Live cell imaging with protein domains capable of recognizing phosphatidylinositol 4,5-bisphosphate; a comparative study |
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| Authors: | Zsofia Szentpetery Andras Balla Yeun Ju Kim Mark A Lemmon Tamas Balla |
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| Institution: | (1) Sections on Molecular Signal Transduction, Program for Developmental Neuroscience, NICHD, National Institutes of Health, Bethesda, MD 20892, USA;(2) Department of Physiology, Semmelweis University, School of Medicine, Budapest, Hungary;(3) Department of Biochemistry and Biophysics, School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA |
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| Abstract: | Background Phosphatidylinositol 4,5-bisphosphate PtdIns(4,5)P
2] is a critically important regulatory phospholipid found in the plasma membrane of all eukaryotic cells. In addition to being
a precursor of important second messengers, PtdIns(4,5)P
2 also regulates ion channels and transporters and serves the endocytic machinery by recruiting clathrin adaptor proteins.
Visualization of the localization and dynamic changes in PtdIns(4,5)P
2 levels in living cells is critical to understanding the biology of PtdIns(4,5)P
2. This has been mostly achieved with the use of the pleckstrin homology (PH) domain of PLCδ1 fused to GFP. Here we report
on a comparative analysis of several recently-described yeast PH domains as well as the mammalian Tubby domain to evaluate
their usefulness as PtdIns(4,5)P
2 imaging tools. |
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