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A more recent version of this article appeared on March 1, 2002
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Submitted on June 18, 2001
Revised on October 31, 2001
Accepted on November 29, 2001
1 Department of Cell Biology, The Johns Hopkins University School of Medicine, 725 N. Wolfe Street, Baltimore MD 21205
2 Howard Hughes Medical Institute and Department of MCD Biology, The University of Colorado, Boulder, CO 80309
3 Department of Genetics, The Institute of Life Sciences, The Hebrew University of Jerusalem, Jerusalem 91904 Israel
4 Department of Embryology, Carnegie Institute of Washington, 115 West University Parkway, Baltimore MD 21210
* Corresponding author. E-mail address: gru{at}vms.huji.ac.il.
Mutations in the C. elegans unc-84 gene cause defects in nuclear migration and anchoring. We show that endogenous UNC-84 protein co-localizes 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.
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