The association of Sam68 with Vav1 contributes to tumorigenesis (Q24293551)

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Liron Pe'er

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Vered Schapira

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Stéphane Richard

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Shulamit Katzav

The haematopoietic specific signal transducer Vav1 is expressed in a subset of human neuroblastomas

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language of work or name

English

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publication date

December 2007

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published in

Cellular Signalling

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volume

19

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issue

12

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page(s)

2479-86

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cites work

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Ectopic expression of VAV1 reveals an unexpected role in pancreatic cancer tumorigenesis

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Vav-family proteins in T-cell signalling

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The Actin Cytoskeleton and Lymphocyte Activation

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Sam68 is a docking protein linking GAP and PI3K in insulin receptor signaling

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Vav proteins, masters of the world of cytoskeleton organization.

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Proximal protein tyrosine kinases in immunoreceptor signaling

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Vav and SLP-76 interact and functionally cooperate in IL-2 gene activation

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BLNK: a central linker protein in B cell activation

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The membrane-microfilament linker ezrin is involved in the formation of the immunological synapse and in T cell activation

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Activation of Vav by Nef induces cytoskeletal rearrangements and downstream effector functions

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Analytical properties of the nanoelectrospray ion source

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An RNA-binding protein associated with Src through its SH2 and SH3 domains in mitosis

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Phosphotyrosine-dependent activation of Rac-1 GDP/GTP exchange by the vav proto-oncogene product

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Dynamin 2 regulates T cell activation by controlling actin polymerization at the immunological synapse

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VAV proteins as signal integrators for multi-subunit immune-recognition receptors

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Mutagenic analysis of Vav reveals that an intact SH3 domain is required for transformation

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p95(vav) associates with the type I interferon (IFN) receptor and contributes to the antiproliferative effect of IFN-alpha in megakaryocytic cell lines

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Characterization of VIK-1: a new Vav-interacting Kruppel-like protein

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The RNA-binding protein Sam68 contributes to proliferation and survival of human prostate cancer cells

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Binding of Vav to Grb2 through dimerization of Src homology 3 domains

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Functional interaction between c-Src and its mitotic target, Sam 68

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Vav is necessary for prolactin-stimulated proliferation and is translocated into the nucleus of a T-cell line

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P62 association with RNA is regulated by tyrosine phosphorylation.

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Specificity and determinants of Sam68 RNA binding. Implications for the biological function of K homology domains

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Vav binding to heterogeneous nuclear ribonucleoprotein (hnRNP) C. Evidence for Vav-hnRNP interactions in an RNA-dependent manner.

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Neoplastic transformation and tumorigenesis associated with sam68 protein deficiency in cultured murine fibroblasts

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Vav1 and Ly-GDI two regulators of Rho GTPases, function cooperatively as signal transducers in T cell antigen receptor-induced pathways

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p95vav associates with the nuclear protein Ku-70

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Sik (BRK) phosphorylates Sam68 in the nucleus and negatively regulates its RNA binding ability

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Regulatory and signaling properties of the Vav family

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Vav-Rac1-mediated activation of the c-Jun N-terminal kinase/c-Jun/AP-1 pathway plays a major role in stimulation of the distal NFAT site in the interleukin-2 gene promoter

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Activation of Vav/Rho GTPase signaling by CXCL12 controls membrane-type matrix metalloproteinase-dependent melanoma cell invasion

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Vav1: an oncogene that regulates specific transcriptional activation of T cells

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Depolarization-induced translocation of the RNA-binding protein Sam68 to the dendrites of hippocampal neurons.

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Ablation of the Sam68 RNA binding protein protects mice from age-related bone loss

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Specific subdomains of Vav differentially affect T cell and NK cell activation

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