Mitochondrial Association of a Plus End–Directed Microtubule Motor Expressed during Mitosis in Drosophila

Pereira, Andrea J.; Dalby, Brian; Stewart, Russell J.; Doxsey, Stephen J.; Goldstein, Lawrence S.B.

doi:10.1083/jcb.136.5.1081

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Article| March 10 1997

Mitochondrial Association of a Plus End–Directed Microtubule Motor Expressed during Mitosis in Drosophila

Andrea J. Pereira,

Andrea J. Pereira

*Howard Hughes Medical Institute, Division of Cellular and Molecular Medicine, Department of Pharmacology, University of California at San Diego, La Jolla, California 92093-0683; ‡Program in Molecular Medicine, University of Massachusetts Medical Center, Worcester, Massachusetts 01605; and §University of Utah, Department of Bioengineering, Salt Lake City, Utah 84112

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Brian Dalby,

Brian Dalby

*Howard Hughes Medical Institute, Division of Cellular and Molecular Medicine, Department of Pharmacology, University of California at San Diego, La Jolla, California 92093-0683; ‡Program in Molecular Medicine, University of Massachusetts Medical Center, Worcester, Massachusetts 01605; and §University of Utah, Department of Bioengineering, Salt Lake City, Utah 84112

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Russell J. Stewart,

Russell J. Stewart

*Howard Hughes Medical Institute, Division of Cellular and Molecular Medicine, Department of Pharmacology, University of California at San Diego, La Jolla, California 92093-0683; ‡Program in Molecular Medicine, University of Massachusetts Medical Center, Worcester, Massachusetts 01605; and §University of Utah, Department of Bioengineering, Salt Lake City, Utah 84112

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Stephen J. Doxsey,

Stephen J. Doxsey

*Howard Hughes Medical Institute, Division of Cellular and Molecular Medicine, Department of Pharmacology, University of California at San Diego, La Jolla, California 92093-0683; ‡Program in Molecular Medicine, University of Massachusetts Medical Center, Worcester, Massachusetts 01605; and §University of Utah, Department of Bioengineering, Salt Lake City, Utah 84112

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Lawrence S.B. Goldstein

*Howard Hughes Medical Institute, Division of Cellular and Molecular Medicine, Department of Pharmacology, University of California at San Diego, La Jolla, California 92093-0683; ‡Program in Molecular Medicine, University of Massachusetts Medical Center, Worcester, Massachusetts 01605; and §University of Utah, Department of Bioengineering, Salt Lake City, Utah 84112

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Author and Article Information

Andrea J. Pereira

*Howard Hughes Medical Institute, Division of Cellular and Molecular Medicine, Department of Pharmacology, University of California at San Diego, La Jolla, California 92093-0683; ‡Program in Molecular Medicine, University of Massachusetts Medical Center, Worcester, Massachusetts 01605; and §University of Utah, Department of Bioengineering, Salt Lake City, Utah 84112

Brian Dalby

*Howard Hughes Medical Institute, Division of Cellular and Molecular Medicine, Department of Pharmacology, University of California at San Diego, La Jolla, California 92093-0683; ‡Program in Molecular Medicine, University of Massachusetts Medical Center, Worcester, Massachusetts 01605; and §University of Utah, Department of Bioengineering, Salt Lake City, Utah 84112

Russell J. Stewart

*Howard Hughes Medical Institute, Division of Cellular and Molecular Medicine, Department of Pharmacology, University of California at San Diego, La Jolla, California 92093-0683; ‡Program in Molecular Medicine, University of Massachusetts Medical Center, Worcester, Massachusetts 01605; and §University of Utah, Department of Bioengineering, Salt Lake City, Utah 84112

Stephen J. Doxsey

*Howard Hughes Medical Institute, Division of Cellular and Molecular Medicine, Department of Pharmacology, University of California at San Diego, La Jolla, California 92093-0683; ‡Program in Molecular Medicine, University of Massachusetts Medical Center, Worcester, Massachusetts 01605; and §University of Utah, Department of Bioengineering, Salt Lake City, Utah 84112

Lawrence S.B. Goldstein

*Howard Hughes Medical Institute, Division of Cellular and Molecular Medicine, Department of Pharmacology, University of California at San Diego, La Jolla, California 92093-0683; ‡Program in Molecular Medicine, University of Massachusetts Medical Center, Worcester, Massachusetts 01605; and §University of Utah, Department of Bioengineering, Salt Lake City, Utah 84112

A.J. Pereira would like to express her gratitude to William S. Gelbart of Harvard University (Cambridge, MA) in whose lab she did a large part of the work reported. She would like to thank Nicholas Lim (Harvard University) for technical assistance, Aruna Purohit (University of Massachusetts, Worcester), Jason Dictenberg (University of Massachusetts, Worcester), Tim Karr (University of Chicago), and Paul Dobner (University of Massachusetts, Worcester) for scientific discussion and advice, and also Kristin White (Brandeis University, Boston, MA) for the use of her confocal microscope and Fuji printer. A.J. Pereira would also like to thank Rafael Garesse (Universidad Autonoma de Madrid, Spain) for an aliquot of anti-Drosophila mitochondrial ATP synthase antisera.

Address all correspondence to L.S.B. Goldstein, HHMI/CMMW RM. 334, University of California at San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0683. Tel.: (619) 534-9702. Fax: (619) 534-9701.

Received: June 10 1996

Revision Received: November 12 1996

Online ISSN: 1540-8140

Print ISSN: 0021-9525

1997

J Cell Biol (1997) 136 (5): 1081–1090.

https://doi.org/10.1083/jcb.136.5.1081

The kinesin superfamily is a large group of proteins (kinesin-like proteins [KLPs]) that share sequence similarity with the microtubule (MT) motor kinesin. Several members of this superfamily have been implicated in various stages of mitosis and meiosis. Here we report our studies on KLP67A of Drosophila. DNA sequence analysis of KLP67A predicts an MT motor protein with an amino-terminal motor domain. To prove this directly, KLP67A expressed in Escherichia coli was shown in an in vitro motility assay to move MTs in the plus direction. We also report expression analyses at both the mRNA and protein level, which implicate KLP67A in the localization of mitochondria in undifferentiated cell types. In situ hybridization studies of the KLP67A mRNA during embryogenesis and larval central nervous system development indicate a proliferation-specific expression pattern. Furthermore, when affinity-purified anti-KLP67A antisera are used to stain blastoderm embryos, mitochondria in the region of the spindle asters are labeled. These data suggest that KLP67A is a mitotic motor of Drosophila that may have the unique role of positioning mitochondria near the spindle.

1997

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