TY - JOUR
T1 - The nuclear phosphoinositide response to stress
AU - Chen, Mo
AU - Wen, Tianmu
AU - Horn, Hudson T.
AU - Chandrahas, Vishwanatha K.
AU - Thapa, Narendra
AU - Choi, Suyong
AU - Cryns, Vincent L.
AU - Anderson, Richard A.
N1 - Funding Information:
We wish to thank members of the Anderson and Cryns lab and apologize to the authors whose work was not cited due to space limitations. This work was supported in part by a National Institutes of Health grant GM114386 (R.A.A.), Department of Defense Breast Cancer Research Program grants W81XWH-17-1-0258 (R.A.A.) and W81XWH-17-1-0259 (V.L.C.), and a grant from the Breast Cancer Research Foundation (V.L.C.).
Funding Information:
This work was supported by the National Institutes of Health [GM114386];U.S. Department of Defense [W81XWH-17-1-0259];U.S. Department of Defense [W81XWH-17-1-0258]. We wish to thank members of the Anderson and Cryns lab and apologize to the authors whose work was not cited due to space limitations. This work was supported in part by a National Institutes of Health grant GM114386 (R.A.A.), Department of Defense Breast Cancer Research Program grants W81XWH-17-1-0258 (R.A.A.) and W81XWH-17-1-0259 (V.L.C.), and a grant from the Breast Cancer Research Foundation (V.L.C.).
Publisher Copyright:
© 2020, © 2020 Informa UK Limited, trading as Taylor & Francis Group.
PY - 2020/2/1
Y1 - 2020/2/1
N2 - 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.
AB - 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.
KW - Nuclear localization
KW - phosphoinositide effectors
KW - phosphoinositides signaling
KW - stress response
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U2 - 10.1080/15384101.2019.1711316
DO - 10.1080/15384101.2019.1711316
M3 - Review article
C2 - 31902273
AN - SCOPUS:85077847016
SN - 1538-4101
VL - 19
SP - 268
EP - 289
JO - Cell Cycle
JF - Cell Cycle
IS - 3
ER -