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First published online December 11, 2006
doi: 10.1242/10.1242/jcs.03303

Journal of Cell Science 119, 5031-5045 (2006)
Published by The Company of Biologists 2006
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When intracellular logistics fails - genetic defects in membrane trafficking

Vesa M. Olkkonen1,* and Elina Ikonen2

1 Department of Molecular Medicine, National Public Health Institute (KTL), Biomedicum, P.O.Box 104, FI-00251 Helsinki, Finland
2 Institute of Biomedicine/Anatomy, University of Helsinki, P.O. Box 63, FI-00014, Finland


Figure 1
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  		Fig. 1. Model for the role of HPS proteins in melanosome biogenesis. The lysosome-related organelle complexes 1, 2 and 3 (BLOC1-BLOC3) and their subunits are schematically illustrated. Solid arrows indicate cargo proteins being targeted to melanosomes and open arrows illustrate organelle maturation. BLOC1 is implicated in the targeting and fusion of trans-Golgi-network-derived vesicles with early-stage melanosomes; BLOC2 may mediate targeting/docking/fusion of vesicles with more mature melanosomes. Some proteins are transported to melanosomes via early endosomes through AP-3- and BLOC3-dependent processes. Components with identified disease mutations in both humans and mice are indicated by * and those with mouse mutations only by bullet. d, {delta}-subunit; m, µ3-subunit; s, {sigma}3-subunit; b3A, ß3A-subunit.

 

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  		Fig. 2. Rab27a regulates the localization and exocytosis of lysosome-related organelles in different cell types through distinct effector proteins. Mutations in Rab27a and its interaction partners cause several diseases characterized by defects in the subcellular distribution or exocytosis of lysosome-related organelles (A) Pigmentation defects involve mutations in Rab27a, myosin 5a or melanophilin, which bridges the former two proteins. This leads to disturbance of tethering and local movement of melanosomes at the distal actin-rich regions of the melanocyte. (B) Immunological deficits involve defects in Rab27a or its effector Munc13-4. The Rab27a defects disturb the targeting of secretory lysosomes of cytotoxic T-cells to the immunological synapse, whereas Munc13-4 defects apparently disturb the priming of lysosomes for fusion with the plasma membrane. The function of Munc13-4 is thought to be connected with that of the SNARE-based fusion machinery. Components with identified disease mutations are indicated by *.

 

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