Negative regulation of EGFR signalling through integrin-α1β1-mediated activation of protein tyrosine phosphatase TCPTP
✍ Scribed by Mattila, Elina; Pellinen, Teijo; Nevo, Jonna; Vuoriluoto, Karoliina; Arjonen, Antti; Ivaska, Johanna
- Book ID
- 109912383
- Publisher
- Nature Publishing Group
- Year
- 2004
- Tongue
- English
- Weight
- 922 KB
- Volume
- 7
- Category
- Article
- ISSN
- 1465-7392
- DOI
- 10.1038/ncb1209
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
## Abstract Maintenance of β1 integrin‐mediated cell adhesion in quiescent human mammary epithelial (HME) cells requires protein phosphatase (PP) 2A for not only dephosphorylation of β1 integrin but also recruitment of IQGAP1 to Rac‐bound β1 integrin. However, how PP2A‐dependent regulatory machiner
## Abstract The substrate specificity of catalytic domains and the activation of full length protein tyrosine phosphatases, SHP‐1 and SHP‐2 have been investigated using synthetic phosphotyrosyl peptides derived from SIPRα1. We found that the catalytic domains of SHP‐1 and SHP‐2 exhibit different su
CD5, a membrane-associated glycoprotein, has been shown to negatively regulate antigen receptor-mediated growth responses in peritoneal B lymphocytes, thymocytes and mature T cells. The CD5-expressing peritoneal B cells (B-1) that are normally unresponsive to B cell receptor (BCR)-mediated growth si