|
|
|
|||||||
|
|||||||||
J. Biol. Chem., Vol. 277, Issue 6, 4477-4484, February 8, 2002
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
From the Using a yeast two-hybrid screen, we identified a
physical interaction between CD46 and DLG4. CD46 is a ubiquitous human
cell-surface receptor for the complement components C3b and C4b and for
measles virus and human herpesvirus 6. DLG4 is a scaffold protein
important for neuronal signaling and is homologous to the
Drosophila tumor suppressor DLG. We show that an
interaction between CD46 and DLG4 is important for polarization in
epithelial cells. Specifically, we show (i) biochemical evidence for an
interaction between CD46 and DLG4, (ii) that this interaction is
specific for the Cyt1 (but not Cyt2) domain of CD46, (iii) that both
CD46 and an alternatively spliced isoform of DLG4 are polarized in
normal human epithelial cells, and (iv) that the polarized expression
of CD46 in epithelial cells requires the DLG4-binding domain and alters
with expression of a truncated form of DLG4. This is the first
identification of a direct and cytoplasmic domain-specific interaction
between CD46 and an intracellular signaling molecule and provides a
molecular mechanism for the polarization of CD46. These data also
indicate that, in addition to the known role for DLG4 in neuronal
cells, DLG4 may be important for polarization in epithelial cells.
A Functional Interaction between CD46 and DLG4
A ROLE FOR DLG4 IN EPITHELIAL POLARIZATION*
§,§,,
,, and**
Peter MacCallum Cancer Institute,
Trescowthick Research Laboratories, St. Andrew's Place, East
Melbourne, Victoria 3002, Australia and the ¶ Austin Research
Institute, Studley Road, Heidelberg, Victoria 3084, Australia
*
The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Present address: St. Vincent's Inst. of Medical Research, 9 Princes St., Fitzroy, Victoria 3065, Australia.
**
Supported by a Wellcome Senior Research Fellowship in Medical
Science in Australia. To whom correspondence should be addressed. Tel.: 613-9656-3727; Fax: 613-9656-1411; E-mail:
s.russell@pmci. unimelb.edu.au.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  J. Oliaro, A. Pasam, N. J. Waterhouse, K. A. Browne, M. J. Ludford-Menting, J. A. Trapani, and S. M. Russell Ligation of the cell surface receptor, CD46, alters T cell polarity and response to antigen presentation PNAS, December 5, 2006; 103(49): 18685 - 18690. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 N. J. Weyand, S. W. Lee, D. L. Higashi, D. Cawley, P. Yoshihara, and M. So Monoclonal Antibody Detection of CD46 Clustering beneath Neisseria gonorrhoeae Microcolonies Infect. Immun., April 1, 2006; 74(4): 2428 - 2435. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M. S. Kim, K. Yamashita, J. H. Baek, H. L. Park, A. L. Carvalho, M. Osada, M. O. Hoque, S. Upadhyay, M. Mori, C. Moon, et al. N-methyl-D-aspartate receptor type 2B is epigenetically inactivated and exhibits tumor-suppressive activity in human esophageal cancer. Cancer Res., April 1, 2006; 66(7): 3409 - 3418. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M. Mizuno, C. L. Harris, N. Suzuki, S. Matsuo, and B. P. Morgan Expression of CD46 in Developing Rat Spermatozoa: Ultrastructural Localization and Utility as a Marker of the Various Stages of the Seminiferous Tubuli Biol Reprod, April 1, 2005; 72(4): 908 - 915. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 B. Crimeen-Irwin, S. Ellis, D. Christiansen, M. J. Ludford-Menting, J. Milland, M. Lanteri, B. E. Loveland, D. Gerlier, and S. M. Russell Ligand Binding Determines Whether CD46 Is Internalized by Clathrin-coated Pits or Macropinocytosis J. Biol. Chem., November 21, 2003; 278(47): 46927 - 46937. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 B. J. McLaughlin, W. Fan, J. J. Zheng, H. Cai, L. V. Del Priore, N. S. Bora, and H. J. Kaplan Novel Role for a Complement Regulatory Protein (CD46) in Retinal Pigment Epithelial Adhesion Invest. Ophthalmol. Vis. Sci., August 1, 2003; 44(8): 3669 - 3674. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 S. W. Lee, R. A. Bonnah, D. L. Higashi, J. P. Atkinson, S. L. Milgram, and M. So CD46 is phosphorylated at tyrosine 354 upon infection of epithelial cells by Neisseria gonorrhoeae J. Cell Biol., March 18, 2002; 156(6): 951 - 957. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |