FBXW7 regulates DISC1 stability via the ubiquitin-proteosome system

Autor: Yalla, K., Elliott, C., Day, J.P., Findlay, J., Barratt, S., Hughes, Z.A., Wilson, L., Whiteley, E., Popiolek, M., Li, Y., Dunlop, J., Killick, R., Adams, D.R., Brandon, N.J., Houslay, M.D., Hao, B., Baillie, G.S.

Publikováno v: Molecular psychiatry, vol 23, iss 5
Yalla, K, Elliott, C, Day, J P, Findlay, J, Barratt, S, Hughes, Z, Wilson, L, Whiteley, E, Popiolek, M, Li, Y, Dunlop, J, Killick, R, Adams, D R, Brandon, N J, Houslay, M D, Hao, B & Baillie, G S 2018, ' FBXW7 regulates DISC1 stability via the ubiquitin-proteosome system ', Molecular Psychiatry, vol. 23, no. 5, pp. 1278-1286 . https://doi.org/10.1038/mp.2017.138

Disrupted in schizophrenia 1 (DISC1) is a multi-functional scaffolding protein that has been associated with neuropsychiatric disease. The role of DISC1 is to assemble protein complexes that promote neural development and signaling, hence tight contr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::b9ae79a531b22aa87e8d823362967754
https://escholarship.org/uc/item/2z19b6cg

Small molecule AKAP/PKA interaction disruptors that activate PKA interfere with compartmentalized cAMP signaling in cardiac myocytes

Autor: Christian, F., Szaszak, M., Friedl, S., Drewianka, S., Lorenz, D., Goncalves, A., Furkert, J., Vargas, C., Schmieder, P., Goetz, F., Zuehlke, K., Moutty, M., Goettert, H., Joshi, M., Reif, B., Haase, H., Morano, I., Grossmann, S., Klukovits, A., Verli, J., Gaspar, R., Noack, C., Bergmann, M., Kass, R., Hampel, K., Kashin, D., Genieser, H.G., Herberg, F.W., Willoughby, D., Cooper, D.M., Baillie, G.S., Houslay, M.D., von Kries, J.P., Zimmermann, B., Rosenthal, W., Klussmann, E.

A-kinase anchoring proteins (AKAPs) tether protein kinase A (PKA) and other signaling proteins to defined intracellular sites, thereby establishing compartmentalized cAMP signaling. AKAP-PKA interactions play key roles in various cellular processes i

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=mdc______med::9a5f045c1e1adb774514b3eca737938e
http://edoc.mdc-berlin.de/11331/1/11331oa.pdf

p75 neurotrophin receptor regulates tissue fibrosis through inhibition of plasminogen activation via a PDE4/cAMP/PKA pathway

Autor: Sachs, B.D., Baillie, G.S., McCall, J.R., Passino, M.A., Schachtrup, C., Wallace, D.A., Dunlop, A.J., MacKenzie, K.F., Klussmann, E., Lynch, M.J., Sikorski, S.L., Nuriel, T., Tsigelny, I., Zhang, J., Houslay, M.D., Chao, M.V., Akassoglou, K.

Clearance of fibrin through proteolytic degradation is a critical step of matrix remodeling that contributes to tissue repair in a variety of pathological conditions, such as stroke, atherosclerosis, and pulmonary disease. However, the molecular mech

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::f708752f795cae1e50122aef181472e3
https://eprints.gla.ac.uk/4108/1/pubmedredirect.html

Scanning peptide array analysis identify overlapping binding sites for the signaling scaffold proteins, beta-arestin and RACK1 in the cAMP-specific phosphodiesterase, PDE4D5

Autor: Bolger, G.B., Baillie, G.S., Li, X., Lynch, M.J., Herzyk, P., Mohamed, A., Mitchell, L., McCahill, A., Hundsrucker, C., Klussmann, E., Adams, D.R., Houslay, M.D.

The cAMP-specific phosphodiesterase PDE4D5 can interact with the signalling scaffold proteins RACK (receptors for activated C-kinase) 1 and β-arrestin. Two-hybrid and co-immunoprecipitation analyses showed that RACK1 and β-arrestin interact with PD

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=core_ac_uk__::70390346948b7fba155ed4070be822ca
https://eprints.gla.ac.uk/3570/1/pubmedredirect.html

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