  - 0 (Afdn protein, mouse)
RN  - 0 (Cadherins)
RN  - 0 (Cell Adhesion Molecules)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Microfilament Proteins)
RN  - 0 (Nectins)
RN  - 0 (Receptors, Tumor Necrosis Factor)
RN  - 0 (Receptors, Tumor Necrosis Factor, Member 14)
RN  - 0 (Receptors, Virus)
RN  - 0 (TNFRSF14 protein, human)
RN  - 0 (Tnfrsf14 protein, mouse)
RN  - 0 (afadin)
RN  - 125361-02-6 (Vinculin)
RN  - EC 3.6.4.1 (Myosins)
RN  - EC 3.6.4.4 (Kinesin)
RN  - SY7Q814VUP (Calcium)
SB  - IM
MH  - Alternative Splicing/genetics
MH  - Amino Acid Sequence
MH  - Animals
MH  - COS Cells/chemistry/metabolism
MH  - Cadherins/*metabolism
MH  - Calcium/metabolism
MH  - Cell Adhesion Molecules/chemistry/*genetics/metabolism
MH  - Cell Aggregation/physiology
MH  - Epithelial Cells/chemistry/cytology/metabolism
MH  - Intercellular Junctions/chemistry/*metabolism/ultrastructure
MH  - Kinesin
MH  - Membrane Glycoproteins/chemistry/genetics/metabolism
MH  - Mice
MH  - Microfilament Proteins/chemistry/*metabolism
MH  - Microscopy, Electron
MH  - Myocardium/chemistry/cytology/metabolism
MH  - Myosins
MH  - Nectins
MH  - Protein Structure, Tertiary
MH  - Rabbits
MH  - *Receptors, Tumor Necrosis Factor
MH  - Receptors, Tumor Necrosis Factor, Member 14
MH  - *Receptors, Virus
MH  - Vinculin/metabolism
PMC - PMC2185068
EDAT- 1999/05/04 02:03
MHDA- 2000/05/29 09:00
CRDT- 1999/05/04 02:03
PHST- 1999/05/04 02:03 [pubmed]
PHST- 2000/05/29 09:00 [medline]
PHST- 1999/05/04 02:03 [entrez]
AID - 10.1083/jcb.145.3.539 [doi]
PST - ppublish
SO  - J Cell Biol. 1999 May 3;145(3):539-49. doi: 10.1083/jcb.145.3.539.