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Rapidly inducible changes in phosphatidylinositol 4,5-bisphosphate levels influence multiple regulatory functions of the lipid in intact living cells

Varnai, Peter, Thyagarajan, Baskaran, Rohacs, Tibor, Balla, Tamas·2006·The Journal of Cell Biology
DOI 10.1083/jcb.200607116PMC PMC2064515
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Abstract

Rapamycin (rapa)-induced heterodimerization of the FRB domain of the mammalian target of rapa and FKBP12 was used to translocate a phosphoinositide 5-phosphatase (5-ptase) enzyme to the plasma membrane (PM) to evoke rapid changes in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) levels. Rapa-induced PM recruitment of a truncated type IV 5-ptase containing only the 5-ptase domain fused to FKBP12 rapidly decreased PM PtdIns(4,5)P2 as monitored by the PLCδ1PH-GFP fusion construct. This decrease was paralleled by rapid termination of the ATP-induced Ca2+ signal and the prompt inactivation of menthol-activated transient receptor potential melastatin 8 (TRPM8) channels. Depletion of PM PtdIns(4,5)P2 was associated with a complete blockade of transferrin uptake and inhibition of epidermal growth factor internalization. None of these changes were observed upon rapa-induced translocation of an mRFP-FKBP12 fusion protein that was used as a control. These data demonstrate that rapid inducible depletion of PM PtdIns(4,5)P2 is a powerful tool to study the multiple regulatory roles of this phospholipid and to study differential sensitivities of various processes to PtdIns(4,5)P2 depletion.

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Metadata

Authors
Varnai, P., Thyagarajan, B., Rohacs, T., & Balla, T.
Venue
The Journal of Cell Biology
Publisher
Rockefeller University Press
Published
2006-11-06
Volume
175
Issue
3
Pages
377-382
ISSN
  • 1540-8140
  • 0021-9525
DOI
10.1083/jcb.200607116
PMC
PMC2064515
Cited by
333
References
1
Language
en

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