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. Author manuscript; available in PMC: 2019 Sep 20.
Published in final edited form as: Mol Cell. 2018 Aug 30;71(6):1092–1104.e5. doi: 10.1016/j.molcel.2018.07.035

Table 1.

Membrane binding properties of Akt isoforms and their PH domains determined by SPR analysis.

Kd (nM) for vesiclesa Relative affinityb
(PI34P2/PIP3)
PC/PS/PI34P2 (77:20:3) PC/PS/PIP3 (77:20:3)
Akt1 PHc 310b ± 45 580 ± 80 1.9
Akt2 PHc 220 ± 30 440 ± 50 2.0
Akt3 PHc 340 ± 60 610 ± 65 1.8
Akt1 FLd 960 ± 150 470 ± 70 0.5
Akt2 FLd 410 ± 80 610 ± 100 1.5
Akt3 FLd 900 ± 100 460 ± 90 0.5
Akt1 FLe 880 ± 160 510 ± 210 0.6
Akt2 FLe 360 ± 150 600 ± 200 1.7
Akt3 FLe 940 ± 260 390 ± 120 0.4
a

Data represent mean ± S.D. from triplicate equilibrium SPR measurements.

b

Kd for PIP3 vesicles /Kd for PI34P2 vesicles.

c

Akt PH domains were expressed as C-terminal EGFP-tagged proteins for enhanced stability. EGFP-tagged Akt PH domains and non-tagged Akt PH domains have essentially the same membrane binding properties.

d

Akt full-length proteins expressed in E. coli.

e

Akt full-length proteins expressed in insect cells.