Document Detail


The cytoplasmic tyrosine kinase Arg regulates gastrulation via control of actin organization.
MedLine Citation:
PMID:  22305799     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Coordinated cell movements are crucial for vertebrate gastrulation and are controlled by multiple signals. Although many factors are shown to mediate non-canonical Wnt pathways to regulate cell polarity and intercalation during gastrulation, signaling molecules acting in other pathways are less investigated and the connections between various signals and cytoskeleton are not well understood. In this study, we show that the cytoplasmic tyrosine kinase Arg modulates gastrulation movements through control of actin remodeling. Arg is expressed in the dorsal mesoderm at the onset of gastrulation, and both gain- and loss-of-function of Arg disrupted axial development in Xenopus embryos. Arg controlled migration of anterior mesendoderm, influenced cell decision on individual versus collective migration, and modulated spreading and protrusive activities of anterior mesendodermal cells. Arg also regulated convergent extension of the trunk mesoderm by influencing cell intercalation behaviors. Arg modulated actin organization to control dynamic F-actin distribution at the cell-cell contact or in membrane protrusions. The functions of Arg required an intact tyrosine kinase domain but not the actin-binding motifs in its carboxyl terminus. Arg acted downstream of receptor tyrosine kinases to regulate phosphorylation of endogenous CrkII and paxillin, adaptor proteins involved in activation of Rho family GTPases and actin reorganization. Our data demonstrate that Arg is a crucial cytoplasmic signaling molecule that controls dynamic actin remodeling and mesodermal cell behaviors during Xenopus gastrulation.
Authors:
Gustavo Bonacci; Jason Fletcher; Madhav Devani; Harsh Dwivedi; Ray Keller; Chenbei Chang
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural     Date:  2012-01-18
Journal Detail:
Title:  Developmental biology     Volume:  364     ISSN:  1095-564X     ISO Abbreviation:  Dev. Biol.     Publication Date:  2012 Apr 
Date Detail:
Created Date:  2012-03-05     Completed Date:  2012-04-12     Revised Date:  2014-09-17    
Medline Journal Info:
Nlm Unique ID:  0372762     Medline TA:  Dev Biol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  42-55     Citation Subset:  IM    
Copyright Information:
© 2012 Elsevier Inc. All rights reserved.
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MeSH Terms
Descriptor/Qualifier:
Actins / metabolism*
Animals
Arginine / genetics,  metabolism
Cadherins / metabolism
Cell Adhesion
Cell Lineage
Cell Movement
Cytoplasm / enzymology*
Embryo, Nonmammalian / cytology,  enzymology*
Gastrulation*
Humans
Phosphorylation
Protein Binding
Protein-Tyrosine Kinases / genetics,  metabolism*
Xenopus laevis / embryology*,  genetics,  metabolism*
Grant Support
ID/Acronym/Agency:
R01 GM083029/GM/NIGMS NIH HHS; R01 GM083029-01A2/GM/NIGMS NIH HHS; R01 GM083029-02/GM/NIGMS NIH HHS; R01-GM083029/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Actins; 0/Cadherins; 94ZLA3W45F/Arginine; EC 2.7.10.1/Protein-Tyrosine Kinases
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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