The fully linked HTML version of this article has now been published.
Development ePress online publication date 2 Feb 2005
doi: 10.1242/dev.01645
Research article
aPKC, Crumbs3 and Lgl2 control apicobasal polarity in early vertebrate development
Andrew D. Chalmers,
Michael Pambos,
Julia Mason,
Stephanie Lang,
Chris Wylie,
and
Nancy Papalopulu*
* Author for correspondence (e-mail: np209{at}mole.bio.cam.ac.uk)
In early vertebrate development, apicobasally polarised blastomeres divide to produce inner non-polarised cells and outer polarised cells that follow different fates. How the polarity of these early blastomeres is established is not known. We have examined the role of Crumbs3, Lgl2 and the apical aPKC in the polarisation of frog blastomeres. Lgl2 localises to the basolateral membrane of blastomeres, while Crumbs3 localises to the apical and basolateral membranes. Overexpression aPKC and Crumbs3 expands the apical domain at the expense of the basolateral and repositions tight junctions in the new apical-basolateral interface. Loss of aPKC function causes loss of apical markers and redirects basolateral markers ectopically to the apical membrane. Cell polarity and tight junctions, but not cell adhesion, are lost and outer polarised cells become inner-like apolar cells. Overexpression of Xenopus Lgl2 phenocopies the aPKC knockout, suggesting that Lgl2 and aPKC act antagonistically. This was confirmed by showing that aPKC and Lgl2 can inhibit the localisation of each other and that Lgl2 rescues the apicalisation caused by aPKC. We conclude that an instrumental antagonistic interaction between aPKC and Lgl2 defines apicobasal polarity in early vertebrate development.
This article has been cited by other articles:
|
|
|
|
 
O. Ossipova, J. Tabler, J. B. A. Green, and S. Y. Sokol
PAR1 specifies ciliated cells in vertebrate ectoderm downstream of aPKC
Development,
December 1, 2007;
134(23):
4297 - 4306.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
C. U. Bialucha, E. C. Ferber, F. Pichaud, S. Y. Peak-Chew, and Y. Fujita
p32 is a novel mammalian Lgl binding protein that enhances the activity of protein kinase C{zeta} and regulates cell polarity
J. Cell Biol.,
August 9, 2007;
178(4):
575 - 581.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
M. Kim, A. Datta, P. Brakeman, W. Yu, and K. E. Mostov
Polarity proteins PAR6 and aPKC regulate cell death through GSK-3beta in 3D epithelial morphogenesis
J. Cell Sci.,
July 15, 2007;
120(14):
2309 - 2317.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
C. Lee, H. M. Scherr, and J. B. Wallingford
Shroom family proteins regulate {gamma}-tubulin distribution and microtubule architecture during epithelial cell shape change
Development,
April 1, 2007;
134(7):
1431 - 1441.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
P. D. Fairbank, C. Lee, A. Ellis, J. D. Hildebrand, J. M. Gross, and J. B. Wallingford
Shroom2 (APXL) regulates melanosome biogenesis and localization in the retinal pigment epithelium
Development,
October 15, 2006;
133(20):
4109 - 4118.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
B. Strauss, R. J. Adams, and N. Papalopulu
A default mechanism of spindle orientation based on cell shape is sufficient to generate cell fate diversity in polarised Xenopus blastomeres
Development,
October 1, 2006;
133(19):
3883 - 3893.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
T. Yamanaka, Y. Horikoshi, N. Izumi, A. Suzuki, K. Mizuno, and S. Ohno
Lgl mediates apical domain disassembly by suppressing the PAR-3-aPKC-PAR-6 complex to orient apical membrane polarity
J. Cell Sci.,
May 15, 2006;
119(10):
2107 - 2118.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
M. Sonawane, Y. Carpio, R. Geisler, H. Schwarz, H.-M. Maischein, and C. Nuesslein-Volhard
Zebrafish penner/lethal giant larvae 2 functions in hemidesmosome formation, maintenance of cellular morphology and growth regulation in the developing basal epidermis
Development,
July 15, 2005;
132(14):
3255 - 3265.
[Abstract]
[Full Text]
[PDF]
|
|
|
© The Company of Biologists Ltd 2005
