PMID- 10583506
OWN - NLM
STAT- MEDLINE
DCOM- 20000113
LR  - 20211203
IS  - 1356-9597 (Print)
IS  - 1356-9597 (Linking)
VI  - 4
IP  - 10
DP  - 1999 Oct
TI  - Similar and differential behaviour between the nectin-afadin-ponsin and
      cadherin-catenin systems during the formation and disruption of the polarized
      junctional alignment in epithelial cells.
PG  - 573-81
AB  - BACKGROUND: We have recently identified a novel cell-cell adhesion system, named 
      NAP system, which is localized at cadherin-based cell-cell adherens junctions
      (AJs). The NAP system is composed of at least nectin, afadin and ponsin. Nectin
      is an immunoglobulin-like cell adhesion molecule. Afadin is an actin
      filament-binding protein which associates nectin with the actin cytoskeleton.
      Ponsin is an afadin-binding protein which furthermore binds to vinculin and
      provides a possible linkage of nectin-afadin to cadherin-catenin through
      vinculin. We compared here the behaviour of the NAP and cadherin-catenin systems 
      during the formation and disruption of the polarized junctional alignment in
      epithelial cells. RESULTS: At the early stage of the formation of the polarized
      junctional alignment in MTD-1 A cells, primordial spot-like junctions were formed
      at the tips of thin cellular protrusions radiating from adjacent cells. Nectin,
      afadin, ponsin, cadherin and catenin were simultaneously recruited to these
      junctions. As the cell polarization proceeded, the spot-like junctions were
      gradually fused to form belt-like AJs where all these proteins were concentrated.
      The disruption of cell-cell AJs in MDCK cells by culturing at a low Ca2+
      concentration caused rapid endocytosis of cadherin, but not that of nectin or
      afadin. Addition of 12-O-tetradecanoylphorbol-13-acetate to the cells formed a
      tight junction-like structure where nectin and afadin, but not cadherin,
      accumulated. CONCLUSION: These results indicate that the NAP and cadherin-catenin
      systems show similar and differential behaviour during the formation and
      disruption of the polarized junctional alignment in epithelial cells.
FAU - Asakura, T
AU  - Asakura T
AD  - Department of Molecular Biology and Biochemistry, Osaka University Graduate
      School of Medicine/Faculty of Medicine, Suita 565-0871, Japan.
FAU - Nakanishi, H
AU  - Nakanishi H
FAU - Sakisaka, T
AU  - Sakisaka T
FAU - Takahashi, K
AU  - Takahashi K
FAU - Mandai, K
AU  - Mandai K
FAU - Nishimura, M
AU  - Nishimura M
FAU - Sasaki, T
AU  - Sasaki T
FAU - Takai, Y
AU  - Takai Y
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Genes Cells
JT  - Genes to cells : devoted to molecular & cellular mechanisms
JID - 9607379
RN  - 0 (AFDN protein, human)
RN  - 0 (Afdn protein, mouse)
RN  - 0 (Cadherins)
RN  - 0 (Cell Adhesion Molecules)
RN  - 0 (Immunoglobulins)
RN  - 0 (Microfilament Proteins)
RN  - 0 (Nectins)
RN  - 0 (afadin)
RN  - 0 (ponsin)
RN  - EC 3.6.4.1 (Myosins)
RN  - EC 3.6.4.4 (Kinesins)
SB  - IM
MH  - Animals
MH  - Cadherins/*metabolism
MH  - Cell Adhesion/physiology
MH  - Cell Adhesion Molecules/*metabolism
MH  - Cell Line
MH  - Epithelial Cells/cytology/metabolism/*physiology
MH  - Humans
MH  - Immunoglobulins/*metabolism
MH  - Intercellular Junctions/chemistry/metabolism/*physiology
MH  - Kinesins
MH  - Mice
MH  - Microfilament Proteins/*metabolism
MH  - Microscopy, Fluorescence
MH  - Myosins
MH  - Nectins
MH  - Rabbits
EDAT- 1999/12/03 00:00
MHDA- 1999/12/03 00:01
CRDT- 1999/12/03 00:00
PHST- 1999/12/03 00:00 [pubmed]
PHST- 1999/12/03 00:01 [medline]
PHST- 1999/12/03 00:00 [entrez]
AID - gtc283 [pii]
AID - 10.1046/j.1365-2443.1999.00283.x [doi]
PST - ppublish
SO  - Genes Cells. 1999 Oct;4(10):573-81. doi: 10.1046/j.1365-2443.1999.00283.x.