Published online 29 December 2003. doi:10.1083/jcb.200307098
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 164, Number 1, 133-144
AHNAK interaction with the annexin 2/S100A10 complex regulates cell membrane cytoarchitecture
Christelle Benaud1,
Benoît J. Gentil1,
Nicole Assard1,
Magalie Court2,
Jerome Garin2,
Christian Delphin1 and
Jacques Baudier1
1 Laboratoire de Transduction du Signal, INSERM EMI-0104, DRDC-TS
2 Laboratoire de Chimie des Proteines, INSERM ERM-0201, DRDC-CP, CEA-Grenoble, 38054 Grenoble Cedex 9, France
Address correspondence to Jacques Baudier, INSERM EMI-0104, DRDC-TS, CEA-Grenoble, 17 rue des Martyrs, 38054 Grenoble Cedex 9, France. Tel.: (33) 4-38-78-43 28. Fax: (33) 4-38-78-50-58. email: jbaudier{at}cea.fr
Remodelling of the plasma membrane cytoarchitecture is crucial for the regulation of epithelial cell adhesion and permeability. In Madin-Darby canine kidney cells, the protein AHNAK relocates from the cytosol to the cytosolic surface of the plasma membrane during the formation of cellcell contacts and the development of epithelial polarity. This targeting is reversible and regulated by Ca2+-dependent cellcell adhesion. At the plasma membrane, AHNAK associates as a multimeric complex with actin and the annexin 2/S100A10 complex. The S100A10 subunit serves to mediate the interaction between annexin 2 and the COOH-terminal regulatory domain of AHNAK. Down-regulation of both annexin 2 and S100A10 using an annexin 2specific small interfering RNA inhibits the association of AHNAK with plasma membrane. In Madin-Darby canine kidney cells, down-regulation of AHNAK using AHNAK-specific small interfering RNA prevents cortical actin cytoskeleton reorganization required to support cell height. We propose that the interaction of AHNAK with the annexin 2/S100A10 regulates cortical actin cytoskeleton organization and cell membrane cytoarchitecture.
Key Words: actin; calcium; cytoskeleton; cell adhesion; S100B
The online version of this article includes supplemental material.
Abbreviation used in this paper: siRNA, small interfering RNA.

CiteULike
Complore
Connotea
Del.icio.us
Digg
Reddit
Technorati What's this?
This article has been cited by other articles:
-
Lee, I. H., Lim, H. J., Yoon, S., Seong, J. K., Bae, D. S., Rhee, S. G., Bae, Y. S.
(2008). Ahnak Protein Activates Protein Kinase C (PKC) through Dissociation of the PKC-Protein Phosphatase 2A Complex. J. Biol. Chem.
283: 6312-6320
[Abstract]
[Full Text]
-
Huang, Y., Laval, S. H., van Remoortere, A., Baudier, J., Benaud, C., Anderson, L. V. B., Straub, V., Deelder, A., Frants, R. R., den Dunnen, J. T., Bushby, K., van der Maarel, S. M.
(2007). AHNAK, a novel component of the dysferlin protein complex, redistributes to the cytoplasm with dysferlin during skeletal muscle regeneration. FASEB J.
21: 732-742
[Abstract]
[Full Text]
-
Babbin, B. A., Parkos, C. A., Mandell, K. J., Winfree, L. M., Laur, O., Ivanov, A. I., Nusrat, A.
(2007). Annexin 2 Regulates Intestinal Epithelial Cell Spreading and Wound Closure through Rho-Related Signaling. Am. J. Pathol.
170: 951-966
[Abstract]
[Full Text]
-
Haase, H.
(2007). Ahnak, a new player in {beta}-adrenergic regulation of the cardiac L-type Ca2+ channel. Cardiovasc Res
73: 19-25
[Abstract]
[Full Text]
-
De Seranno, S., Benaud, C., Assard, N., Khediri, S., Gerke, V., Baudier, J., Delphin, C.
(2006). Identification of an AHNAK Binding Motif Specific for the Annexin2/S100A10 Tetramer. J. Biol. Chem.
281: 35030-35038
[Abstract]
[Full Text]
-
Gokhale, N. A., Abraham, A., Digman, M. A., Gratton, E., Cho, W.
(2005). Phosphoinositide Specificity of and Mechanism of Lipid Domain Formation by Annexin A2-p11 Heterotetramer. J. Biol. Chem.
280: 42831-42840
[Abstract]
[Full Text]
-
Haase, H., Alvarez, J., Petzhold, D., Doller, A., Behlke, J., Erdmann, J., Hetzer, R., Regitz-Zagrosek, V., Vassort, G., Morano, I.
(2005). Ahnak is critical for cardiac Ca(v)1.2 calcium channel function and its {beta}-adrenergic regulation. FASEB J.
19: 1969-1977
[Abstract]
[Full Text]
-
Markoff, A., Gerke, V.
(2005). Expression and functions of annexins in the kidney. Am. J. Physiol. Renal Physiol.
289: F949-F956
[Abstract]
[Full Text]
-
Yamada, A., Irie, K., Hirota, T., Ooshio, T., Fukuhara, A., Takai, Y.
(2005). Involvement of the Annexin II-S100A10 Complex in the Formation of E-cadherin-based Adherens Junctions in Madin-Darby Canine Kidney Cells. J. Biol. Chem.
280: 6016-6027
[Abstract]
[Full Text]
-
Lee, I. H., You, J. O., Ha, K. S., Bae, D. S., Suh, P.-G., Rhee, S. G., Bae, Y. S.
(2004). AHNAK-mediated Activation of Phospholipase C-{gamma}1 through Protein Kinase C. J. Biol. Chem.
279: 26645-26653
[Abstract]
[Full Text]
-
Rescher, U., Gerke, V.
(2004). Annexins - unique membrane binding proteins with diverse functions. J. Cell Sci.
117: 2631-2639
[Abstract]
[Full Text]