title: Nuclear Phosphatidylinositol Signaling: Focus on Phosphatidylinositol Phosphate Kinases and Phospholipases C.
abstract: Phosphatidylinositol (PI) metabolism represents the core of a network of signaling pathways which modulate many cellular functions including cell proliferation, cell differentiation, apoptosis, and membrane trafficking. An array of kinases, phosphatases, and lipases acts on PI creating an important number of second messengers involved in different cellular processes. Although, commonly, PI signaling was described to take place at the plasma membrane, many evidences indicated the existence of a PI cycle residing in the nuclear compartment of eukaryotic cells. The discovery of this mechanism shed new light on many nuclear functions, such as gene transcription, DNA modifications, and RNA expression. As these two PI cycles take place independently of one another, understanding how nuclear lipid signaling functions and modulates nuclear output is fundamental in the study of many cellular processes. J. Cell. Physiol. 231: 1645-1655, 2016. © 2015 Wiley Periodicals, Inc.
authors.affiliation: Department of Biomedical Sciences, University of Bologna, Bologna, Italy.
authors.forename: Alessandro
authors.initials: A
authors.lastname: Poli
authors.affiliation: Department of Biomedical Sciences, University of Bologna, Bologna, Italy.
authors.forename: Anna Maria
authors.initials: AM
authors.lastname: Billi
authors.affiliation: Department of Biomedical Sciences, University of Bologna, Bologna, Italy.
authors.forename: Sara
authors.initials: S
authors.lastname: Mongiorgi
authors.affiliation: Department of Biomedical Sciences, University of Bologna, Bologna, Italy.
authors.forename: Stefano
authors.initials: S
authors.lastname: Ratti
authors.affiliation: Department of Microbiology and Immunology, Brody School of Medicine, East Carolina University, Greenville, North Carolina.
authors.forename: James A
authors.initials: JA
authors.lastname: McCubrey
authors.affiliation: School of Life Sciences, Ulsan National Institute of Science and Technology, Ulsan, Republic of Korea.
authors.forename: Pann-Ghill
authors.initials: PG
authors.lastname: Suh
authors.affiliation: Department of Biomedical Sciences, University of Bologna, Bologna, Italy.
authors.forename: Lucio
authors.initials: L
authors.lastname: Cocco
authors.affiliation: Department of Biomedical Sciences, University of Bologna, Bologna, Italy.
authors.forename: Giulia
authors.initials: G
authors.lastname: Ramazzotti
mesh_terms: D000818:Animals; D059447:Cell Cycle Checkpoints; D002454:Cell Differentiation; D002467:Cell Nucleus / Q000201:enzymology* / Q000473:pathology; D049109:Cell Proliferation; D006801:Humans; D006868:Hydrolysis; D009190:Myelodysplastic Syndromes / Q000201:enzymology / Q000473:pathology; D009369:Neoplasms / Q000201:enzymology / Q000473:pathology; D019269:Phosphatidylinositol 4,5-Diphosphate / Q000378:metabolism; D010716:Phosphatidylinositols / Q000378:metabolism*; D017853:Phosphotransferases (Alcohol Group Acceptor) / Q000378:metabolism*; D015290:Second Messenger Systems; D014158:Transcription, Genetic; D010738:Type C Phospholipases / Q000378:metabolism*
chemical_list: D019269:Phosphatidylinositol 4,5-Diphosphate; D010716:Phosphatidylinositols; D017853:Phosphotransferases (Alcohol Group Acceptor); D010738:Type C Phospholipases