60
Views
4
CrossRef citations to date
0
Altmetric
Reviews

Role of phospholipase C in nuclear envelope assembly

, &
Pages 103-112 | Published online: 18 Jan 2017

Bibliography

  • WW, Scheer U, Krohne G, Jarasch ED: The nuclear envelope and the architecture of the nuclear periphery. J. Cell Biol. 91, 39S–50S (1981)
  • Heessen S, Fornerod M: The inner nuclear envelope as a transcription factor resting place. EMBO Rep. 8, 914–919 (2007)
  • Akhtar A, Gasser SM: The nuclear envelope and transcriptional control. Nat. Rev. Genet. 8, 507–517 (2007)
  • Gilson E, Laroche T, Gasser SM: Telomeres and the functional architecture of the nucleus. Trends Cell Biol. 3, 128–134 (1993)
  • Ledeen RW, Wu G: Nuclear sphingolipids: metabolism and signaling. J. Lipid Res. 49, 1176–1186 (2008)
  • Byrne RD, Garnier-Lhomme M, Han K et al.: PLC³ is enriched on polyphosphoinositide- rich vesicles to control nuclear envelope assembly. Cell. Signal. 19, 913–922 (2007).
  • Describes for the first time the full lipid composition of nuclear envelope precursor membrane vesicles.
  • Tzur YB, Wilson KL, Gruenbaum Y: SUN-domain proteins: ‘Velcro’ that links the nucleoskeleton to the cytoskeleton. Nat. Rev. Mol. Cell. Biol. 7, 782–788 (2006)
  • Rowat AC, Lammerding J, Herrmann H, Aebi U: Towards an integrated understanding of the structure and mechanics of the cell nucleus. Bioessays 30, 226–236 (2008)
  • Worman HJ, Bonne G: ‘Laminopathies’: a wide spectrum of human diseases. Exp. Cell Res. 313, 2121–2133 (2007)
  • Dechat T, Pfleghaar K, Sengupta K et al.: Nuclear lamins: major factors in the structural organization and function of the nucleus and chromatin. Genes Dev. 22, 832–853 (2008)
  • Zink D, Fischer AH, Nickerson JA: Nuclear structure in cancer cells. Nat. Rev. Cancer 4, 677–687 (2004)
  • Kaufmann SH, Mabry M, Jasti R, Shaper JH: Differential expression of nuclear envelope lamins A and C in human lung cancer cell lines. Cancer Res. 51, 581–586 (1991)
  • Czerniak B, Koss LG, Sherman A: Nuclear pores and DNA ploidy in human bladder carcinomas. Cancer Res. 44, 3752–3756 (1984)
  • Shitashige M, Satow R, Honda K et al.: Regulation of Wnt signaling by the nuclear pore complex. Gastroenterology 134, 1961–1971, 1971 E1961–E1964 (2008)
  • Ghannam G, Takeda A, Camarata T et al.: The oncogene Nup98-HOXA9 induces gene transcription in myeloid cells. J. Biol. Chem. 279, 866–875 (2004)
  • Takeda A, Goolsby C, Yaseen NR: NUP98-HOXA9 induces long-term proliferation and blocks differentiation of primary human CD34+ hematopoietic cells. Cancer Res. 66, 6628–6637 (2006)
  • Anderson DJ, Hetzer MW: The life cycle of the metazoan nuclear envelope. Curr. Opin. Cell Biol. 20, 386–392 (2008)
  • Anderson DJ, Hetzer MW: Nuclear envelope formation by chromatin-mediated reorganization of the endoplasmic reticulum. Nat. Cell Biol. 9, 1160–1166 (2007).
  • A new model of postmitotic envelope formation is described involving the envelopment of nuclei by an endoplasmic reticulum network.
  • Anderson DJ, Hetzer MW: Shaping the endoplasmic reticulum into the nuclear envelope. J. Cell Sci. 121, 137–142 (2008)
  • Longo FJ, Anderson E: The fine structure of pronuclear development and fusion in the sea urchin, Arbacia punctulata. J. Cell Biol. 39, 339–368. (1968).
  • Seminal electron microscopy study of fertilization in sea urchin eggs.
  • Cameron LA, Poccia DL: In vitro development of the sea urchin male pronucleus. Dev. Biol. 162, 568–578. (1994)
  • Lohka MJ, Masui Y: Formation in vitro of sperm pronuclei and mitotic chromosomes induced by amphibian ooplasmic components. Science 220, 719–721 (1983)
  • Ulitzur N, Gruenbaum Y: Nuclear envelope assembly around sperm chromatin in cell-free preparations from Drosophila embryos. FEBS Lett. 259, 113–116 (1989)
  • Byrne RD, Zhendre V, Larijani B, Poccia DL: Nuclear envelope formation in vitro: a sea urchin egg cell-free system. In: The Nucleus Volume 2: Chromatin, Transcription, Envelope, Proteins, Dynamics, and Imaging. Hancock R (Ed.). Humana Press, NY, USA 207–223 (2008)
  • Collas P, Poccia D: Lipophilic organizing structures of sperm nuclei target membrane vesicle binding and are incorporated into the nuclear envelope. Dev. Biol. 169, 123–135 (1995)
  • Stephens S, Beyer B, Balthazar-Stablein U et al.: Two kinase activities are sufficient for sea urchin sperm chromatin decondensation in vitro. Mol. Reprod. Dev. 62, 496–503 (2002)
  • Collas P, Poccia D: Distinct egg membrane vesicles differing in binding and fusion properties contribute to sea urchin male pronuclear envelopes formed in vitro. J. Cell. Sci. 109, 1275–1283 (1996).
  • Separation and characterization of the distinct nuclear envelope precursor membrane fractions, and describes their interdependency during envelope formation.
  • Collas P, Courvalin JC, Poccia D: Targeting of membranes to sea urchin sperm chromatin is mediated by a lamin B receptor-like integral membrane protein. J. Cell Biol. 135, 1715–1725 (1996)
  • Byrne RD, Barona TM, Garnier M et al.: Nuclear envelope assembly is promoted by phosphoinositide-specific phospholipase C with selective recruitment of phosphatidylinositol-enriched membranes. Biochem. J. 387, 393–400 (2005)
  • Larijani B, Poccia DL, Dickinson LC: Phospholipid identification and quantification of membrane vesicle subfractions by 31P–1H two-dimensional nuclear magnetic resonance. Lipids 35, 1289–1297 (2000)
  • Barona T, Byrne RD, Pettitt TR et al.: Diacylglycerol induces fusion of nuclear envelope membrane precursor vesicles. J. Biol. Chem. 280, 41171–41177 (2005).
  • Pivotal role for the fusogenic lipid diaglycerol in nuclear envelope formation is demonstrated in model membranes.
  • Garnier-Lhomme M, Dufourc EJ, Larijani B, Poccia D: Lipid quantification and structure determination of nuclear envelope precursor membranes in the sea urchin. In: Lipid Signaling Protocols. Larijani B, Woscholski R, Rosser CA (Eds). Humana Press, NY, USA 89–110 (2008)
  • Parker PJ: The ubiquitous phosphoinositides. Biochem. Soc. Trans. 32, 893–898 (2004)
  • Allan D, Thomas P, Michell RH: Rapid transbilayer diffusion of 1,2-diacylglycerol and its relevance to control of membrane curvature. Nature 276, 289–290 (1978)
  • Kozlovsky Y, Chernomordik LV, Kozlov MM: Lipid intermediates in membrane fusion: formation, structure, and decay of hemifusion diaphragm. Biophys. J. 83, 2634–2651 (2002)
  • Chernomordik LV, Kozlov MM: Mechanics of membrane fusion. Nat. Struct. Mol. Biol. 15, 675–683 (2008)
  • Martelli AM, Manzoli L, Cocco L: Nuclear inositides: facts and perspectives. Pharmacol. Ther. 101, 47–64 (2004)
  • Visnjic D, Banfic H: Nuclear phospholipid signaling: phosphatidylinositol-specific phospholipase C and phosphoinositide 3-kinase. Pflugers Arch. 455, 19–30 (2007)
  • Chan CB, Ye K: PIKE GTPase are phosphoinositide-3-kinase enhancers, suppressing programmed cell death. J. Cell. Mol. Med. 11, 39–53 (2007)
  • Martelli AM, Fala F, Faenza I et al.: Metabolism and signaling activities of nuclear lipids. Cell. Mol. Life Sci. 61, 1143–1156 (2004)
  • Larijani B, Dufourc EJ: Polyunsaturated phosphatidylinositol and diacylglycerol substantially modify the fluidity and polymorphism of biomembranes: a solid-state deuterium NMR study. Lipids 41, 925–932 (2006).
  • For the first time, a role for phosphoinositide lipids was demonstrated in nuclear envelope assembly.
  • Rongish BJ, Wu W, Kinsey WH: Fertilization-induced activation of phospholipase C in the sea urchin egg. Dev. Biol. 215, 147–154 (1999)
  • Albi E, Rossi G, Maraldi NM et al.: Involvement of nuclear phosphatidylinositol-dependent phospholipases C in cell cycle progression during rat liver regeneration. J. Cell Physiol. 197, 181–188 (2003)
  • Sudhof TC: The synaptic vesicle cycle. Annu. Rev. Neurosci. 27, 509–547 (2004)
  • Larijani B, Barona TM, Poccia DL: Role for phosphatidylinositol in nuclear envelope formation. Biochem. J. 356, 495–501. (2001)
  • Kim HK, Kim JW, Zilberstein A et al.: PDGF stimulation of inositol phospholipid hydrolysis requires PLC-³ 1 phosphorylation on tyrosine residues 783 and 1254. Cell 65, 435–441 (1991)
  • Clarke PR, Zhang C: Spatial and temporal coordination of mitosis by Ran GTPase. Nat. Rev. Mol. Cell Biol. 9, 464–477 (2008)
  • Jordens I, Marsman M, Kuijl C, Neefjes J: Rab proteins, connecting transport and vesicle fusion. Traffic 6, 1070–1077 (2005)
  • Coward K, Owen H, Tunwell R, Swann K, Parrington J: Phospholipid binding properties and functional characterization of a sea urchin phospholipase C´ in urchin and mouse eggs. Biochem. Biophys. Res. Commun. 357, 964–970 (2007)
  • Kulisz A, Dowal L, Scarlata S, Shen SS: Cloning and characterization of a phospholipase C-² isoform from the sea urchin Lytechinus pictus. Dev. Growth Differ. 47, 307–321 (2005)
  • Bauer CS, Woolley RJ, Teschemacher AG, Seward EP: Potentiation of exocytosis by phospholipase C-coupled G-protein-coupled receptors requires the priming protein Munc13–1. J. Neurosci. 27, 212–219 (2007)
  • Beaudouin J, Gerlich D, Daigle N, Eils R, Ellenberg J: Nuclear envelope breakdown proceeds by microtubule-induced tearing of the lamina. Cell 108, 83–96 (2002)
  • Salina D, Bodoor K, Eckley DM et al.: Cytoplasmic dynein as a facilitator of nuclear envelope breakdown. Cell 108, 97–107 (2002)
  • Macaulay C, Forbes DJ: Assembly of the nuclear pore: biochemically distinct steps revealed with NEM, GTP ³ S, and BAPTA. J. Cell Biol. 132, 5–20 (1996)
  • Mayorga LS, Diaz R, Colombo MI, Stahl PD: GTP ³ S stimulation of endosome fusion suggests a role for a GTP-binding protein in the priming of vesicles before fusion. Cell Regul. 1, 113–124 (1989).

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.