Spatial control of phospholipid flux restricts endoplasmic reticulum sheet formation to allow nuclear envelope breakdown.
The nuclear envelope is a subdomain of the endoplasmic reticulum (ER). Here we characterize CNEP-1 (CTD [C-terminal domain] nuclear envelope phosphatase-1), a nuclear envelope-enriched activator of the ER-associated phosphatidic acid phosphatase lipin that promotes synthesis of major membrane phospholipids over phosphatidylinositol (PI). CNEP-1 inhibition led to ectopic ER sheets in the vicinity of the nucleus that encased the nuclear envelope and interfered with nuclear envelope breakdown (NEBD) during cell division. Reducing PI synthesis suppressed these phenotypes, indicating that CNEP-1 spatially regulates phospholipid flux, biasing it away from PI production in the vicinity of the nuclear envelope to prevent excess ER sheet formation and NEBD defects.
Ludwig Institute for Cancer Research, Department of Cellular and Molecular Medicine, University of California at San Diego, La Jolla, California 92093, USA;
Shirin
S
Bahmanyar
Ronald
R
Biggs
Amber L
AL
Schuh
Arshad
A
Desai
Thomas
T
Müller-Reichert
Anjon
A
Audhya
Jack E
JE
Dixon
Karen
K
Oegema
D000818:Animals; D017173:Caenorhabditis elegans / Q000201:enzymology / Q000378:metabolism*; D002467:Cell Nucleus / Q000378:metabolism; D004625:Embryo, Nonmammalian; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D009685:Nuclear Envelope / Q000378:metabolism*; D009930:Organic Chemicals / Q000378:metabolism; D010743:Phospholipids / Q000378:metabolism*; D010749:Phosphoprotein Phosphatases / Q000378:metabolism
D009930:Organic Chemicals; D010743:Phospholipids; C088310:lipine; D010749:Phosphoprotein Phosphatases
endoplasmic reticulum; lipin; phosphatidylinositol; phospholipid synthesis