The LIS1-related NUDF Protein of Aspergillus nidulans Interacts with the Coiled-Coil Domain of the NUDE/RO11 Protein

doi:10.1083/jcb.150.3.681

Published online 7 August 2000. doi:10.1083/jcb.150.3.681

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© The Rockefeller University Press, 0021-9525/2000/8/681/ $5.00
The Journal of Cell Biology, Volume 150, Number 3, August 7, 2000 681-688

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The LIS1-related NUDF Protein of Aspergillus nidulans Interacts with the Coiled-Coil Domain of the NUDE/RO11 Protein

Vladimir P. Efimov^a and N. Ronald Morris^a
^a University of Medicine and Dentistry or New Jersey, Robert Wood Johnson Medical School, Department of Pharmacology, 675 Hoes Lane, Piscataway, New Jersey 08854-5635

Correspondence to: N. Ronald Morris, UMDNJ-Robert Wood Johnson Medical School, Department of Pharmacology, 675 Hoes Lane, Piscataway, NJ 08854-5635. Tel:(732) 235-4081 Fax:(732) 235-4073 E-mail:morrisnr{at}umdnj.edu.

The nudF gene of the filamentous fungus Aspergillus nidulansacts in the cytoplasmic dynein/dynactin pathway and is requiredfor distribution of nuclei. NUDF protein, the product of thenudF gene, displays 42% sequence identity with the human proteinLIS1 required for neuronal migration. Haploinsufficiency ofthe LIS1 gene causes a malformation of the human brain knownas lissencephaly. We screened for multicopy suppressors of amutation in the nudF gene. The product of the nudE gene isolatedin the screen, NUDE, is a homologue of the nuclear distributionprotein RO11 of Neurospora crassa. The highly conserved NH₂-terminalcoiled-coil domain of the NUDE protein suffices for proteinfunction when overexpressed. A similar coiled-coil domain ispresent in several putative human proteins and in the mitoticphosphoprotein 43 (MP43) of X. laevis. NUDF protein interactswith the Aspergillus NUDE coiled-coil in a yeast two-hybridsystem, while human LIS1 interacts with the human homologueof the NUDE/RO11 coiled-coil and also the Xenopus MP43 coiled-coil.In addition, NUDF coprecipitates with an epitope-tagged NUDE.The fact that NUDF and LIS1 interact with the same protein domainstrengthens the notion that these two proteins are functionallyrelated.

Key Words: dynein, dynactin, lissencephaly, nudF, LIS1

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