作者: Wei Tao , Cheryl L. Malone , Addison D. Ault , Robert J. Deschenes , Jan S. Fassler
DOI: 10.1046/J.1365-2958.2002.02757.X
关键词: MAP kinase kinase kinase 、 Biology 、 Cell biology 、 Biochemistry 、 Mitogen-activated protein kinase kinase 、 Histidine kinase 、 ASK1 、 Cyclin-dependent kinase 9 、 Cyclin-dependent kinase 2 、 Kinase activity 、 MAP2K7
摘要: Summary The yeast histidine kinase, Sln1p, is a plasma membrane-associated osmosensor that regulates the activity of osmotic stress MAP kinase pathway. Changes in environment cell influence autokinase cytoplasmic domain Sln1p. Neither nature stimulus, mechanism by which signal transduced nor manner regulated currently clear. We have identified several mutations located linker region Sln1 (just upstream domain) cause hyperactivity kinase. This kinases largely uncharacterized, but its location between transmembrane domains and suggests it may potential role transduction. In this study, we investigated order to understand function transduction regulation activity. Our results indicate forms coiled-coil structure suggest alterations induced altering alignment phospho-accepting with respect catalytic