QUICK SEARCH:   [advanced] Author: Keyword(s):
Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents

First published online 20 January 2004
doi: 10.1242/jcs.00922

This Article Figures Only Full Text Full Text (PDF) All Versions of this Article: jcs.00922v1 117/5/771    most recent Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Williams, J. A. Articles by Thomas, G. H. Search for Related Content PubMed PubMed Citation Articles by Williams, J. A. Articles by Thomas, G. H.

The C-terminal domain of Drosophila ßHeavy-spectrin exhibits autonomous membrane association and modulates membrane area

Department of Biology, Department of Biochemistry and Molecular Biology, Eberly College of Science, The Pennsylvania State University, University Park, PA 16802, USA

^* Author for correspondence (e-mail: gxt5{at}psu.edu)

Accepted 3 October 2003

Current models of cell polarity invoke asymmetric cues that reorganize the secretory apparatus to induce polarized protein delivery. An important step in this process is the stabilization of the protein composition in each polarized membrane domain. The spectrin-based membrane skeleton is thought to contribute to such stabilization by increasing the half-life of many proteins at the cell surface. Genetic evidence is consistent with a negative role for Drosophila ß_Heavy-spectrin in endocytosis, but the inhibitory mechanism has not been elucidated. Here, we investigated the membrane binding properties of the C-terminal nonrepetitive domain of ß_Heavy-spectrin through its in vivo expression in transgenic flies. We found that this region is a membrane-association domain that requires a pleckstrin homology domain for full activity, and we showed for the first time that robust membrane binding by such a C-terminal domain requires additional contributions outside the pleckstrin homology. In addition, we showed that expression of the ß_Heavy-spectrin C-terminal domain has a potent effect on epithelial morphogenesis. This effect is associated with its ability to induce an expansion in plasma membrane surface area. The membrane expansions adopt a very specific bi-membrane structure that sequesters both the C-terminal domain and the endocytic protein dynamin. Our data provide supporting evidence for the inhibition of endocytosis by ß_Heavy-spectrin, and suggest that the C-terminal domain mediates this effect through interaction with the endocytic machinery. Spectrin may be an active partner in the stabilization of polarized membrane domains.

Key words: Spectrin, Endocytosis, Dynamin, Epithelium, Cell polarity, Drosophila

This article has been cited by other articles:

				K. Legendre, S. Safieddine, P. Kussel-Andermann, C. Petit, and A. El-Amraoui {alpha}II-{beta}V spectrin bridges the plasma membrane and cortical lattice in the lateral wall of the auditory outer hair cells J. Cell Sci., October 15, 2008; 121(20): 3347 - 3356. [Abstract] [Full Text] [PDF]

				A. Das, C. Base, D. Manna, W. Cho, and R. R. Dubreuil Unexpected Complexity in the Mechanisms That Target Assembly of the Spectrin Cytoskeleton J. Biol. Chem., May 2, 2008; 283(18): 12643 - 12653. [Abstract] [Full Text] [PDF]

				J. Hulsmeier, J. Pielage, C. Rickert, G. M. Technau, C. Klambt, and T. Stork Distinct functions of {alpha}-Spectrin and {beta}-Spectrin during axonal pathfinding Development, February 15, 2007; 134(4): 713 - 722. [Abstract] [Full Text] [PDF]

				M. D. Phillips and G. H. Thomas Brush border spectrin is required for early endosome recycling in Drosophila J. Cell Sci., April 1, 2006; 119(7): 1361 - 1370. [Abstract] [Full Text] [PDF]

				K. Bialkowska, T. C. Saido, and J. E. B. Fox SH3 domain of spectrin participates in the activation of Rac in specialized calpain-induced integrin signaling complexes J. Cell Sci., January 15, 2005; 118(2): 381 - 395. [Abstract] [Full Text] [PDF]