The GFP-ML1Nx2 probe does not dissociate from the Rab5-positive membranes in response to blockade of PtdIns3<i>P</i> synthesis. Gerald R. V. Hammond Shunsuke Takasuga Takehiko Sasaki Tamas Balla 10.1371/journal.pone.0139957.g002 https://plos.figshare.com/articles/figure/_The_GFP_ML1Nx2_probe_does_not_dissociate_from_the_Rab5_positive_membranes_in_response_to_blockade_of_PtdIns3_P_synthesis_/1573629 <p>Images show a representative cell expressing the three indicated constructs before and 1 h after treatment with 100 nM wortmannin, which inhibits the PI 3-kinase that synthesizes PtdIns3<i>P</i>, the substrate for PtdIns(3,5)<i>P</i><sub>2</sub> synthesis. The graph at right shows mean fluorescence intensity at Rab5-positive membranes normalized to the whole cell for the indicated construct (data are means ± s.e.m. of 12 cells from three independent experiments). No dissociation of the GFP-ML1Nx2 is observed despite robust depletion of FYVE-EEA1 within 15 min of wortmannin application. Scale bar = 15 μm.</p> 2015-10-13 03:18:21 ML 1Nx Eukaryotic cells probe phosphatidylinositol endocytic membrane traffic organism physiology biosensor localization PtdIn genomic interventions