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Structural requirements for PACSIN/syndapin operation during zebrafish embryonic notochord development

Edeling, MA and Sanker, S and Shima, T and Umasankar, PK and Höning, S and Kim, HY and Davidson, LA and Watkins, SC and Tsang, M and Owen, DJ and Traub, LM (2009) Structural requirements for PACSIN/syndapin operation during zebrafish embryonic notochord development. PLoS ONE, 4 (12).

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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 phenotype of a stunted body axis and contorted trunk is rescued by ectopic expression of Drosophila Syndapin, and depends critically on both the prong that protrudes from the surface of the bowed Syndapin EFC domain and the ability of the antiparallel dimer to bind tightly to phosphoinositides. Our data confirm linkage between directional migration, endocytosis and cell specification during embryonic morphogenesis and highlight a key role for Pacsin3 in this coupling in the notochord. © 2009 Edeling et al.


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Item Type: Article
Status: Published
CreatorsEmailPitt UsernameORCID
Edeling, MA
Sanker, Ssus48@pitt.eduSUS48
Shima, T
Umasankar, PK
Höning, S
Kim, HY
Davidson, LAlad43@pitt.eduLAD430000-0002-2956-0437
Watkins, SCsimon.watkins@pitt.eduSWATKINS
Tsang, Mtsang@pitt.eduTSANG
Owen, DJ
Traub, LMtraub@pitt.eduTRAUB
ContributionContributors NameEmailPitt UsernameORCID
Date: 1 December 2009
Date Type: Publication
Journal or Publication Title: PLoS ONE
Volume: 4
Number: 12
DOI or Unique Handle: 10.1371/journal.pone.0008150
Schools and Programs: School of Medicine > Cell Biology and Molecular Physiology
Swanson School of Engineering > Bioengineering
Refereed: Yes
MeSH Headings: Amino Acid Sequence; Animals; Carrier Proteins--chemistry; Carrier Proteins--metabolism; Cell Movement--drug effects; Embryo, Nonmammalian--abnormalities; Embryo, Nonmammalian--pathology; Embryo, Nonmammalian--ultrastructure; Embryonic Development--drug effects; HeLa Cells; Humans; Liposomes--metabolism; Molecular Sequence Data; Notochord--abnormalities; Notochord--drug effects; Notochord--embryology; Notochord--pathology; Oligonucleotides, Antisense--pharmacology; Phenotype; Protein Binding--drug effects; Protein Structure, Tertiary; Structure-Activity Relationship; Zebrafish--embryology; Zebrafish Proteins--chemistry; Zebrafish Proteins--metabolism
Other ID: NLM PMC2780292
PubMed Central ID: PMC2780292
PubMed ID: 19997509
Date Deposited: 03 Aug 2012 18:34
Last Modified: 27 Jan 2019 02:55


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