Cell Adhesion Regulates Ubiquitin-mediated Degradation of the Platelet-derived Growth Factor Receptor β
Open Access
- 1 December 2000
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 275 (50) , 39318-39323
- https://doi.org/10.1074/jbc.m003618200
Abstract
No abstract availableKeywords
This publication has 35 references indexed in Scilit:
- Ubiquitin Ligase Activity and Tyrosine Phosphorylation Underlie Suppression of Growth Factor Signaling by c-Cbl/Sli-1Molecular Cell, 1999
- The Tyrosine Kinase Negative Regulator c-Cbl as a RING-Type, E2-Dependent Ubiquitin-Protein LigaseScience, 1999
- Ligand-induced Ubiquitination of the Epidermal Growth Factor Receptor Involves the Interaction of the c-Cbl RING Finger and UbcH7Journal of Biological Chemistry, 1999
- Interactions between mitogenic stimuli, or, a thousand and one connectionsCurrent Opinion in Cell Biology, 1999
- Mechanism of Action and In Vivo Role of Platelet-Derived Growth FactorPhysiological Reviews, 1999
- alpha vbeta 3 integrin associates with activated insulin and PDGFbeta receptors and potentiates the biological activity of PDGFThe EMBO Journal, 1997
- Growth factor activation of MAP kinase requires cell adhesionThe EMBO Journal, 1997
- Phosphotyrosine Binding Domain-Dependent Upregulation of the Platelet-Derived Growth Factor Receptor α Signaling Cascade by Transforming Mutants of Cbl: Implications for Cbl’s Function and OncogenicityMolecular and Cellular Biology, 1997
- Integrins can collaborate with growth factors for phosphorylation of receptor tyrosine kinases and MAP kinase activation: roles of integrin aggregation and occupancy of receptors.The Journal of cell biology, 1996
- Mechanism of action of platelet-derived growth factorThe International Journal of Biochemistry & Cell Biology, 1996