Journal article

Structural requirements for PACSIN/Syndapin operation during zebrafish embryonic notochord development.

Melissa A Edeling, Subramaniam Sanker, Takaki Shima, PK Umasankar, Stefan Höning, Hye Y Kim, Lance A Davidson, Simon C Watkins, Michael Tsang, David J Owen, Linton M Traub

PLoS One | Public Library of Science (PLoS) | 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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University of Melbourne Researchers