Unknown

Dataset Information

0

The ML1Nx2 Phosphatidylinositol 3,5-Bisphosphate Probe Shows Poor Selectivity in Cells.


ABSTRACT: Phosphatidylinositol (3,5)-bisphosphate (PtdIns(3,5)P2) is a quantitatively minor phospholipid in eukaryotic cells that plays a fundamental role in regulating endocytic membrane traffic. Despite its clear importance for cellular function and organism physiology, mechanistic details of its biology have so far not been fully elucidated. In part, this is due to a lack of experimental tools that specifically probe for PtdIns(3,5)P2 in cells to unambiguously identify its dynamics and site(s) of action. In this study, we have evaluated a recently reported PtdIns(3,5)P2 biosensor, GFP-ML1Nx2, for its veracity as such a probe. We report that, in live cells, the localization of this biosensor to sub-cellular compartments is largely independent of PtdIns(3,5)P2, as assessed after pharmacological, chemical genetic or genomic interventions that block the lipid's synthesis. We therefore conclude that it is unwise to interpret the localization of ML1Nx2 as a true and unbiased biosensor for PtdIns(3,5)P2.

SUBMITTER: Hammond GR 

PROVIDER: S-EPMC4604148 | biostudies-literature | 2015

REPOSITORIES: biostudies-literature

altmetric image

Publications

The ML1Nx2 Phosphatidylinositol 3,5-Bisphosphate Probe Shows Poor Selectivity in Cells.

Hammond Gerald R V GR   Takasuga Shunsuke S   Sasaki Takehiko T   Balla Tamas T  

PloS one 20151013 10


Phosphatidylinositol (3,5)-bisphosphate (PtdIns(3,5)P2) is a quantitatively minor phospholipid in eukaryotic cells that plays a fundamental role in regulating endocytic membrane traffic. Despite its clear importance for cellular function and organism physiology, mechanistic details of its biology have so far not been fully elucidated. In part, this is due to a lack of experimental tools that specifically probe for PtdIns(3,5)P2 in cells to unambiguously identify its dynamics and site(s) of actio  ...[more]

Similar Datasets

| S-EPMC3876232 | biostudies-literature
| S-EPMC3906640 | biostudies-literature
| S-EPMC5921506 | biostudies-literature
| S-EPMC3001011 | biostudies-literature
| S-EPMC3666695 | biostudies-literature
| S-EPMC5385934 | biostudies-literature
| S-EPMC6589561 | biostudies-literature
| S-EPMC10012956 | biostudies-literature
| S-EPMC5494527 | biostudies-literature
| S-EPMC2173454 | biostudies-literature