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Genetic studies suggest that these genes function in the same or overlapping pathways and are supported by biochemical studies showing that\n                    <jats:italic>d<\/jats:italic>\n                    encodes an actin-based melanosome transport motor, MyoVa, whereas\n                    <jats:italic>ash<\/jats:italic>\n                    encodes Rab27a, a protein that localizes to the melanosome and is postulated to serve as the MyoVa receptor. Here we show that\n                    <jats:italic>ln<\/jats:italic>\n                    encodes melanophilin (Mlph), a previously undescribed protein with homology to Rab effectors such as granuphilin, Slp3-a, and rabphilin-3A. Like all of these effectors, Mlph possesses two Zn\n                    <jats:sup>2+<\/jats:sup>\n                    -binding CX\n                    <jats:sub>2<\/jats:sub>\n                    CX\n                    <jats:sub>13,14<\/jats:sub>\n                    CX\n                    <jats:sub>2<\/jats:sub>\n                    C motifs and a short aromatic-rich amino acid region that is critical for Rab binding. However, Mlph does not contain the two Ca\n                    <jats:sup>2+<\/jats:sup>\n                    -binding C\n                    <jats:sub>2<\/jats:sub>\n                    domains found in these and other proteins involved in vesicle transport, suggesting that it represents a previously unrecognized class of Rab effectors. Collectively, our data show that Mlph is a critical component of the melanosome transport machinery and suggest that Mlph might function as part of a transport complex with Rab27a and MyoVa.\n                  <\/jats:p>","DOI":"10.1073\/pnas.181336698","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T10:45:09Z","timestamp":1027680309000},"page":"10238-10243","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":228,"title":["Mutations in\n                    <i>Mlph<\/i>\n                    , encoding a member of the Rab effector family, cause the melanosome transport defects observed in\n                    <i>leaden<\/i>\n                    mice"],"prefix":"10.1073","volume":"98","author":[{"given":"Lydia E.","family":"Matesic","sequence":"first","affiliation":[{"name":"Mouse Cancer Genetics Program, National Cancer Institute, Frederick, MD 21702"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Richard","family":"Yip","sequence":"additional","affiliation":[{"name":"Mouse Cancer Genetics Program, National Cancer Institute, Frederick, MD 21702"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andre\u00e9 E.","family":"Reuss","sequence":"additional","affiliation":[{"name":"Mouse Cancer Genetics Program, National Cancer Institute, Frederick, MD 21702"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Deborah A.","family":"Swing","sequence":"additional","affiliation":[{"name":"Mouse Cancer Genetics Program, National Cancer Institute, Frederick, MD 21702"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"T. 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