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A correction to this article has been published: Wu et al., J. Cell Biol. 172 (4) 633
Published 24 October 2005. doi:10.1083/jcb.200503028
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 171, Number 2, 201-207
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Melanophilin and myosin Va track the microtubule plus end on EB1



Xufeng S. Wu, Grace L. Tsan, and John A. Hammer, III

Laboratory of Cell Biology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892

Correspondence to John A. Hammer: hammerj{at}nhlbi.nih.gov


Abstract

In mouse melanocytes, myosin Va is recruited onto the surface of melanosomes by a receptor complex containing Rab27a that is present in the melanosome membrane and melanophilin (Mlp), which links myosin Va to Rab27a. In this study, we show that Mlp is also a microtubule plus end–tracking protein or +TIP. Moreover, myosin Va tracks the plus end in a Mlp-dependent manner. Data showing that overexpression and short inhibitory RNA knockdown of the +TIP EB1 have opposite effects on Mlp–microtubule interaction, that Mlp interacts directly with EB1, and that deletion from Mlp of a region similar to one in the adenomatous polyposis coli protein involved in EB1 binding blocks Mlp's ability to plus end track argue that Mlp tracks the plus end directly by hitchhiking on EB1. These results identify a novel +TIP and indicate that vertebrate cells possess a +TIP complex that is similar to the Myo2p–Kar9p–Bim1p complex in yeast. We suggest that the +TIP complex identified in this study may serve to focus the transfer of melanosomes from microtubules to actin at the microtubule plus end.

Abbreviations used in this paper: APC, adenomatous polyposis coli protein; MBP, maltose-binding protein; Mlp, melanophilin; MTOC, microtubule-organizing center; RBD, Rab27a-binding domain; siEB1, short inhibitory RNA for EB1.


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