QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

Vol. 20, Issue 8, 2254-2264, April 15, 2009

This Article Full Text Full Text (PDF) Supplemental Materials All Versions of this Article: E08-10-1072v1 20/8/2254    most recent Alert me when this article is cited Alert me if a correction is posted Services 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 Kumar, V. Articles by Ramaswami, M. Search for Related Content PubMed PubMed Citation Articles by Kumar, V. Articles by Ramaswami, M.

Syndapin Promotes Formation of a Postsynaptic Membrane System in Drosophila

Vimlesh Kumar^*, Robert Fricke, Debjani Bhar, Suneel Reddy-Alla, K. S. Krishnan^,, Sven Bogdan, and Mani Ramaswami^*,,||

*Smurfit Institute of Genetics and Trinity College Institute of Neuroscience, University of Dublin Trinity College, Dublin-2, Ireland Institut für Neurobiologie, Universität Münster, D-48149 Münster, Germany Department of Biological Science, Tata Institute of Fundamental Research, Colaba, Mumbai 400005, India National Centre for Biological Sciences, Bangalore 560085, India ^||Department of Molecular and Cellular Biology, University of Arizona, Tucson, AZ 85721

Submitted October 28, 2008; Revised January 30, 2009; Accepted February 18, 2009
Monitoring Editor: Marcos Gonzalez-Gaitan

Syndapins belong to the F-BAR domain protein family whose predicted functions in membrane tubulation remain poorly studied in vivo. At Drosophila neuromuscular junctions, syndapin is associated predominantly with a tubulolamellar postsynaptic membrane system known as the subsynaptic reticulum (SSR). We show that syndapin overexpression greatly expands this postsynaptic membrane system. Syndapin can expand the SSR in the absence of dPAK and Dlg, two known regulators of SSR development. Syndapin's N-terminal F-BAR domain, required for membrane tubulation in cultured cells, is required for SSR expansion. Consistent with a model in which syndapin acts directly on postsynaptic membrane, SSR expansion requires conserved residues essential for membrane binding in vitro. However, syndapin's Src homology (SH) 3 domain, which negatively regulates membrane tubulation in cultured cells, is required for synaptic targeting and strong SSR induction. Our observations advance knowledge of syndapin protein function by 1) demonstrating the in vivo relevance of membrane remodeling mechanisms suggested by previous in vitro and structural analyses, 2) showing that SH3 domains are necessary for membrane expansion observed in vivo, and 3) confirming that F-BAR proteins control complex membrane structures.

Address correspondence to: Vimlesh Kumar (kumarv{at}tcd.ie) or Mani Ramaswami (mani{at}u.arizona.edu)

This article has been cited by other articles:

				Q. Wang, M. V. A. S. Navarro, G. Peng, E. Molinelli, S. Lin Goh, B. L. Judson, K. R. Rajashankar, and H. Sondermann Molecular mechanism of membrane constriction and tubulation mediated by the F-BAR protein Pacsin/Syndapin PNAS, August 4, 2009; 106(31): 12700 - 12705. [Abstract] [Full Text] [PDF]