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PRL-3 and PRL-1 promote cell migration, invasion, and metastasis.
TLDR
It is demonstrated that Chinese hamster ovary cells stably expressing PRL-3, a M(r) 20000 prenylated protein tyrosine phosphatase, or its relative,PRL-1, exhibit enhanced motility and invasive activity, and it is shown that PRl-3 is associated with diverse membrane structures involved in cell movement. Expand
Akt phosphorylates the Y-box binding protein 1 at Ser102 located in the cold shock domain and affects the anchorage-independent growth of breast cancer cells
TLDR
It is determined that activated Akt is positively correlated with the protein expression of the transcription/translation factor Y-box binding protein-1 (YB-1) in primary breast cancer by screening tumor tissue microarrays and disruption of this specific site inhibits tumor cell growth. Expand
F3/Contactin Acts as a Functional Ligand for Notch during Oligodendrocyte Maturation
TLDR
F3/contactin specifically initiates a Notch/Deltex1 signaling pathway that promotes oligodendrocyte maturation and myelination that upregulates the myelin-related protein MAG in OLN-93 cells. Expand
PRL PTPs: mediators and markers of cancer progression
TLDR
The identification of PRL substrates is key to understanding their roles in cancer progression and exploiting their potential as exciting new therapeutic targets for cancer treatment. Expand
Prenylation-dependent Association of Protein-tyrosine Phosphatases PRL-1, -2, and -3 with the Plasma Membrane and the Early Endosome*
TLDR
The results establish that the primary association of PRL-1, -2, and -3 with the membrane of the cell surface and the early endosome is dependent on their prenylation and that nuclear localization of these proteins may be triggered by a regulatory event that inhibits their preNylation. Expand
Targeted disruption of the tyrosine phosphatase PTPα leads to constitutive downregulation of the kinases Src and Fyn
TLDR
Results indicate that PTPalpha has a dual function as a positive and negative regulator of tyrosine phosphorylation events, increasing phosphotyrosyl proteins through activation of Src and Fyn, and directly or indirectly removing tyrosin phosphate from other unidentified proteins. Expand
PTPα regulates integrin-stimulated FAK autophosphorylation and cytoskeletal rearrangement in cell spreading and migration
TLDR
It is established that PTPα is required for early integrin-proximal events, acting upstream ofFAK to affect the timely and efficient phosphorylation of FAK Tyr-397. Expand
Neural recognition molecules CHL1 and NB‐3 regulate apical dendrite orientation in the neocortex via PTPα
TLDR
It is shown thatCHL1 directly associates with NB‐3, a member of the F3/contactin family of neural recognition molecules, and enhances its cell surface expression, and proposes a signaling complex in which PTPα mediates CHL1 andNB‐3‐regulated apical dendrite projection in the developing caudal cortex. Expand
Ewing sarcoma with novel translocation t(2;16) producing an in-frame fusion of FUS and FEV.
TLDR
This represents the first reported case of Ewing family tumors demonstrating a variant translocation involving FUS and FEV and highlights the need to consider alternative permutations of fusion partners for molecular diagnosis of sarcomas. Expand
Protein Tyrosine Phosphatase α (Ptpα) and Contactin Form a Novel Neuronal Receptor Complex Linked to the Intracellular Tyrosine Kinase Fyn
TLDR
It is demonstrated that PTPα, an RPTP that dephosphorylates and activates src family kinases, forms a novel membrane-spanning complex with the neuronal GPI-anchored receptor contactin, and postulate that the role of contactin is to assemble a phosphorylation-competent system at the cell surface, conferring a dynamic signal transduction capability to the recognition element. Expand
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