Cbl: many adaptations to regulate protein tyrosine kinases
Top Cited Papers
- 1 April 2001
- journal article
- review article
- Published by Springer Nature in Nature Reviews Molecular Cell Biology
- Vol. 2 (4) , 294-307
- https://doi.org/10.1038/35067100
Abstract
Responses to extracellular stimuli are often transduced from cell-surface receptors to protein tyrosine kinases which, when activated, initiate the formation of protein complexes that transmit signals throughout the cell. A prominent component of these complexes is the product of the proto-oncogene c-Cbl, which specifically targets activated protein tyrosine kinases and regulates their signalling. How, then, does this multidomain protein shape the responses generated by these signalling complexes?Keywords
This publication has 106 references indexed in Scilit:
- Evidence for Direct Interaction between Sprouty and CblPublished by Elsevier ,2001
- A Di-leucine Signal in the Ubiquitin MoietyJournal of Biological Chemistry, 2000
- Polyubiquitination of the Epidermal Growth Factor Receptor Occurs at the Plasma Membrane upon Ligand-induced ActivationPublished by Elsevier ,2000
- Cloning and Characterization of a Novel Adaptor Protein, CIN85, That Interacts with c-CblBiochemical and Biophysical Research Communications, 2000
- Recognition of the polyubiquitin proteolytic signalThe EMBO Journal, 2000
- cbl-b inhibits epidermal growth factor receptor signalingOncogene, 1999
- Cbl-mediated Negative Regulation of the Syk Tyrosine KinaseJournal of Biological Chemistry, 1998
- Tyrosine phosphorylation of p120cbl in BCR/abl transformed hematopoietic cells mediates enhanced association with phosphatidylinositol 3-kinaseOncogene, 1997
- A Novel Phosphotyrosine-binding Domain in the N-terminal Transforming Region of Cbl Interacts Directly and Selectively with ZAP-70 in T CellsPublished by Elsevier ,1996
- SH2 domains recognize specific phosphopeptide sequencesPublished by Elsevier ,1993