Letter abstract
Nature Cell Biology 6, 1195 - 1203 (2004)
Published online: 14 November 2004 | doi:10.1038/ncb1197
Rab27A-binding protein Slp2-a is required for peripheral melanosome distribution and elongated cell shape in melanocytes
Taruho S. Kuroda1,1 & Mitsunori Fukuda1
The synaptotagmin-like protein (Slp) family is implicated in regulating Rab27A-mediated membrane transport1, 2, 3, but how it might do this is unknown. Here we report that Slp2-a, a previously uncharacterized Rab27A-binding protein in melanocytes, controls melanosome distribution in the cell periphery and regulates the morphology of melanocytes. Slp2-a is the most abundantly expressed of the Slp- and Slac2-family proteins in melanocytes and colocalizes with Rab27A on melanosomes. Knockdown of endogenous Slp2-a protein by small-interfering RNAs (siRNAs) markedly reduced the number of melanosomes in the cell periphery of mouse melanocytes ('peripheral dilution'). Expression of siRNA-resistant Slp2-a (Slp2-aSR) rescued the peripheral dilution of melanosomes induced by Slp2-a siRNAs, but Slp2-aSR mutants, which failed to interact with either phospholipids or Rab27A, did not. Loss of Slp2-a protein also induced a change in melanocyte morphology, from their normal elongated shape to a more rounded shape, which depended on the phospholipid-binding activity of Slp2-a, but not on its Rab27A-binding activity. By contrast, knockdown of Slac2-a (also called melanophilin), another Rab27A-binding protein in melanocytes4, 5, caused perinuclear aggregation of melanosomes alone without altering cell shape. These results reveal the differential and sequential roles of Rab27A-binding proteins in melanosome transport in melanocytes.
- Fukuda Initiative Research Unit, RIKEN (The Institute of Physical and Chemical Research), 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.
Correspondence to: Mitsunori Fukuda1 e-mail: mnfukuda@brain.riken.go.jp
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