Abstract:
:Integrin and receptor tyrosine kinase signalling networks cooperate to regulate various biological functions. The molecular details underlying the integration of both signalling networks remain largely uncharacterized. Here we identify a signalling module composed of a fibronectin-α5β1-integrin-integrin-linked-kinase (ILK) complex that, in concert with epidermal growth factor (EGF) cues, cooperatively controls the formation of transient actin-based circular dorsal ruffles (DRs) in fibroblasts. DR formation depends on the precise spatial activation of Src at focal adhesions by integrin and EGF receptor signals, in an ILK-dependent manner. In a SILAC-based phosphoproteomics screen we identified the tumour-suppressor Cyld as being required for DR formation induced by α5β1 integrin and EGF receptor co-signalling. Furthermore, EGF-induced Cyld tyrosine phosphorylation is controlled by integrin-ILK and Src as a prerequisite for DR formation. This study provides evidence for a novel function of integrin-ILK and EGF signalling crosstalk in mediating Cyld tyrosine phosphorylation and fast actin-based cytoskeletal rearrangements.
journal_name
J Cell Scijournal_title
Journal of cell scienceauthors
Azimifar SB,Böttcher RT,Zanivan S,Grashoff C,Krüger M,Legate KR,Mann M,Fässler Rdoi
10.1242/jcs.091652subject
Has Abstractpub_date
2012-01-15 00:00:00pages
435-48issue
Pt 2eissn
0021-9533issn
1477-9137pii
jcs.091652journal_volume
125pub_type
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