%0 Journal Article %1 breitkreutz2010global %A Breitkreutz, Ashton %A Choi2, Hyungwon %A Sharom, Jeffrey R. %A Boucher, Lorrie %A Neduva, Victor %A Larsen, Brett %A Lin, Zhen-Yuan %A Breitkreutz, Bobby-Joe %A Stark, Chris %A Liu, Guomin %A Ahn, Jessica %A Dewar-Darch, Danielle %A Reguly, Teresa %A Tang, Xiaojing %A Almeida, Ricardo %A Qin, Zhaohui Steve %A Pawson, Tony %A Gingras, Anne-Claude %A Nesvizhskii, Alexey I. %A and Mike Tyers, %D 2010 %I American Association for the Advancement of Science %J Science %K biology network protein social.network %N 5981 %P 1043 %R 10.1126/science.1176495 %T A global protein kinase and phosphatase interaction network in yeast %V 328 %X The interactions of protein kinases and phosphatases with their regulatory subunits and substrates underpin cellular regulation. We identified a kinase and phosphatase interaction (KPI) network of 1844 interactions in budding yeast by mass spectrometric analysis of protein complexes. The KPI network contained many dense local regions of interactions that suggested new functions. Notably, the cell cycle phosphatase Cdc14 associated with multiple kinases that revealed roles for Cdc14 in mitogen-activated protein kinase signaling, the DNA damage response, and metabolism, whereas interactions of the target of rapamycin complex 1 (TORC1) uncovered new effector kinases in nitrogen and carbon metabolism. An extensive backbone of kinase-kinase interactions cross-connects the proteome and may serve to coordinate diverse cellular responses.

@article{breitkreutz2010global, abstract = {The interactions of protein kinases and phosphatases with their regulatory subunits and substrates underpin cellular regulation. We identified a kinase and phosphatase interaction (KPI) network of 1844 interactions in budding yeast by mass spectrometric analysis of protein complexes. The KPI network contained many dense local regions of interactions that suggested new functions. Notably, the cell cycle phosphatase Cdc14 associated with multiple kinases that revealed roles for Cdc14 in mitogen-activated protein kinase signaling, the DNA damage response, and metabolism, whereas interactions of the target of rapamycin complex 1 (TORC1) uncovered new effector kinases in nitrogen and carbon metabolism. An extensive backbone of kinase-kinase interactions cross-connects the proteome and may serve to coordinate diverse cellular responses.}, added-at = {2011-09-27T22:48:43.000+0200}, author = {Breitkreutz, Ashton and Choi2, Hyungwon and Sharom, Jeffrey R. and Boucher, Lorrie and Neduva, Victor and Larsen, Brett and Lin, Zhen-Yuan and Breitkreutz, Bobby-Joe and Stark, Chris and Liu, Guomin and Ahn, Jessica and Dewar-Darch, Danielle and Reguly, Teresa and Tang, Xiaojing and Almeida, Ricardo and Qin, Zhaohui Steve and Pawson, Tony and Gingras, Anne-Claude and Nesvizhskii, Alexey I. and and Mike Tyers}, biburl = {https://www.bibsonomy.org/bibtex/2899f44acfcf7cce756ca8af8c307de75/ytyoun}, doi = {10.1126/science.1176495}, interhash = {5cddebeea0990090f721e54ad4e14162}, intrahash = {899f44acfcf7cce756ca8af8c307de75}, journal = {Science}, keywords = {biology network protein social.network}, number = 5981, pages = 1043, publisher = {American Association for the Advancement of Science}, timestamp = {2016-11-16T07:57:34.000+0100}, title = {A global protein kinase and phosphatase interaction network in yeast}, volume = 328, year = 2010 }