Reversible chemical dimerizer-induced recovery of PIP2 levels moves clathrin to the plasma membrane

Martina Schifferer, Suihan Feng, Frank Stein, Christian Tischer, Carsten Schultz

Research output: Contribution to journalArticlepeer-review

8 Scopus citations

Abstract

Chemical dimerizers are powerful non-invasive tools for bringing molecules together inside intact cells. We recently introduced a rapidly reversible chemical dimerizer system which enables transient translocation of enzymes to and from the plasma membrane (PM). Here we have applied this system to transiently activate phosphatidylinositol 4,5-bisphosphate (PIP2) breakdown at the PM via translocation of phosphoinositide 5-phosphatase (5Ptase). We found that the PIP2 sensor phospholipase C-δ PH domain (PLCδ-PH) is released from the PM upon addition of the reversible chemical dimerizer rCD1. By outcompeting rCD1, rapid release of the 5Ptase from the PM is followed by PIP2 recovery. This permits the observation of the PIP2-dependent clathrin assembly at the PM.

Original languageEnglish (US)
Pages (from-to)2862-2867
Number of pages6
JournalBioorganic and Medicinal Chemistry
Volume23
Issue number12
DOIs
StatePublished - May 29 2015

Keywords

  • Adapter proteins
  • Clathrin
  • Endocytosis
  • Phosphatidylinositol 4,5-bisphosphate
  • Phosphoinositol 5-phosphatase

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmaceutical Science
  • Drug Discovery
  • Clinical Biochemistry
  • Organic Chemistry

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