Lamin-dependent localization of UNC-84, a protein required for nuclear migration in Caenorhabditis elegans

Mol Biol Cell. 2002 Mar;13(3):892-901. doi: 10.1091/mbc.01-06-0294.

Abstract

Mutations in the Caenorhabditis elegans unc-84 gene cause defects in nuclear migration and anchoring. We show that endogenous UNC-84 protein colocalizes with Ce-lamin at the nuclear envelope and that the envelope localization of UNC-84 requires Ce-lamin. We also show that during mitosis, UNC-84 remains at the nuclear periphery until late anaphase, similar to known inner nuclear membrane proteins. UNC-84 protein is first detected at the 26-cell stage and thereafter is present in most cells during development and in adults. UNC-84 is properly expressed in unc-83 and anc-1 lines, which have phenotypes similar to unc-84, suggesting that neither the expression nor nuclear envelope localization of UNC-84 depends on UNC-83 or ANC-1 proteins. The envelope localization of Ce-lamin, Ce-emerin, Ce-MAN1, and nucleoporins are unaffected by the loss of UNC-84. UNC-84 is not required for centrosome attachment to the nucleus because centrosomes are localized normally in unc-84 hyp7 cells despite a nuclear migration defect. Models for UNC-84 localization are discussed.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Caenorhabditis elegans / cytology
  • Caenorhabditis elegans / embryology*
  • Caenorhabditis elegans / genetics
  • Caenorhabditis elegans / metabolism
  • Caenorhabditis elegans Proteins*
  • Centrosome / metabolism
  • Gene Expression Regulation, Developmental
  • Helminth Proteins / metabolism
  • Lamins / metabolism*
  • Membrane Glycoproteins / genetics
  • Membrane Glycoproteins / metabolism*
  • Membrane Proteins / metabolism
  • Mitosis / physiology
  • Models, Biological
  • Nuclear Envelope / metabolism*
  • Nuclear Pore Complex Proteins / metabolism
  • Nuclear Proteins / genetics
  • Nuclear Proteins / metabolism*
  • Recombinant Fusion Proteins / metabolism
  • Thymopoietins / metabolism

Substances

  • Caenorhabditis elegans Proteins
  • Helminth Proteins
  • Lamins
  • Membrane Glycoproteins
  • Membrane Proteins
  • Nuclear Pore Complex Proteins
  • Nuclear Proteins
  • Recombinant Fusion Proteins
  • Thymopoietins
  • Unc-84 protein, C elegans
  • emerin
  • lem-2 protein, C elegans