Journal article
Structural requirements for PACSIN/syndapin operation during zebrafish embryonic notochord development
MA Edeling, S Sanker, T Shima, PK Umasankar, S Höning, HY Kim, LA Davidson, SC Watkins, M Tsang, DJ Owen, LM Traub
Plos One | PUBLIC LIBRARY SCIENCE | Published : 2009
Abstract
PACSIN/Syndapin proteins are membrane-active scaffolds that participate in endocytosis. The structure of the Drosophila Syndapin N-terminal EFC domain reveals a crescent shaped antiparallel dimer with a high affinity for phosphoinositides and a unique membrane-inserting prong upon the concave surface. Combined structural, biochemical and reverse genetic approaches in zebrafish define an important role for Syndapin orthologue, Pacsin3, in the early formation of the notochord during embryonic development. In pacsin3-morphant embryos, midline convergence of notochord precursors is defective as axial mesodermal cells fail to polarize, migrate and differentiate properly. The pacsin3 morphant phen..
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Awarded by Eunice Kennedy Shriver National Institute of Child Health and Human Development
Funding Acknowledgements
This study was supported by NIH grants R01 DK53249 and pilot project on P30 DK79307 to LMT, R01 HD044750 to LAD and R01 HL088016 to MT, a Wellcome Trust Senior Fellowship to DJO, and German Science Foundation grants (SFB 635 and SFB670) to SH. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.