The nuclear phosphoinositide response to stress

Mo Chen, Tianmu Wen, Hudson T. Horn, Vishwanatha K. Chandrahas, Narendra Thapa, Suyong Choi, Vincent L. Cryns, Richard A. Anderson

Research output: Contribution to journalReview articlepeer-review

13 Scopus citations


Accumulating evidence reveals that nuclear phosphoinositides (PIs) serve as central signaling hubs that control a multitude of nuclear processes by regulating the activity of nuclear proteins. In response to cellular stressors, PIs accumulate in the nucleus and multiple PI isomers are synthesized by the actions of PI-metabolizing enzymes, kinases, phosphatases and phospholipases. By directly interacting with effector proteins, phosphoinositide signals transduce changes in cellular functions. Here we describe nuclear phosphoinositide signaling in multiple sub-nuclear compartments and summarize the literature that demonstrates roles for specific kinases, phosphatases, and phospholipases in the orchestration of nuclear phosphoinositide signaling in response to cellular stress. Additionally, we discuss the specific PI-protein complexes through which these lipids execute their functions by regulating the configuration, stability, and transcription activity of their effector proteins. Overall, our review provides a detailed landscape of the current understanding of the nuclear PI-protein interactome and its role in shaping the coordinated response to cellular stress.

Original languageEnglish (US)
Pages (from-to)268-289
Number of pages22
JournalCell Cycle
Issue number3
StatePublished - Feb 1 2020
Externally publishedYes


  • Nuclear localization
  • phosphoinositide effectors
  • phosphoinositides signaling
  • stress response

ASJC Scopus subject areas

  • Molecular Biology
  • Developmental Biology
  • Cell Biology


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