Please use this identifier to cite or link to this item: https://doi.org/10.1371/journal.pone.0010125
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dc.titleA vertebrate-specific Chp-PAK-PIX pathway maintains E-cadherin at adherens junctions during zebrafish epiboly
dc.contributor.authorTay H.G.
dc.contributor.authorNg Y.W.
dc.contributor.authorManser E.
dc.date.accessioned2019-11-07T08:02:01Z
dc.date.available2019-11-07T08:02:01Z
dc.date.issued2010
dc.identifier.citationTay H.G., Ng Y.W., Manser E. (2010). A vertebrate-specific Chp-PAK-PIX pathway maintains E-cadherin at adherens junctions during zebrafish epiboly. PLoS ONE 5 (4) : e10125. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.pone.0010125
dc.identifier.issn19326203
dc.identifier.urihttps://scholarbank.nus.edu.sg/handle/10635/161811
dc.description.abstractBackground: In early vertebrate development, embryonic tissues modulate cell adhesiveness and acto-myosin contractility to correctly orchestrate the complex processes of gastrulation. E-cadherin (E-cadh) is the earliest expressed cadherin and is needed in the mesendodermal progenitors for efficient migration [1,2]. Regulatory mechanisms involving directed E-cadh trafficking have been invoked downstream of Wnt11/5 signaling [3]. This non-canonical Wnt pathway regulates RhoA-ROK/ DAAM1 to control the acto-myosin network. However, in this context nothing is known of the intracellular signals that participate in the correct localization of E-cadh, other than a need for Rab5c signaling [3]. Methodology/Principal Findings: By studying loss of Chp induced by morpholino-oligonucleotide injection in zebrafish, we find that the vertebrate atypical Rho-GTPase Chp is essential for the proper disposition of cells in the early embryo. The underlying defect is not leading edge F-actin assembly (prominent in the cells of the envelope layer), but rather the failure to localize E-cadh and ?-catenin at the adherens junctions. Loss of Chp results in delayed epiboly that can be rescued by mRNA co-injection, and phenocopies zebrafish E-cadh mutants [4,5]. This new signaling pathway involves activation of an effector kinase PAK, and involvement of the adaptor PAK-interacting exchange factor PIX. Loss of signaling by any of the three components results in similar underlying defects, which is most prominent in the epithelial-like envelope layer. Conclusions/Significance: Our current study uncovers a developmental pathway involving Chp/PAK/PIX signaling, which helps co-ordinate E-cadh disposition to promote proper cell adhesiveness, and coordinate movements of the three major cell layers in epiboly. Our data shows that without Chp signaling, E-cadh shifts to intracellular vesicles rather than the adhesive contacts needed for directed cell movement. These events may mirror the requirement for PAK2 signaling essential for the proper formation of the blood-brain barrier [6,7].© 2010 Tay et al.
dc.rightsAttribution 4.0 International
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/
dc.sourceUnpaywall 20191101
dc.subjectadaptor PAK interacting exchange factor
dc.subjectadaptor protein
dc.subjectbeta catenin
dc.subjectF actin
dc.subjectmessenger RNA
dc.subjectoligonucleotide
dc.subjectp21 activated kinase
dc.subjectphosphotransferase
dc.subjectprotein
dc.subjectRho guanine nucleotide binding protein
dc.subjectunclassified drug
dc.subjectuvomorulin
dc.subjectcadherin
dc.subjectguanine nucleotide exchange factor
dc.subjectrho guanine nucleotide exchange factors
dc.subjectanimal tissue
dc.subjectarticle
dc.subjectblood brain barrier
dc.subjectcell adhesion
dc.subjectcell junction
dc.subjectcell motion
dc.subjectcell vacuole
dc.subjectcontrolled study
dc.subjectembryo
dc.subjectenzyme activation
dc.subjectgastrulation
dc.subjectmutant
dc.subjectnonhuman
dc.subjectnucleotide sequence
dc.subjectprotein assembly
dc.subjectprotein depletion
dc.subjectprotein localization
dc.subjectsignal transduction
dc.subjectvertebrate
dc.subjectzebra fish
dc.subjectanimal
dc.subjectanimal embryo
dc.subjectmetabolism
dc.subjectphysiology
dc.subjectsignal transduction
dc.subjectDanio rerio
dc.subjectVertebrata
dc.subjectAdherens Junctions
dc.subjectAnimals
dc.subjectCadherins
dc.subjectCell Adhesion
dc.subjectCell Movement
dc.subjectEmbryo, Nonmammalian
dc.subjectGuanine Nucleotide Exchange Factors
dc.subjectp21-Activated Kinases
dc.subjectrho GTP-Binding Proteins
dc.subjectSignal Transduction
dc.subjectVertebrates
dc.subjectZebrafish
dc.typeArticle
dc.contributor.departmentDUKE-NUS MEDICAL SCHOOL
dc.contributor.departmentDEPT OF PHARMACOLOGY
dc.description.doi10.1371/journal.pone.0010125
dc.description.sourcetitlePLoS ONE
dc.description.volume5
dc.description.issue4
dc.description.pagee10125
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