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