AI Article Synopsis
- The study investigates the role of XGIPC/kermit2 in regulating alpha5beta1 integrin during Xenopus gastrulation, highlighting its binding to the alpha5 subunit.
- Kermit2 is crucial for fibronectin matrix assembly at early gastrulation stages and modulates integrin endocytosis in response to activin signaling.
- Disrupting kermit2 function affects mesoderm cell migration without impacting adhesion, indicating that the recycling of alpha5beta1 integrin is vital for cell movement.
Article 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.
Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2871791 | PMC |
| http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0010665 | PLOS |
Publication Analysis
Top Keywords
Similar Publications
Want AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!