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Pinpointing phosphotyrosine‐dependent interactions downstream of the collagen receptor DDR1
Author(s) -
Koo Diana H.H.,
McFadden Catherine,
Huang Yun,
Abdulhussein Rahim,
Friese-Hamim Manja,
Vogel Wolfgang F.
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.11.035
Subject(s) - ddr1 , discoidin domain , tyrosine , sh2 domain , phosphopeptide , phosphorylation , chemistry , tyrosine phosphorylation , receptor tyrosine kinase , microbiology and biotechnology , biology , biochemistry
Using phosphopeptide mapping and site‐directed mutagenesis, we here identified multiple tyrosine phosphorylation sites within DDR1. We found that Nck2 and Shp‐2, two SH2 domain‐containing proteins, bind to DDR1 in a collagen‐dependent manner. The binding site of Shp‐2 was mapped to tyrosine‐740 of DDR1 within an ITIM‐consensus sequence. Lastly, ablation of DDR1 in the mouse mammary gland resulted in delocalized expression of Nck2, suggesting that defects observed during alveologenesis are caused by the lack of the DDR1–Nck2 interaction.