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Volume 34 Issue 8
Aug.  2007
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Article Contents

The BLOC Interactomes Form a Network in Endosomal Transport

doi: 10.1016/S1673-8527(07)60076-9
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  • Corresponding author: E-mail address: wli@genetics.ac.cn (Wei Li)
  • Received Date: 2007-06-25
  • Accepted Date: 2007-06-27
  • Available Online: 2007-08-21
  • Publish Date: 2007-08-20
  • With the identification of more than a dozen novel Hermansky-Pudlak Syndrome (HPS) proteins in vesicle trafficking in higher eukaryotes, a new class of trafficking pathways has been described. It mainly consists of three newly-defined protein complexes, BLOC-1, -2, and -3. Compelling evidence indicates that these complexes together with two other well-known complexes, AP3 and HOPS, play important roles in endosomal transport. The interactions between these complexes form a network in protein traffickingvia endosomes and cytoskeleton. Each node of this network has intra-complex and extra-complex interactions. These complexes are connected by direct interactions between the subunits from different complexes or by indirect interactions through coupling nodes that interact with two or more subunits from different complexes. The dissection of this network facilitates the understanding of a dynamic but elaborate transport machinery in protein/membrane trafficking. The disruption of this network may lead to abnormal trafficking or defective organellar development as described in patients with Hermansky-Pudlak syndrome.
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  • [1]
    Bonifacino, JS, Glick, et al. The mechanisms of vesicle budding and fusion Cell, 116 (2004),pp. 153-166
    [2]
    Hermansky, F, Pudlak, et al. Albinism associated with hemorrhagic diathesis and unusual pigmented reticular cells in the bone marrow: report of two cases with histochemical studies Blood, 14 (1959),pp. 162-169
    [3]
    Huizing, M, Gahl, et al. Disorders of vesicles of lysosome lineage: the Hermansky-Pudlak syndromes Curr Mol Med, 2 (2002),pp. 451-467
    [4]
    Dell'Angelica, EC, Mullins, et al. Lysosome-related organelles FASEB J, 14 (2000),pp. 1265-1278
    [5]
    Bonifacino, JS Insights into the biogenesis of lysosome-related organelles from the study of the Hermansky-Pudlak syndrome Ann NY Acad Sci, 1038 (2004),pp. 103-114
    [6]
    Wei, ML Hermansky-Pudlak syndrome: a disease of protein trafficking and organelle function Pigment Cell Res, 19 (2006),pp. 19-42
    [7]
    Swank, RT, Novak, et al. Mouse models of Hermansky-Pudlak syndrome: a review Pigment Cell Res, 11 (1998),pp. 60-80
    [8]
    Li, W, Rusiniak, et al. Murine Hermansky-Pudlak syndrome: Genes which control lysosome-related organelles BioEssays, 26 (2004),pp. 616-628
    [9]
    Li, W, He, et al. Mutational data integration in gene-oriented files of Hermansky-Pudlak syndrome Hum Mutat, 27 (2006),pp. 402-407
    [10]
    Chintala, S, Li, et al. Proc Natl Acad Sci USA, 102 (2005),pp. 10964-10969
    [11]
    Wilson, SM, Yip, et al. Proc Natl Acad Sci USA, 97 (2000),pp. 7933-7938
    [12]
    Chintala, S, Tan, et al. Blood, 109 (2007),pp. 1533-1540
    [13]
    Dell'Angelica, EC The building BLOC(k)s of lysosomes and related organelles Curr Opin Cell Biol, 16 (2004),pp. 458-464
    [14]
    Falcon-Perez, JM, Starcevic, et al. BLOC-1, a novel complex containing the pallidin and muted proteins involved in the biogenesis of melanosomes and platelet-dense granules J Biol Chem, 277 (2002),pp. 28191-28199
    [15]
    Moriyama, K, Bonifacino, et al. Pallidin is a component of a multi-protein complex involved in the biogenesis of lysosome-related organelles Traffic, 3 (2002),pp. 666-677
    [16]
    Ciciotte, SL, Gwynn, et al. Cappuccino, a mouse model of Hermansky-Pudlak syndrome, encodes a novel protein that is part of the pallidin-muted complex (BLOC-1) Blood, 101 (2003),pp. 4402-4407
    [17]
    Li, W, Zhang, et al. Hermansky-Pudlak syndrome type 7 (HPS-7) results from mutant dysbindin, a member of the biogenesis of lysosome-related organelles complex 1 (BLOC-1) Nat Genet, 35 (2003),pp. 84-89
    [18]
    Starcevic, M, Dell'Angelica, et al. Identification of snapin and three novel proteins (BLOS1, BLOS2, and BLOS3/reduced pigmentation) as subunits of biogenesis of lysosome-related organelles complex-1 (BLOC-1) J Biol Chem, 279 (2004),pp. 28393-28401
    [19]
    Gwynn, B, Martina, et al. Reduced pigmentation (rp), a mouse model of Hermansky-Pudlak syndrome, encodes a novel component of the BLOC-1 complex Blood, 104 (2004),pp. 3181-3189
    [20]
    Zhang, Q, Zhao, et al. Ru2 and Ru encode mouse orthologs of the genes mutated in human Hermansky-Pudlak syndrome types 5 and 6 Nat Genet, 33 (2003),pp. 145-154
    [21]
    Gautum, R, Chintala, et al. The Hermansky-Pudlak syndrome 3 (cocoa) protein is a component of the biogenesis of lysosome-related organelle complex 2 (BLOC-2) J Biol Chem, 279 (2004),pp. 12935-12942
    [22]
    Di Pietro, SM, Falcon-Perez, et al. Characterization of BLOC-2, a complex containing the Hermansky-Pudlak syndrome proteins HPS3, HPS5 and HPS6 Traffic, 5 (2004),pp. 276-283
    [23]
    Suzuki, T, Li, et al. Hermansky-Pudlak syndrome is caused by mutations in HPS4, the human homolog of the mouse light-ear gene Nat Genet, 30 (2002),pp. 321-324
    [24]
    Chiang, PW, Oiso, et al. The Hermansky-Pudlak syndrome 1 (HPS1) and HPS4 proteins are components of two complexes, BLOC-3 and BLOC-4, involved in the biogenesis of lysosome-related organelles J Biol Chem, 278 (2003),pp. 20332-20337
    [25]
    Martina, JA, Moriyama, et al. BLOC-3, a protein complex containing the Hermansky-Pudlak syndrome gene products HPS1 and HPS4 J Biol Chem, 278 (2003),pp. 9376-9384
    [26]
    Nazarian, R, Falcon-Perez, et al. Biogenesis of lysosome-related organelles complex 3 (BLOC-3): a complex containing the Hermansky-Pudlak syndrome (HPS) proteins HPS1 and HPS4 Proc Natl Acad Sci USA, 100 (2003),pp. 8770-8775
    [27]
    Di Pietro, SM, Falcon-Perez, et al. BLOC-1 interacts with BLOC-2 and the AP-3 complex to facilitate protein trafficking on endosomes Mol Biol Cell, 17 (2006),pp. 4027-4038
    [28]
    Salazar, G, Craige, et al. BLOC-1 complex deficiency alters the targeting of adaptor protein complex-3 cargoes Mol Biol Cell, 17 (2006),pp. 4014-4026
    [29]
    Setty, SR, Tenza, et al. BLOC-1 is required for cargo-specific sorting from vacuolar early endosomes toward lysosome-related organelles Mol Biol Cell, 18 (2007),pp. 768-780
    [30]
    Huang, L, Kuo, et al. The pallid gene encodes a novel syntaxin 13-interacting protein involved in platelet storage pool deficiency Nat Genet, 14 (1999),pp. 300-306
    [31]
    Zhang, Q, Li, et al. The gene for the muted (mu) mouse, a model for Hermansky-Pudlak syndrome, defines a novel protein which regulates vesicle trafficking Hum Mol Genet, 11 (2002),pp. 697-706
    [32]
    Vites, O, Rhee, et al. Reinvestigation of the role of snapin in neurotransmitter release J Biol Chem, 279 (2004),pp. 26251-26256
    [33]
    Burkhard, P, Stetefeld, et al. Coiled coils: a highly versatile protein folding motif Trends Cell Biol, 11 (2001),pp. 82-88
    [34]
    Nazarian, R, Starcevic, et al. Reinvestigation of the dysbindin subunit of BLOC-1 (biogenesis of lysosome-related organelles complex-1) as a dystrobrevinbinding protein Biochem J, 395 (2006),pp. 587-598
    [35]
    Ungar, D, Oka, et al. Subunit architecture of the conserved oligomeric Golgi complex J Biol Chem, 280 (2005),pp. 32729-32735
    [36]
    Benson, MA, Newey, et al. Dysbindin, a novel coiled-coil-containing protein that interacts with the dystrobrevins in muscle and brain J Biol Chem, 276 (2001),pp. 24232-24241
    [37]
    Benson, MA, Tinsley, et al. Myospryn is a novel binding partner for dysbindin in muscle J Biol Chem, 279 (2004),pp. 10450-10458
    [38]
    Numakawa, T, Yagasaki, et al. Evidence of novel neuronal functions of dysbindin, a susceptibility gene for schizophrenia Hum Mol Genet, 13 (2004),pp. 2699-2708
    [39]
    Kumamoto, N, Matsuzaki, et al. Hyperactivation of midbrain dopaminergic system in schizophrenia could be attributed to the down-regulation of dysbindin Biochem Biophys Res Commun, 345 (2006),pp. 904-909
    [40]
    Straub, RE, Jiang, et al. Am J Hum Genet, 71 (2002),pp. 337-348
    [41]
    Ilardi, JM, Mochida, et al. Snapin: a SNARE associated protein implicated in synaptic transmission Nat Neurosci, 2 (1999),pp. 119-124
    [42]
    Tian, JH, Wu, et al. The role of Snapin in neurosecretion: snapin knock-out mice exhibit impaired calcium-dependent exocytosis of large dense-core vesicles in chromaffin cells J Neurosci, 25 (2005),pp. 10546-10555
    [43]
    Chheda, MG, Ashery, et al. Phosphorylation of Snapin by PKA modulates its interaction with the SNARE complex Nat Cell Biol, 3 (2001),pp. 331-338
    [44]
    Hong, WJ SNAREs and traffic Biochim Biophys Acta, 1744 (2005),pp. 120-144
    [45]
    Buxton, P, Zhang, et al. Identification and characterization of snapin as a ubiquitously expressed SNARE-binding protein that interacts with SNAP23 in non-neuronal cells Biochem J, 375 (2003),pp. 433-440
    [46]
    Morenilla-Palao, C, Planells-Cases, et al. Regulated exocytosis contributes to protein kinase C potentiation of vanilloid receptor activity J Biol Chem, 279 (2004),pp. 25665-25672
    [47]
    Fukui, K, Yang, et al. The HNF-1 target collectrin controls insulin exocytosis by SNARE complex formation Cell Metab, 2 (2005),pp. 373-384
    [48]
    Ruder, C, Reimer, et al. EBAG9 adds a new layer of control on large dense-core vesicle exocytosis via interaction with Snapin Mol Biol Cell, 16 (2005),pp. 1245-1257
    [49]
    Chen, M, Lucas, et al. A novel role for snapin in dendrite patterning: interaction with cypin Mol Biol Cell, 16 (2005),pp. 5103-5114
    [50]
    Zissimopoulos, S, West, et al. Ryanodine receptor interaction with the SNARE-associated protein snapin J Cell Sci, 119 (2006),pp. 2386-2397
    [51]
    Krapivinsky, G, Mochida, et al. The TRPM7 ion channel functions in cholinergic synaptic vesicles and affects transmitter release Neuron, 52 (2006),pp. 485-496
    [52]
    Wolff, S, Stoter, et al. Casein kinase 1 delta (CK1delta) interacts with the SNARE associated protein snapin FEBS Lett, 580 (2006),pp. 6477-6484
    [53]
    Hunt, RA, Edris, et al. Snapin interacts with the N-terminus of regulator of G protein signaling 7 Biochem Biophys Res Commun, 303 (2003),pp. 594-599
    [54]
    Chou, JL, Huang, et al. Regulation of type VI adenylyl cyclase by Snapin, a SNAP25-binding protein J Biol Chem, 279 (2004),pp. 46271-46279
    [55]
    Schaaf, CP, Benzing, et al. Novel interaction partners of the TPR/MET tyrosine kinase FASEB J, 19 (2005),pp. 267-269
    [56]
    Yuan, X, Shan, et al. Interaction between Snapin and G-CSF receptor Cytokine, 33 (2006),pp. 219-225
    [57]
    Yin, H, Laguna, et al. Dysbindin structural homologue CK1BP is an isoform-selective binding partner of human casein kinase-1 Biochemistry, 45 (2006),pp. 5297-5308
    [58]
    McBride, HM, Rybin, et al. Oligomeric complexes link Rab5 effectors with NSF and drive membrane fusion via interactions between EEA1 and Syntaxin 13 Cell, 98 (1999),pp. 377-386
    [59]
    Richardson, SC, Winistorfer, et al. Mammalian late Vps orthologues participate in early endosomal fusion and interact with the cytoskeleton Mol Biol Cell, 15 (2004),pp. 1197-1210
    [60]
    Thakur, P, Stevens, et al. Effects of PKA-mediated phosphorylation of snapin on synaptic transmission in cultured hippocampal neurons J Neurosci, 24 (2004),pp. 6476-6481
    [61]
    Di Pietro, SM, Dell'Angelica, et al. The cell biology of Hermansky-Pudlak syndrome: recent advances Traffic, 6 (2005),pp. 525-533
    [62]
    Falcon-Perez, JM, Romero-Calderon, et al. The drosophila pigment gene pink (p) encodes a human homologue of Hermansky-Pudlak syndrome 5 (HPS5) Traffic, 8 (2007),pp. 154-168
    [63]
    Lafer, EM Clathrin-protein interactions Traffic, 3 (2002),pp. 513-520
    [64]
    Helip-Wooley, A, Westbroek, et al. Association of the Hermansky-Pudlak syndrome type-3 protein with clathrin BMC Cell Biol, 6 (2005),p. 33
    [65]
    Chiang, PW, Bennett, et al. BLOC3 affects the cytoskeleton of the secretory pathway Pigment Cell Res, 18 (2005)
    [66]
    Gautum, R, Novak, et al. Interaction of Hermansky-Pudlak Syndrome genes in the regulation of lysosome-related organelles Traffic, 7 (2006),pp. 779-792
    [67]
    Feng, L, Novak, et al. The Hermansky-Pudlak syndrome 1 (HPS1) and HPS2 genes independently contribute to the production and function of platelet dense granules, melanosomes, and lysosomes Blood, 99 (2002),pp. 1651-1658
    [68]
    Richmond, B, Huizing, et al. Melanocytes derived from patients with Hermansky-Pudlak Syndrome types 1, 2, and 3 have distinct defects in cargo trafficking J Invest Dermatol, 124 (2005),pp. 420-427
    [69]
    Oh, J, Liu, et al. The Hermansky-Pudlak syndrome (HPS) protein is part of a high molecular weight complex involved in biogenesis of early melanosomes Hum Mol Genet, 9 (2000),pp. 375-385
    [70]
    Falcon-Perez, JM, Nazarian, et al. Distribution and dynamics of Lamp1-containing endocytic organelles in fibroblasts deficient in BLOC-3 J Cell Sci, 118 (2005),pp. 5243-5255
    [71]
    Peden, AA, Oorschot, et al. Localization of the AP-3 adaptor complex defines a novel endosomal exit site for lysosomal membrane proteins J Cell Biol, 164 (2004),pp. 1065-1076
    [72]
    Huizing, M, Sarangarajan, et al. AP-3 mediates tyrosinase but not TRP-1 trafficking in human melanocytes Mol Biol Cell, 12 (2001),pp. 2075-2085
    [73]
    Nguyen, T, Novak, et al. Melanosome morphologies in murine models of Hermansky-Pudlak syndrome reflect blocks in organelle development J Invest Dermatol, 119 (2002),pp. 1156-1164
    [74]
    Borner, GH, Harbour, et al. Comparative proteomics of clathrin-coated vesicles J Cell Biol, 175 (2006),pp. 571-578
    [75]
    Rehling, P, Darsow, et al. Formation of AP-3 transport intermediates requires Vps41 function Nat Cell Biol, 6 (1999),pp. 346-353
    [76]
    Kaleeba, JA, Berger, et al. Kaposi's sarcoma-associated herpesvirus fusion-entry receptor: cystine transporter xCT Science, 311 (2006),pp. 1921-1924
    [77]
    Seong, E, Wainer, et al. Genetic analysis of the neuronal and ubiquitous AP-3 adaptor complexes reveals divergent functions in brain Mol Biol Cell, 16 (2005),pp. 128-140
    [78]
    Uetz, P, From protein networks to biological systems FEBS Lett, 579 (2005),pp. 1821-1827
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