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© The Rockefeller University Press, 0021-9525/1999//469 $5.00
The Journal of Cell Biology, Volume 145, Number 3, , 1999 469-479

Novel Dendritic Kinesin Sorting Identified by Different Process Targeting of Two Related Kinesins: KIF21A and KIF21B

Joseph R. Marszalek^*,, Joshua A. Weiner, Samuel J. Farlow, Jerold Chun^*,, and Lawrence S.B. Goldstein^*,

^* Biomedical Sciences Graduate Program; Neurosciences Graduate Program; and Howard Hughes Medical Institute, Division of Cellular and Molecular Medicine, Department of Pharmacology, University of California San Diego, La Jolla, California 92093-0683

Neurons use kinesin and dynein microtubule-dependent motor proteins to transport essential cellular components along axonal and dendritic microtubules. In a search for new kinesin-like proteins, we identified two neuronally enriched mouse kinesins that provide insight into a unique intracellular kinesin targeting mechanism in neurons. KIF21A and KIF21B share colinear amino acid similarity to each other, but not to any previously identified kinesins outside of the motor domain. Each protein also contains a domain of seven WD-40 repeats, which may be involved in binding to cargoes. Despite the amino acid sequence similarity between KIF21A and KIF21B, these proteins localize differently to dendrites and axons. KIF21A protein is localized throughout neurons, while KIF21B protein is highly enriched in dendrites. The plus end-directed motor activity of KIF21B and its enrichment in dendrites indicate that models suggesting that minus end-directed motor activity is sufficient for dendrite specific motor localization are inadequate. We suggest that a novel kinesin sorting mechanism is used by neurons to localize KIF21B protein to dendrites since its mRNA is restricted to the cell body.

Key Words: kinesin • protein sorting • WD-40 repeats • neuron transport • dendrite

Abbreviations used in this paper: KLPs, kinesin-like proteins; nt, nucleotide; pNF-H, phosphorylated neurofilament H.

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