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© The Rockefeller University Press, 0021-9525/1999//507 $5.00
The Journal of Cell Biology, Volume 147, Number 3, , 1999 507-518

Original Article

Kinesin-II Is Required for Axonal Transport of Choline Acetyltransferase in Drosophila



Krishanu Raya, Sharon E. Perezb, Zhaohuai Yanga, Jenny Xua, Bruce W. Ritchingsa, Hermann Stellerb, and Lawrence S.B. Goldsteina

a Howard Hughes Medical Institute, Department of Cellular and Molecular Medicine, Department of Pharmacology, University of California, San Diego, La Jolla, California 92093-0683
b Howard Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139
Howard Hughes Medical Institute/CMMW, Rm. 334, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0683.(858) 534-9701(858) 534-9702

lgoldstein{at}ucsd.edu

KLP64D and KLP68D are members of the kinesin-II family of proteins in Drosophila. Immunostaining for KLP68D and ribonucleic acid in situ hybridization for KLP64D demonstrated their preferential expression in cholinergic neurons. KLP68D was also found to accumulate in cholinergic neurons in axonal obstructions caused by the loss of kinesin light chain. Mutations in the KLP64D gene cause uncoordinated sluggish movement and death, and reduce transport of choline acetyltransferase from cell bodies to the synapse. The inviability of KLP64D mutations can be rescued by expression of mammalian KIF3A. Together, these data suggest that kinesin-II is required for the axonal transport of a soluble enzyme, choline acetyltransferase, in a specific subset of neurons in Drosophila. Furthermore, the data lead to the conclusion that the cargo transport requirements of different classes of neurons may lead to upregulation of specific pathways of axonal transport.

Key Words: Drosophila • kinesin-like proteins • axonal transport • microtubule motors • neurobiology

© 1999 The Rockefeller University Press

1.used in this paper: aa, amino acid(s); ChAT, choline acetyltransferase; CNS, central nervous system; CSP, cysteine string protein; EMS, ethyl methanesulphonate; KHC, kinesin heavy chain; nAChR, nicotinic acetylcholine receptor(s); PNS, peripheral nervous system; SYT, synaptotagmin

S. Perez's present address is Division of Biology, California Institute of Technology, Pasadena, CA 91125.


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