Correction
for
Wu et al., J. Cell Biol. 171 (2) 201-207.
Published 13 February 2006. doi:10.1083/jcb.20050302820060126c
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 172, Number 4, 633-633
Xufeng S. Wu,
Grace L. Tsan, and
John A. Hammer, III
Vol. 171, No. 2, October 24, 2005. Pages 201207.
In the right column, fourth line of the abstract, the word "indirectly" mistakenly appeared as "directly." The corrected abstract appears below with the corrected word in bold.
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 endtracking 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 Mlpmicrotubule 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 indirectly by hitchhiking on EB1. These results identify a novel +TIP and indicate that vertebrate cells possess a +TIP complex that is similar to the Myo2pKar9pBim1p 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.

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