Novel interaction partners of the TPR/MET tyrosine kinase

  title={Novel interaction partners of the TPR/MET tyrosine kinase},
  author={Christian Patrick Schaaf and J{\"o}rg Benzing and Thomas L. Schmitt and Dorothee Erz and Magdalena Tewes and Claus Rainer Bartram and Johannes WG Janssen},
  journal={The FASEB Journal},
A large variety of biological processes is mediated by stimulation of the receptor tyrosine kinase MET. Screening a mouse embryo cDNA library, we were able to identify several novel, putative intracellular TPR/MET‐substrates: SNAPIN, DCOHM, VAV‐1, Sorting nexin 2, Death associated protein kinase 3, SMC‐1, Centromeric protein C, and hTID‐1. Interactions as identified by yeast two‐hybrid analysis were validated in vitro and in vivo by mammalian two‐hybrid studies, a far‐western assay and… 

Sorting nexin 2‐mediated membrane trafficking of c‐Met contributes to sensitivity of molecular‐targeted drugs

It is shown that the siRNA‐mediated knockdown of SNX2 decreases the cell‐surface localization of c‐Met, but not that of EGFR, resulting in lysosomal degradation of the c‐ Met protein.

Novel Regulation of Adenylyl Cyclases by Direct Protein-Protein Interactions: Insights from Snapin and Ric8a

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Insights into the PX (phox-homology) domain and SNX (sorting nexin) protein families: structures, functions and roles in disease.

An overview of the PX domain proteins is presented, incorporating recent functional and structural insights, and an updated classification of the proteins into distinct subfamilies is proposed on the basis of these insights.

Retromer and sorting nexins in development.

  • M. Verges
  • Biology
    Frontiers in bioscience : a journal and virtual library
  • 2007
Data from genetically modified mice, and from a simpler organism such as the nematode Caenorhabtidis elegans, has revealed that retromer performs an essential role during embryogenesis, and implications of recent work on this subject will be discussed.

A novel role for snapin in dendrite patterning: interaction with cypin.

Together, the data suggest that snapin regulates dendrite number in developing neurons by modulating cypin-promoted microtubule assembly and that overexpression of snapin in primary cultures of hippocampal neurons results in decreased primary dendrites present on these neurons and increased probability of branching.

Many Faces of Mortalin and Tid1

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The UT-A1 Urea Transporter Interacts with Snapin, a SNARE-associated Protein*

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SNARE complex regulation by phosphorylation

This review focuses on the location and effects of phosphorylation on SNARE regulation, and identifies some of the specific effects that phosphorylated proteins at these sites can produce.

Biochemical and functional characterization of Epstein–Barr virus-encoded BARF1 protein: interaction with human hTid1 protein facilitates its maturation and secretion

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The Jak family of protein-tyrosine kinases are crucial for the signaling of a large number of different polypeptide ligands, including the interferons, many cytokines, erythropoietin, and growth

Ligand-regulated Binding of FAP68 to the Hepatocyte Growth Factor Receptor*

FAP68 represents a novel type of effector that interacts with the inactive HGF receptor and is released upon receptor phosphorylation, which suggests a role for FAP68 in coupling HGF receptors signaling to the p70S6K pathway.

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In vivo data indicate that further direct or indirect binding sites for PLCγ, GRB2, c-src and lck on the human Ufo receptor may exist, and indicates that intracellular signaling may be regulated by a new family of receptor tyrosine kinases.

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Hrs Interacts with Sorting Nexin 1 and Regulates Degradation of Epidermal Growth Factor Receptor*

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Identification of the hepatocyte growth factor receptor as the c-met proto-oncogene product.

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The tyrosine kinase encoded by the MET proto-oncogene is activated by autophosphorylation

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A Mouse Homologue of the Drosophila Tumor Suppressor l(2)tid Gene Defines a Novel Ras GTPase-activating Protein (RasGAP)-binding Protein*

It is demonstrated that both cytoplasmic precursor and mitochondrial mature forms of mTid-1 associate with GAP in vivo, and the possibility that Tid chaperone proteins may play a role in governing the conformation, activity, and/or subcellular distribution of GAP, thereby influencing its biochemical and biological activity within cells is raised.

Mirk Protein Kinase Is Activated by MKK3 and Functions as a Transcriptional Activator of HNF1α*

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