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. Author manuscript; available in PMC: 2009 Oct 5.
Published in final edited form as: Oncogene. 2008 Sep 18;27(41):5486–5496. doi: 10.1038/onc.2008.244

Figure 4.

Figure 4

The interactions with p85 and with Ras define two distinct molecular mechanisms for the gain of function seen in the hot spot mutations in p110α. The helical domain mutations are largely but not completely independent of binding to p85 but require the interaction with Ras. The kinase domain mutation completely depends on the interaction with p85 but is not affected by a loss of Ras-binding. However, the kinase domain mutation still shows residual signaling activity in the absence of p85-binding.