Membrane-anchored Cbl suppresses Hck protein-tyrosine kinase mediated cellular transformation

  title={Membrane-anchored Cbl suppresses Hck protein-tyrosine kinase mediated cellular transformation},
  author={Christopher J. Howlett and Stephen M. Robbins},
The mammalian proto-oncogene Cbl and its cellular homologues in Caenorhabditis elegans (Sli-1) and Drosophila (D-Cbl) are negative regulators of some growth factor receptor signaling pathways. Herein we show that Cbl can negatively regulate another signaling molecule, namely theSrc-family kinase Hck by targeting it for degradation. Hck-mediated cellular transformation of murine fibroblasts is reverted by ectopic expression of a membrane-anchored allele of Cbl as assessed by the cellular… 

Cbl-c suppresses v-Src-induced transformation through ubiquitin-dependent protein degradation

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This review will endeavor to provide a summary of current studies focused on the effects of Cbl proteins on various biological processes and the mechanism of these effects.

c-Cbl-facilitated cytoskeletal effects in v-Abl-transformed fibroblasts are regulated by membrane association of c-Cbl

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Role of the Adapter Protein 3BP2 in BCR-ABL-mediated Signal Transduction and Leukemogenesis

3BP2 is able to modulate signalling through BCR-ABL and affect BCR -ABL-induced disease outcome and a phospho-SRC family protein and a 116 kDaospho-protein were identified as 3BP2 interaction partners in response to B CR-ABl activation.

Cbl signaling networks in the regulation of cell function

It is becoming obvious that temporal and spatial changes in Cbl signaling networks are essential for the control of physiological processes in a variety of cells and organs and that their deregulation can result in the development of human diseases.

Myristoylation and Membrane Binding Regulate c-Src Stability and Kinase Activity

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The ESCRT machinery mediates polarization of fibroblasts through regulation of myosin light chain

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Tyrosine Residues Direct the Ubiquitination and Degradation of the NY-1 Hantavirus G1 Cytoplasmic Tail

It is demonstrated that specific conserved tyrosines within the G1 cytoplasmic tail direct the polyubiquitination and degradation of expressed G1 proteins and provide a potential means for down-regulating hantavirus G1 surface glycoproteins and cellular proteins that interact with G1.

Breakdown of endocytosis in the oncogenic activation of receptor tyrosine kinases.

This review will focus on recent advances linking defective endocytosis of RTKs in the development of cancer.



The Proto-oncogene p120CblIs a Downstream Substrate of the Hck Protein-Tyrosine Kinase

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Cbl: complex formation and functional implications.

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Tissue Hyperplasia and Enhanced T-Cell Signalling via ZAP-70 in c-Cbl-Deficient Mice

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The tyrosine kinase regulator Cbl enhances the ubiquitination and degradation of the platelet-derived growth factor receptor alpha.

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c-Cbl/Sli-1 regulates endocytic sorting and ubiquitination of the epidermal growth factor receptor.

An endosomal sorting machinery capable of controlling the fate, and, hence, signaling potency, of growth factor receptors is revealed.

Regulation of the Src family tyrosine kinase Blk through E6AP-mediated ubiquitination.

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Tyrosine phosphorylation of C-Cbl facilitates adhesion and spreading while suppressing anchorage-independent growth of V-Abl-transformed NIH3T3 fibroblasts

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