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. 2019 Apr 4;14(4):e0214736. doi: 10.1371/journal.pone.0214736

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© 2019 Tsujioka et al

This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

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Fig 2 — (A) Biochemical assay to determine the binding specificities of the FERM domain of talin B to the plasma membrane components. A bacterial lysate containing GST-FERM was reacted with a membrane strip spotted with 15 unique lipids. GST-FERM bound to the indicated lipids was immunologically detected. TG, triglyceride; DAG, diacylglycerol; PA, phosphatidic acid; PS, phosphatidylserine; PE, phosphatidylethanolamine; PC, phosphatidylcholine; PG, phosphatidylglycerol; CL, cardiolipin; PI, phosphatidylinositol; PIP, PtdIns(4)P; PIP₂, PtdIns(4,5)P₂; PIP₃, PtdIns(3,4,5)P₃; CHO, cholesterol; SPH, sphingomyelin; and SUL, 3-sulfogalactosylceramide. (B) Sub-cellular localizations of the GFP-PH domain of CRAC, a probe for PtdIns(3,4,5)P₃, as well as GFP-talin B and talin A-GFP, in the cAMP gradient after treatment of starved cells with latrunculin A. Scale bar: 10 μm.