The nuclear phosphoinositide response to stress
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...
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| Veröffentlicht in: | Cell cycle (Georgetown, Tex.) Tex.), 2020-02, Vol.19 (3), p.268-289 |
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| creator | Chen, Mo Wen, Tianmu Horn, Hudson T. Chandrahas, Vishwanatha K. Thapa, Narendra Choi, Suyong Cryns, Vincent L. Anderson, Richard A. |
| description | 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. |
| doi_str_mv | 10.1080/15384101.2019.1711316 |
| format | Article |
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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. 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Wen, Tianmu ; Horn, Hudson T. ; Chandrahas, Vishwanatha K. ; Thapa, Narendra ; Choi, Suyong ; Cryns, Vincent L. ; Anderson, Richard A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c534t-759c2a970ca666d706a62a5cbaff44bdc8395c4d7c04bfb96ba37c03566bcfbb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>Animals</topic><topic>Cell Nucleus - enzymology</topic><topic>Cell Nucleus - metabolism</topic><topic>Humans</topic><topic>Nuclear localization</topic><topic>Nuclear Proteins - metabolism</topic><topic>Phosphatidylinositol 3-Kinases - metabolism</topic><topic>Phosphatidylinositols - metabolism</topic><topic>phosphoinositide effectors</topic><topic>Phosphoinositide Phosphatases - metabolism</topic><topic>phosphoinositides signaling</topic><topic>Review</topic><topic>Signal Transduction - genetics</topic><topic>stress response</topic><topic>Stress, Physiological - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Chen, Mo</creatorcontrib><creatorcontrib>Wen, Tianmu</creatorcontrib><creatorcontrib>Horn, Hudson T.</creatorcontrib><creatorcontrib>Chandrahas, Vishwanatha K.</creatorcontrib><creatorcontrib>Thapa, Narendra</creatorcontrib><creatorcontrib>Choi, Suyong</creatorcontrib><creatorcontrib>Cryns, Vincent L.</creatorcontrib><creatorcontrib>Anderson, Richard A.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Cell cycle (Georgetown, Tex.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Chen, Mo</au><au>Wen, Tianmu</au><au>Horn, Hudson T.</au><au>Chandrahas, Vishwanatha K.</au><au>Thapa, Narendra</au><au>Choi, Suyong</au><au>Cryns, Vincent L.</au><au>Anderson, Richard A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The nuclear phosphoinositide response to stress</atitle><jtitle>Cell cycle (Georgetown, Tex.)</jtitle><addtitle>Cell Cycle</addtitle><date>2020-02-01</date><risdate>2020</risdate><volume>19</volume><issue>3</issue><spage>268</spage><epage>289</epage><pages>268-289</pages><issn>1538-4101</issn><eissn>1551-4005</eissn><abstract>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.</abstract><cop>United States</cop><pub>Taylor & Francis</pub><pmid>31902273</pmid><doi>10.1080/15384101.2019.1711316</doi><tpages>22</tpages><orcidid>https://orcid.org/0000-0003-0355-2268</orcidid><orcidid>https://orcid.org/0000-0002-1147-4194</orcidid><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central |
| subjects | Animals Cell Nucleus - enzymology Cell Nucleus - metabolism Humans Nuclear localization Nuclear Proteins - metabolism Phosphatidylinositol 3-Kinases - metabolism Phosphatidylinositols - metabolism phosphoinositide effectors Phosphoinositide Phosphatases - metabolism phosphoinositides signaling Review Signal Transduction - genetics stress response Stress, Physiological - genetics |
| title | The nuclear phosphoinositide response to stress |
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