Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
XB-ART-41531
PLoS One May 17, 2010; 5 (5): e10665.
Show Gene links Show Anatomy links

Integrin alpha5beta1 function is regulated by XGIPC/kermit2 mediated endocytosis during Xenopus laevis gastrulation.

Spicer E , Suckert C , Al-Attar H , Marsden M .


Abstract
During Xenopus gastrulation alpha5beta1 integrin function is modulated in a temporally and spatially restricted manner, however, the regulatory mechanisms behind this regulation remain uncharacterized. Here we report that XGIPC/kermit2 binds to the cytoplasmic domain of the alpha5 subunit and regulates the activity of alpha5beta1 integrin. The interaction of kermit2 with alpha5beta1 is essential for fibronectin (FN) matrix assembly during the early stages of gastrulation. We further demonstrate that kermit2 regulates alpha5beta1 integrin endocytosis downstream of activin signaling. Inhibition of kermit2 function impairs cell migration but not adhesion to FN substrates indicating that integrin recycling is essential for mesoderm cell migration. Furthermore, we find that the alpha5beta1 integrin is colocalized with kermit2 and Rab 21 in embryonic and XTC cells. These data support a model where region specific mesoderm induction acts through kermit2 to regulate the temporally and spatially restricted changes in adhesive properties of the alpha5beta1 integrin through receptor endocytosis.

PubMed ID: 20498857
PMC ID: PMC2871791
Article link: PLoS One


Species referenced: Xenopus laevis
Genes referenced: akt1 bcr dnai1 fn1 gipc1 gipc2 herpud1 itga5 itgb1 pigy rab21 tbxt
Antibodies: Fn1 Ab10 Gipc1 Ab1 HA Ab7 Itgav Ab1 Itgb1 Ab1 Itgb1 Ab3 Rab21 Ab1
Morpholinos: gipc2 MO1


Article Images: [+] show captions
References [+] :
Aota, The short amino acid sequence Pro-His-Ser-Arg-Asn in human fibronectin enhances cell-adhesive function. 1994, Pubmed