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Full-Text Articles in Life Sciences

Drosophila Unpaired Encodes A Secreted Protein That Activates The Jak Signaling Pathway, Douglas A. Harrison, Patricia E. Mccoon, Richard Binari, Michael Gilman, Norbert Perrimon Oct 1998

Drosophila Unpaired Encodes A Secreted Protein That Activates The Jak Signaling Pathway, Douglas A. Harrison, Patricia E. Mccoon, Richard Binari, Michael Gilman, Norbert Perrimon

Biology Faculty Publications

In vertebrates, many cytokines and growth factors have been identified as activators of the JAK/STAT signaling pathway. In Drosophila, JAK and STAT molecules have been isolated, but no ligands or receptors capable of activating the pathway have been described. We have characterized the unpaired (upd) gene, which displays the same distinctive embryonic mutant defects as mutations in the Drosophila JAK (hopscotch) and STAT (stat92E) genes. Upd is a secreted protein, associated with the extracellular matrix, that activates the JAK pathway. We propose that Upd is a ligand that relies on JAK signaling to stimulate transcription of pair-rule genes in a …


Identification Of Putative Cytoskeletal Protein Homologues In The Protozoan Host Hartmannella Vermiformis As Substrates For Induced Tyrosine Phosphatase Activity Upon Attachment To The Legionnaires' Disease Bacterium, Legionella Pneumophila, Chandrasekar Venkataraman, Lian-Yang Gao, Subbarao Bondada, Yousef Abu Kwaik Aug 1998

Identification Of Putative Cytoskeletal Protein Homologues In The Protozoan Host Hartmannella Vermiformis As Substrates For Induced Tyrosine Phosphatase Activity Upon Attachment To The Legionnaires' Disease Bacterium, Legionella Pneumophila, Chandrasekar Venkataraman, Lian-Yang Gao, Subbarao Bondada, Yousef Abu Kwaik

Microbiology, Immunology, and Molecular Genetics Faculty Publications

The Legionnaires' disease bacterium, Legionella pneumophila, is a facultative intracellular pathogen that invades and replicates within two evolutionarily distant hosts, free living protozoa and mammalian cells. Invasion and intracellular replication within protozoa are thought to be major factors in the transmission of Legionnaires' disease. We have recently reported the identification of a galactose/N-acetyl-d-galactosamine (Gal/GalNAc) lectin in the protozoan host Hartmannella vermiformis as a receptor for attachment and invasion by L. pneumophila (Venkataraman, C., B.J. Haack, S. Bondada, and Y.A. Kwaik. 1997. J. Exp. Med. 186:537–547). In this report, we extended our studies to the …


The Snare Machinery Is Involved In Apical Plasma Membrane Trafficking In Mdck Cells, Seng Hui Low, Steven J. Chapin, Christian Wimmer, Sidney W. Whiteheart, László G. Kömüves, Keith E. Mostov, Thomas Weimbs Jun 1998

The Snare Machinery Is Involved In Apical Plasma Membrane Trafficking In Mdck Cells, Seng Hui Low, Steven J. Chapin, Christian Wimmer, Sidney W. Whiteheart, László G. Kömüves, Keith E. Mostov, Thomas Weimbs

Molecular and Cellular Biochemistry Faculty Publications

We have investigated the controversial involvement of components of the SNARE (soluble N-ethyl maleimide–sensitive factor [NSF] attachment protein [SNAP] receptor) machinery in membrane traffic to the apical plasma membrane of polarized epithelial (MDCK) cells. Overexpression of syntaxin 3, but not of syntaxins 2 or 4, caused an inhibition of TGN to apical transport and apical recycling, and leads to an accumulation of small vesicles underneath the apical plasma membrane. All other tested transport steps were unaffected by syntaxin 3 overexpression. Botulinum neurotoxin E, which cleaves SNAP-23, and antibodies against α-SNAP inhibit both TGN to apical and basolateral transport in …