@article {827,
	title = {Thrombin receptor signaling to cytoskeleton requires Hsp90.},
	journal = {J Biol Chem},
	volume = {276},
	year = {2001},
	month = {2001 Aug 31},
	pages = {32642-7},
	abstract = {<p>Thrombin is a serine protease that evokes various cellular responses involved in injury and repair of the nervous system through the activation of protease-activated receptor-1 (PAR-1). Signals that modulate cell morphology precede most PAR-1 effects, but the initial signal transduction molecules are not known. Using the yeast two-hybrid system, we identified Hsp90, a chaperone with known signaling properties, as a binding partner of PAR-1. The interaction was confirmed by glutathione S-transferase pull-down, overlay, and co-immunoprecipitation assays. Morphological assays in mouse astrocytes were carried out to evaluate the importance of Hsp90 during cytoskeletal signaling. Reducing Hsp90 levels by antisense treatment or disruption of the Hsp90.PAR-1 complex by the Hsp90-specific drug geldanamycin attenuated thrombin-mediated astrocyte shape changes. Furthermore, overexpression of the PAR-1 cytoplasmic tail abrogated thrombin-induced cytoskeletal changes in neuronal cells. Treatment with geldanamycin specifically inhibited activation of RhoA without affecting thrombin-mediated intracellular calcium release, revealing the regulation of a distinct signaling pathway by Hsp90. Taken together, these studies demonstrate that Hsp90 may be essential for PAR-1-mediated signaling to the cytoskeleton.</p>},
	keywords = {Animals, Animals, Newborn, Astrocytes, Cells, Cultured, Cerebral Cortex, Cloning, Molecular, Cytoskeleton, HSP90 Heat-Shock Proteins, Humans, Neurons, Oligodeoxyribonucleotides, Antisense, Rats, Rats, Sprague-Dawley, Receptor, PAR-1, Receptors, Thrombin, Recombinant Fusion Proteins, rhoA GTP-Binding Protein, Saccharomyces cerevisiae, Signal Transduction, Thrombin},
	issn = {0021-9258},
	doi = {10.1074/jbc.M104212200},
	author = {Pai, K S and Mahajan, V B and Lau, A and Cunningham, D D}
}
@article {831,
	title = {Connectin: a homophilic cell adhesion molecule expressed on a subset of muscles and the motoneurons that innervate them in Drosophila.},
	journal = {Cell},
	volume = {70},
	year = {1992},
	month = {1992 Aug 21},
	pages = {553-67},
	abstract = {<p>Each abdominal hemisegment in the Drosophila embryo contains a stereotyped array of 30 muscles, each specifically innervated by one or a few motoneurons. We screened 11,000 enhancer trap lines, isolated several expressing beta-galactosidase in small subsets of muscle fibers prior to innervation, and identified two of these as inserts in connectin and Toll, members of the leucine-rich repeat gene family. Connectin contains a signal sequence, ten leucine-rich repeats, and a putative phosphatidylinositol membrane linkage; in S2 cells, connectin can mediate homophilic cell adhesion. Connectin is expressed on the surface of eight muscles, the motoneurons that innervate them, and several glial cells along the pathways leading to them. During synapse formation, the protein localizes to synaptic sites; afterward, it largely disappears. Thus, connectin is a novel cell adhesion molecule whose expression suggests a role in target recognition.</p>
},
	keywords = {Amino Acid Sequence, Animals, Base Sequence, Cell Adhesion Molecules, Cloning, Molecular, Connectin, DNA, Drosophila, Molecular Sequence Data, Motor Neurons, Muscle Proteins, Muscles, Protein Kinases, Sequence Alignment},
	issn = {0092-8674},
	author = {Nose, A and Mahajan, V B and Goodman, C S}
}
