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. 2016 May 31;4:49. doi: 10.3389/fcell.2016.00049

Figure 1.

Figure 1

Allosteric regulation of KSR2. A regulatory RAF interacts with KSR in cis to induce a conformational switch on MEK to expose its activation loop, subject to phosphorylation by RAF in trans. In the KSR2–MEK1 hetero-tetramer (left), the inaccessible activation segment of MEK1 is released through the interaction of KSR2 with RAF, induced by a conformational change, allowing a “catalytic” RAF to phosphorylate MEK (right).