• Register
Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.


Leaving Community

Are you sure you want to leave this community? Leaving the community will revoke any permissions you have been granted in this community.


Inactivation of the C. elegans lipin homolog leads to ER disorganization and to defects in the breakdown and reassembly of the nuclear envelope.

The nuclear envelope (NE) is a dynamic structure, undergoing periods of growth, breakdown and reassembly during the cell cycle. In yeast, altering lipid synthesis by inactivating the yeast homolog of lipin, a phosphatidic acid phosphohydrolase, leads to disorganization of the peripheral ER and abnormal nuclear shape. These results suggest that lipid metabolism contributes to NE dynamics; however, since yeast undergo closed mitosis, the relevance of these observations to higher eukaryotes is unclear. In mammals, lipin has been implicated in adipose tissue differentiation, insulin resistance, lipid storage and obesity, but the underlying cellular defects caused by altering lipin levels are not known. Here, we identify the Caenorhabditis elegans lipin homolog (LPIN-1) and examine its affect on NE dynamics. We find that downregulating LPIN-1 by RNAi results in the appearance of membrane sheets and other abnormal structures in the peripheral ER. Moreover, lpin-1 RNAi causes defects in NE breakdown, abnormal chromosome segregation and irregular nuclear morphology. These results uncover cellular processes affected by lipin in metazoa, and suggest that lipid synthesis has a role in NE dynamics.

Pubmed ID: 19494126


  • Golden A
  • Liu J
  • Cohen-Fix O


Journal of cell science

Publication Data

June 15, 2009

Associated Grants

  • Agency: NIGMS NIH HHS, Id: R01 GM066953
  • Agency: Intramural NIH HHS, Id:

Mesh Terms

  • Animals
  • Animals, Genetically Modified
  • Caenorhabditis elegans Proteins
  • Cell Nucleus
  • Cell Nucleus Division
  • Chromosome Segregation
  • Embryo, Nonmammalian
  • Endoplasmic Reticulum
  • Gene Silencing
  • Lipid Metabolism
  • Nuclear Envelope
  • Nuclear Proteins
  • RNA, Small Interfering
  • Sequence Homology