Sabine Bardin

Thank you for your interest in spreading the word about bioRxiv. NOTE: Your email address is requested solely to identify you as the sender of this article. Your Email * Your Name * Send To * Enter multiple addresses on separate lines or separate them with commas. Message Subject (Your Name) has forwarded a page to you from bioRxiv Message Body (Your Name) thought you would like to see this page from the bioRxiv website.

We have previously shown that RAB6 and Myosin II are implicated in the fission of RAB6-positive transport carriers at the Golgi complex6. The inhibition of this process leads to the formation of long membrane tubes connected to the Golgi complex6. Detailed analysis of time-lapse microscopy of HeLa cells stably expressing GFP-RAB6 (Supplementary Fig. 1, Supplementary Movie 1) now revealed that RAB6-positive vesicles exit the Golgi complex in defined areas (Fig. 1a, Supplementary Fig.

Ubiquitously expressed RAB6 GTPases exist in two alternatively spliced isoforms (RAB6A and RAB6A?, henceforward RAB6) that share numerous effectors and only differ by three amino acids21. We first investigated the subcellular localization of RAB6 in melanoma cells (human melanocytic MNT-1 cell line—a well-defined system to study melanosome biology22,23), as well as in primary human and mouse melanocytes (NHEM: Normal Human Epidermal Melanocytes; NMM: Normal Mouse Melanocytes).