Functional analysis of Slac2-a/melanophilin as a linker protein between Rab27A and myosin Va in melanosome transport

Taruho S. Kuroda, Takashi Itoh, Mitsunori Fukuda

Research output: Contribution to journalReview articlepeer-review

24 Citations (Scopus)

Abstract

Slac2-a/melanophilin regulates melanosome transport in mammalian skin melanocytes by linking melanosome-bound Rab27A and an actin-based motor protein, myosin Va. Slac2-a consists of an N-terminal Slp homology domain (SHD), which has been identified as a specific GTP-Rab27-binding domain, a myosin Va-binding domain (MBD) in the middle region, and an actin-binding domain (ABD) at the C-terminus. Mutations in the slac2-a/mlph gene cause the abnormal pigmentation (i.e., perinuclear melanosome aggregation in melanocytes) in human Griscelli syndrome type III and in leaden mice because of the inability to form the tripartite protein complex consisting of Rab27A, Slac2-a, and myosin Va. In this chapter we describe the methods, including in vivo melanosome distribution assay combined with dominant-negative approaches and RNA interference technology, that have been used to analyze the function of Slac2-a in melanosome transport in melanocytes.

Original languageEnglish
Article number37
Pages (from-to)419-431
Number of pages13
JournalMethods in enzymology
Volume403
DOIs
Publication statusPublished - 2005
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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