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Vol. 13, Issue 5, 1735-1749, May 2002
Laboratories of Cell Biology and Molecular Cardiology, National
Heart, Lung, and Blood Institute, National Institutes of Health,
Bethesda, Maryland 20892
Melanocytes that lack the GTPase Rab27a (ashen) are
disabled in myosin Va-dependent melanosome capture because the
association of the myosin with the melanosome surface depends on the
presence of this resident melanosomal membrane protein. One
interpretation of these observations is that Rab27a functions wholly or
in part as the melanosome receptor for myosin Va (Myo5a). Herein, we
show that the ability of the myosin Va tail domain to localize to the melanosome and generate a myosin Va null (dilute)
phenotype in wild-type melanocytes is absolutely dependent on the
presence of exon F, one of two alternatively spliced exons present in
the tail of the melanocyte-spliced isoform of myosin Va but not the brain-spliced isoform. Exon D, the other melanocyte-specific tail exon,
is not required. Similarly, the ability of full-length myosin Va to
colocalize with melanosomes and to rescue their distribution in
dilute melanocytes requires exon F but not exon D. These
results predict that an interaction between myosin Va and Rab27a should be exon F dependent. Consistent with this, Rab27a present in detergent lysates of melanocytes binds to beads coated with purified, full-length melanocyte myosin Va and melanocyte myosin Va lacking exon D, but not
to beads coated with melanocyte myosin Va lacking exon F or brain
myosin Va. Moreover, the preparation of melanocyte lysates in the
presence of GDP rather than
guanosine-5'-O-(3-thio)triphosphate reduces the
amount of Rab27a bound to melanocyte myosin Va-coated beads by
approximately fourfold. Finally, pure Rab27a does not bind to myosin
Va-coated beads, suggesting that these two proteins interact
indirectly. Together, these results argue that Rab27a is an essential
component of a protein complex that serves as the melanosome receptor
for myosin Va, suggest that this complex contains at least one
additional protein capable of bridging the indirect interaction between
Rab27a and myosin Va, and imply that the recruitment of myosin Va to
the melanosome surface in vivo should be regulated by factors
controlling the nucleotide state of Rab27a.
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