spacer gif spacer gif spacer gif spacer gif spacer gif
QUICK SEARCH:   [advanced]


spacer gif
     Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents    

First published online 9 January 2007
doi: 10.1242/jcs.03336

Journal of Cell Science 120, 395-406 (2007)
Published by The Company of Biologists 2007
This Article
Right arrow Figures Only
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplementary Material
Right arrow All Versions of this Article:
jcs.03336v1
120/3/395    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Neumann-Giesen, C.
Right arrow Articles by Tikkanen, R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Neumann-Giesen, C.
Right arrow Articles by Tikkanen, R.

Research Article

Role of EGF-induced tyrosine phosphorylation of reggie-1/flotillin-2 in cell spreading and signaling to the actin cytoskeleton

Carolin Neumann-Giesen, Inga Fernow, Monia Amaddii and Ritva Tikkanen*

Institute of Biochemistry II, University Clinic of Frankfurt am Main and Cluster of Excellence, Frankfurt, Theodor-Stern-Kai 7, 60590 Frankfurt am Main, Germany

* Author for correspondence (e-mail: tikkanen{at}biochem2.de)

Accepted 13 November 2006

Cholesterol and sphingolipid-rich membrane microdomains or rafts have been shown to be involved in signaling through many growth factor receptors but the molecular details of these processes are not well understood. The reggie/flotillin proteins are ubiquitously expressed proteins with a poorly characterized function. They are constitutively associated with membrane rafts by means of acylation and oligomerization. Previous studies have implicated reggies in signaling, regulation of actin cytoskeleton and in membrane transport processes. In this study, we analyzed the putative role of reggie-1/flotillin-2 in signaling through the epidermal growth factor receptor. We show that reggie-1 becomes phosphorylated by Src kinase at several tyrosines upon stimulation of cells with epidermal growth factor. In addition, Src and reggie-1 are present as a molecular complex. Epidermal growth factor stimulation of cells results in a Tyr163-dependent translocation of reggie-1 from the plasma membrane into endosomes. We also show that reggie-1 is capable of enhancing the spreading of cells, again in a tyrosine-dependent manner, and knockdown of reggie-1 interferes with spreading. Thus, we reveal a new function for reggie-1 in the regulation of cell adhesion and actin dynamics and in growth factor signaling.

Key words: Reggie, Flotillin, Tyrosine phosphorylation, Rafts, Cell spreading, Endocytosis




This article has been cited by other articles:


Home page
 J. Neurosci.Home page
A. Schneider, L. Rajendran, M. Honsho, M. Gralle, G. Donnert, F. Wouters, S. W. Hell, and M. Simons
Flotillin-Dependent Clustering of the Amyloid Precursor Protein Regulates Its Endocytosis and Amyloidogenic Processing in Neurons
J. Neurosci., March 12, 2008; 28(11): 2874 - 2882.
[Abstract] [Full Text] [PDF]

Home page
 Cancer Res.Home page
I. B. Quintero, C. L. Araujo, A. E. Pulkka, R. S. Wirkkala, A. M. Herrala, E.-L. Eskelinen, E. Jokitalo, P. A. Hellstrom, H. J. Tuominen, P. P. Hirvikoski, et al.
Prostatic Acid Phosphatase Is Not a Prostate Specific Target
Cancer Res., July 15, 2007; 67(14): 6549 - 6554.
[Abstract] [Full Text] [PDF]


© The Company of Biologists Ltd 2007