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Volumn 214, Issue 6, 2009, Pages 403-421

Protein trafficking in immune cells

Author keywords

Endocytosis; Exocytosis; GTPase; Immune cells; Mast cells; Sorting; Synaptotagmin

Indexed keywords

ADAPTOR PROTEIN; CARRIER PROTEIN; COAT PROTEIN; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE TRIPHOSPHATASE; RAB27 PROTEIN; SNARE PROTEIN; SYNAPTOTAGMIN; UNCLASSIFIED DRUG;

EID: 64649102533     PISSN: 01712985     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.imbio.2008.12.008     Document Type: Article
Times cited : (15)

References (175)
  • 1
    • 0033519624 scopus 로고    scopus 로고
    • O-linked glycans mediate apical sorting of human intestinal sucrase-isomaltase through association with lipid rafts
    • Alfalah M., Jacob R., Preuss U., Zimmer K.P., Naim H., and Naim H.Y. O-linked glycans mediate apical sorting of human intestinal sucrase-isomaltase through association with lipid rafts. Curr. Biol. 9 (1999) 593-596
    • (1999) Curr. Biol. , vol.9 , pp. 593-596
    • Alfalah, M.1    Jacob, R.2    Preuss, U.3    Zimmer, K.P.4    Naim, H.5    Naim, H.Y.6
  • 2
    • 0031031701 scopus 로고    scopus 로고
    • Direct interaction of Syk and Lyn protein tyrosine kinases in rat basophilic leukemia cells activated via type I Fc epsilon receptors
    • Amoui M., Draberova L., Tolar P., and Draber P. Direct interaction of Syk and Lyn protein tyrosine kinases in rat basophilic leukemia cells activated via type I Fc epsilon receptors. Eur. J. Immunol. 27 (1997) 321-328
    • (1997) Eur. J. Immunol. , vol.27 , pp. 321-328
    • Amoui, M.1    Draberova, L.2    Tolar, P.3    Draber, P.4
  • 5
    • 0032526224 scopus 로고    scopus 로고
    • Sorting and storage during secretory granule biogenesis: looking backward and looking forward
    • Arvan P., and Castle D. Sorting and storage during secretory granule biogenesis: looking backward and looking forward. Biochem. J. 332 (1998) 593-610
    • (1998) Biochem. J. , vol.332 , pp. 593-610
    • Arvan, P.1    Castle, D.2
  • 6
    • 17844382166 scopus 로고    scopus 로고
    • O-glycosylation is essential for intracellular targeting of synaptotagmins I and II in non-neuronal specialized secretory cells
    • Atiya-Nasagi Y., Cohen H., Medalia O., Fukudan M., and Sagi-Eisenberg R. O-glycosylation is essential for intracellular targeting of synaptotagmins I and II in non-neuronal specialized secretory cells. J. Cell Sci. 118 (2005) 1363-1372
    • (2005) J. Cell Sci. , vol.118 , pp. 1363-1372
    • Atiya-Nasagi, Y.1    Cohen, H.2    Medalia, O.3    Fukudan, M.4    Sagi-Eisenberg, R.5
  • 9
    • 0036035987 scopus 로고    scopus 로고
    • Synaptotagmin II negatively regulates MHC class II presentation by mast cells
    • Baram D., Peng Z., Medalia O., Mekori Y., and Sagi-Eisenberg R. Synaptotagmin II negatively regulates MHC class II presentation by mast cells. Mol. Immunol. 38 (2002) 1347-1352
    • (2002) Mol. Immunol. , vol.38 , pp. 1347-1352
    • Baram, D.1    Peng, Z.2    Medalia, O.3    Mekori, Y.4    Sagi-Eisenberg, R.5
  • 10
    • 12844268551 scopus 로고    scopus 로고
    • The adaptor protein AP-4 as a component of the clathrin coat machinery: a morphological study
    • Barois N., and Bakke O. The adaptor protein AP-4 as a component of the clathrin coat machinery: a morphological study. Biochem. J. 385 (2005) 503-510
    • (2005) Biochem. J. , vol.385 , pp. 503-510
    • Barois, N.1    Bakke, O.2
  • 12
    • 0032579398 scopus 로고    scopus 로고
    • Lysosomal targeting of P-selectin is mediated by a novel sequence within its cytoplasmic tail
    • Blagoveshchenskaya A.D., Norcott J.P., and Cutler D.F. Lysosomal targeting of P-selectin is mediated by a novel sequence within its cytoplasmic tail. J. Biol. Chem. 273 (1998) 2729-2737
    • (1998) J. Biol. Chem. , vol.273 , pp. 2729-2737
    • Blagoveshchenskaya, A.D.1    Norcott, J.P.2    Cutler, D.F.3
  • 13
    • 0032693673 scopus 로고    scopus 로고
    • Di-leucine signals mediate targeting of tyrosinase and synaptotagmin to synaptic-like microvesicles within PC12 cells
    • Blagoveshchenskaya A.D., Hewitt E.W., and Cutler D.F. Di-leucine signals mediate targeting of tyrosinase and synaptotagmin to synaptic-like microvesicles within PC12 cells. Mol. Biol. Cell 10 (1999) 3979-3990
    • (1999) Mol. Biol. Cell , vol.10 , pp. 3979-3990
    • Blagoveshchenskaya, A.D.1    Hewitt, E.W.2    Cutler, D.F.3
  • 14
    • 0034927311 scopus 로고    scopus 로고
    • Fas ligand is targeted to secretory lysosomes via a proline-rich domain in its cytoplasmic tail
    • Blott E.J., Bossi G., Clark R., Zvelebil M., and Griffiths G.M. Fas ligand is targeted to secretory lysosomes via a proline-rich domain in its cytoplasmic tail. J. Cell Sci. 114 (2001) 2405-2416
    • (2001) J. Cell Sci. , vol.114 , pp. 2405-2416
    • Blott, E.J.1    Bossi, G.2    Clark, R.3    Zvelebil, M.4    Griffiths, G.M.5
  • 15
    • 0035890324 scopus 로고    scopus 로고
    • Functional and physical interactions of the adaptor protein complex AP-4 with ADP-ribosylation factors (ARFs)
    • Boehm M., Aguilar R.C., and Bonifacino J.S. Functional and physical interactions of the adaptor protein complex AP-4 with ADP-ribosylation factors (ARFs). EMBO J. 20 (2001) 6265-6276
    • (2001) EMBO J. , vol.20 , pp. 6265-6276
    • Boehm, M.1    Aguilar, R.C.2    Bonifacino, J.S.3
  • 16
    • 0034752915 scopus 로고    scopus 로고
    • GGA proteins: new players in the sorting game
    • Boman A.L. GGA proteins: new players in the sorting game. J. Cell Sci. 114 (2001) 3413-3418
    • (2001) J. Cell Sci. , vol.114 , pp. 3413-3418
    • Boman, A.L.1
  • 17
    • 0347762565 scopus 로고    scopus 로고
    • The GGA proteins: adaptors on the move
    • Bonifacino J.S. The GGA proteins: adaptors on the move. Nat. Rev. Mol. Cell. Biol. 5 (2004) 23-32
    • (2004) Nat. Rev. Mol. Cell. Biol. , vol.5 , pp. 23-32
    • Bonifacino, J.S.1
  • 18
    • 0033620656 scopus 로고    scopus 로고
    • Molecular bases for the recognition of tyrosine-based sorting signals
    • Bonifacino J.S., and Dell'Angelica E.C. Molecular bases for the recognition of tyrosine-based sorting signals. J. Cell Biol. 145 (1999) 923-926
    • (1999) J. Cell Biol. , vol.145 , pp. 923-926
    • Bonifacino, J.S.1    Dell'Angelica, E.C.2
  • 19
    • 0038795645 scopus 로고    scopus 로고
    • Signals for sorting of transmembrane proteins to endosomes and lysosomes
    • Bonifacino J.S., and Traub L.M. Signals for sorting of transmembrane proteins to endosomes and lysosomes. Annu. Rev. Biochem. 72 (2003) 395-447
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 395-447
    • Bonifacino, J.S.1    Traub, L.M.2
  • 20
    • 0032974475 scopus 로고    scopus 로고
    • Degranulation plays an essential part in regulating cell surface expression of Fas ligand in T cells and natural killer cells
    • Bossi G., and Griffiths G.M. Degranulation plays an essential part in regulating cell surface expression of Fas ligand in T cells and natural killer cells. Nat. Med. 5 (1999) 90-96
    • (1999) Nat. Med. , vol.5 , pp. 90-96
    • Bossi, G.1    Griffiths, G.M.2
  • 22
    • 0028970788 scopus 로고
    • 2+ regulates the interaction between synaptotagmin and syntaxin 1
    • 2+ regulates the interaction between synaptotagmin and syntaxin 1. J. Biol. Chem. 270 (1995) 23667-23671
    • (1995) J. Biol. Chem. , vol.270 , pp. 23667-23671
    • Chapman, E.R.1    Hanson, P.I.2    An, S.3    Jahn, R.4
  • 23
    • 34547764415 scopus 로고    scopus 로고
    • A LYST/beige homolog is involved in biogenesis of Dictyostelium secretory lysosomes
    • Charette S.J., and Cosson P. A LYST/beige homolog is involved in biogenesis of Dictyostelium secretory lysosomes. J. Cell Sci. 120 (2007) 2338-2343
    • (2007) J. Cell Sci. , vol.120 , pp. 2338-2343
    • Charette, S.J.1    Cosson, P.2
  • 24
    • 40449090799 scopus 로고    scopus 로고
    • Altered composition and secretion of lysosome-derived compartments in Dictyostelium AP-3 mutant cells
    • Charette S.J., and Cosson P. Altered composition and secretion of lysosome-derived compartments in Dictyostelium AP-3 mutant cells. Traffic 9 (2008) 588-596
    • (2008) Traffic , vol.9 , pp. 588-596
    • Charette, S.J.1    Cosson, P.2
  • 25
    • 0025250145 scopus 로고
    • NPXY, a sequence often found in cytoplasmic tails, is required for coated pit-mediated internalization of the low density lipoprotein receptor
    • Chen W.J., Goldstein J.L., and Brown M.S. NPXY, a sequence often found in cytoplasmic tails, is required for coated pit-mediated internalization of the low density lipoprotein receptor. J. Biol. Chem. 265 (1990) 3116-3123
    • (1990) J. Biol. Chem. , vol.265 , pp. 3116-3123
    • Chen, W.J.1    Goldstein, J.L.2    Brown, M.S.3
  • 29
    • 0033007616 scopus 로고    scopus 로고
    • Altered trafficking of lysosomal proteins in Hermansky-Pudlak syndrome due to mutations in the beta 3A subunit of the AP-3 adaptor
    • Dell'Angelica E.C., Shotelersuk V., Aguilar R.C., Gahl W.A., and Bonifacino J.S. Altered trafficking of lysosomal proteins in Hermansky-Pudlak syndrome due to mutations in the beta 3A subunit of the AP-3 adaptor. Mol. Cell. 3 (1999) 11-21
    • (1999) Mol. Cell. , vol.3 , pp. 11-21
    • Dell'Angelica, E.C.1    Shotelersuk, V.2    Aguilar, R.C.3    Gahl, W.A.4    Bonifacino, J.S.5
  • 32
    • 0030792177 scopus 로고    scopus 로고
    • Interaction of furin in immature secretory granules from neuroendocrine cells with the AP-1 adaptor complex is modulated by casein kinase II phosphorylation
    • Dittie A.S., Thomas L., Thomas G., and Tooze S.A. Interaction of furin in immature secretory granules from neuroendocrine cells with the AP-1 adaptor complex is modulated by casein kinase II phosphorylation. EMBO J. 16 (1997) 4859-4870
    • (1997) EMBO J. , vol.16 , pp. 4859-4870
    • Dittie, A.S.1    Thomas, L.2    Thomas, G.3    Tooze, S.A.4
  • 33
    • 0026623115 scopus 로고
    • ADP-ribosylation factor, a small GTP-binding protein, is required for binding of the coatomer protein {beta}-COP to Golgi membranes
    • Donaldson J.G., Cassel D., Kahn R.A., and Klausner R.D. ADP-ribosylation factor, a small GTP-binding protein, is required for binding of the coatomer protein {beta}-COP to Golgi membranes. Proc. Natl. Acad. Sci. USA 89 (1992) 6408-6412
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 6408-6412
    • Donaldson, J.G.1    Cassel, D.2    Kahn, R.A.3    Klausner, R.D.4
  • 35
    • 0041659220 scopus 로고    scopus 로고
    • Structural insights into the SNARE mechanism
    • Fasshauer D. Structural insights into the SNARE mechanism. Biochim. Biophys. Acta 1641 (2003) 87-97
    • (2003) Biochim. Biophys. Acta , vol.1641 , pp. 87-97
    • Fasshauer, D.1
  • 36
    • 0039311662 scopus 로고    scopus 로고
    • ADP ribosylation factor 1 is required for synaptic vesicle budding in PC12 cells
    • Faundez V., Horng J.T., and Kelly R.B. ADP ribosylation factor 1 is required for synaptic vesicle budding in PC12 cells. J. Cell Biol. 138 (1997) 505-515
    • (1997) J. Cell Biol. , vol.138 , pp. 505-515
    • Faundez, V.1    Horng, J.T.2    Kelly, R.B.3
  • 37
    • 0032076102 scopus 로고    scopus 로고
    • A function for the AP3 coat complex in synaptic vesicle formation from endosomes
    • Faundez V., Horng J.T., and Kelly R.B. A function for the AP3 coat complex in synaptic vesicle formation from endosomes. Cell 93 (1998) 423-432
    • (1998) Cell , vol.93 , pp. 423-432
    • Faundez, V.1    Horng, J.T.2    Kelly, R.B.3
  • 38
    • 0033836583 scopus 로고    scopus 로고
    • The AP-3 complex required for endosomal synaptic vesicle biogenesis is associated with casein kinase Ia-like isoform
    • Faundez V.V., and Kelly R.B. The AP-3 complex required for endosomal synaptic vesicle biogenesis is associated with casein kinase Ia-like isoform. Mol. Biol. Cell 10 (2000) 2591-2604
    • (2000) Mol. Biol. Cell , vol.10 , pp. 2591-2604
    • Faundez, V.V.1    Kelly, R.B.2
  • 39
    • 0242713072 scopus 로고    scopus 로고
    • Neutrophil granules and secretory vesicles in inflammation
    • Faurschou M., and Borregaard N. Neutrophil granules and secretory vesicles in inflammation. Microbes Infect. 5 (2003) 1317-1327
    • (2003) Microbes Infect. , vol.5 , pp. 1317-1327
    • Faurschou, M.1    Borregaard, N.2
  • 40
    • 0027524778 scopus 로고
    • The synaptic vesicle proteins SV2, synaptotagmin and synaptophysin are sorted to separate cellular compartments in CHO fibroblasts
    • Feany M.B., Yee A.G., Delvy M.L., and Buckley K.M. The synaptic vesicle proteins SV2, synaptotagmin and synaptophysin are sorted to separate cellular compartments in CHO fibroblasts. J. Cell Biol. 123 (1993) 575-584
    • (1993) J. Cell Biol. , vol.123 , pp. 575-584
    • Feany, M.B.1    Yee, A.G.2    Delvy, M.L.3    Buckley, K.M.4
  • 43
    • 0034331295 scopus 로고    scopus 로고
    • Genomic structure of the mouse Ap3b1 gene in normal and pearl mice
    • Feng L., Rigatti B.W., Novak E.K., Gorin M.B., and Swank R.T. Genomic structure of the mouse Ap3b1 gene in normal and pearl mice. Genomics 69 (2000) 370-379
    • (2000) Genomics , vol.69 , pp. 370-379
    • Feng, L.1    Rigatti, B.W.2    Novak, E.K.3    Gorin, M.B.4    Swank, R.T.5
  • 45
    • 0035937156 scopus 로고    scopus 로고
    • Binding of AP2 to sorting signals is modulated by AP2 phosphorylation
    • Fingerhut A., von Figura K., and Honing S. Binding of AP2 to sorting signals is modulated by AP2 phosphorylation. J. Biol. Chem. 276 (2001) 5476-5482
    • (2001) J. Biol. Chem. , vol.276 , pp. 5476-5482
    • Fingerhut, A.1    von Figura, K.2    Honing, S.3
  • 46
    • 33846498689 scopus 로고    scopus 로고
    • Expression and function of synaptotagmin VII in CTLs
    • Fowler K.T., Andrews N.W., and Huleatt J.W. Expression and function of synaptotagmin VII in CTLs. J. Immunol. 178 (2007) 1498-1504
    • (2007) J. Immunol. , vol.178 , pp. 1498-1504
    • Fowler, K.T.1    Andrews, N.W.2    Huleatt, J.W.3
  • 47
    • 3042782694 scopus 로고    scopus 로고
    • RNA interference-mediated silencing of synaptotagmin IX, but not synaptotagmin I, inhibits dense-core vesicle exocytosis in PC12 cells
    • Fukuda M. RNA interference-mediated silencing of synaptotagmin IX, but not synaptotagmin I, inhibits dense-core vesicle exocytosis in PC12 cells. Biochem. J. 380 (2004) 875-879
    • (2004) Biochem. J. , vol.380 , pp. 875-879
    • Fukuda, M.1
  • 48
    • 17044383478 scopus 로고    scopus 로고
    • Versatile role of Rab27 in membrane trafficking: focus on the Rab27 effector families
    • Fukuda M. Versatile role of Rab27 in membrane trafficking: focus on the Rab27 effector families. J. Biochem. (Tokyo) 137 (2005) 9-16
    • (2005) J. Biochem. (Tokyo) , vol.137 , pp. 9-16
    • Fukuda, M.1
  • 49
    • 0027986795 scopus 로고
    • Inositol-1,3,4,5-tetrakisphosphate binding to C2B domain of IP4BP/synaptotagmin II
    • Fukuda M., Aruga J., Niinobe M., Aimoto S., and Mikoshiba K. Inositol-1,3,4,5-tetrakisphosphate binding to C2B domain of IP4BP/synaptotagmin II. J. Biol. Chem. 269 (1994) 29206-29211
    • (1994) J. Biol. Chem. , vol.269 , pp. 29206-29211
    • Fukuda, M.1    Aruga, J.2    Niinobe, M.3    Aimoto, S.4    Mikoshiba, K.5
  • 51
    • 0020365635 scopus 로고
    • Spatial relationships of microtubule-organizing centers and the contact area of cytotoxic T lymphocytes and target cells
    • Geiger B., Rosen D., and Berke G. Spatial relationships of microtubule-organizing centers and the contact area of cytotoxic T lymphocytes and target cells. J. Cell. Biol. 95 (1982) 137-143
    • (1982) J. Cell. Biol. , vol.95 , pp. 137-143
    • Geiger, B.1    Rosen, D.2    Berke, G.3
  • 52
    • 0025879767 scopus 로고
    • Synaptotagmin II. A novel differentially distributed form of synaptotagmin
    • Geppert M., Archer B.D., and Sudhof T.C. Synaptotagmin II. A novel differentially distributed form of synaptotagmin. J. Biol. Chem. 266 (1991) 13548-13552
    • (1991) J. Biol. Chem. , vol.266 , pp. 13548-13552
    • Geppert, M.1    Archer, B.D.2    Sudhof, T.C.3
  • 54
    • 0038190920 scopus 로고    scopus 로고
    • Phosphorylation-induced conformational changes regulate GGAs 1 and 3 function at the trans-Golgi network
    • Ghosh P., and Kornfeld S. Phosphorylation-induced conformational changes regulate GGAs 1 and 3 function at the trans-Golgi network. J. Biol. Chem. 278 (2003) 14543-14549
    • (2003) J. Biol. Chem. , vol.278 , pp. 14543-14549
    • Ghosh, P.1    Kornfeld, S.2
  • 55
    • 4744350042 scopus 로고    scopus 로고
    • Involvement of Rab27 in antigen-induced histamine release from rat basophilic leukemia 2H3 cells
    • Goishi K., Mizuno K., Nakanishi H., and Sasaki T. Involvement of Rab27 in antigen-induced histamine release from rat basophilic leukemia 2H3 cells. Biochim. Biophys. Res. Commun. 324 (2004) 294-301
    • (2004) Biochim. Biophys. Res. Commun. , vol.324 , pp. 294-301
    • Goishi, K.1    Mizuno, K.2    Nakanishi, H.3    Sasaki, T.4
  • 56
    • 26444479437 scopus 로고    scopus 로고
    • Granuphilin molecularly docks insulin granules to the fusion machinery
    • Gomi H., Mizutani S., Kasai K., Itohara S., and Izumi T. Granuphilin molecularly docks insulin granules to the fusion machinery. J. Cell Biol. 171 (2005) 99-109
    • (2005) J. Cell Biol. , vol.171 , pp. 99-109
    • Gomi, H.1    Mizutani, S.2    Kasai, K.3    Itohara, S.4    Izumi, T.5
  • 57
    • 35848959050 scopus 로고    scopus 로고
    • Rab27b is expressed in a wide range of exocytic cells and involved in the delivery of secretory granules near the plasma membrane
    • Gomi H., Mori K., Itohara S., and Izumi T. Rab27b is expressed in a wide range of exocytic cells and involved in the delivery of secretory granules near the plasma membrane. Mol. Biol. Cell 18 (2007) 4377-4386
    • (2007) Mol. Biol. Cell , vol.18 , pp. 4377-4386
    • Gomi, H.1    Mori, K.2    Itohara, S.3    Izumi, T.4
  • 58
    • 0030248423 scopus 로고    scopus 로고
    • Secretory lysosomes - a special mechanism of regulated secretion in haemopoietic cells
    • Griffiths G.M. Secretory lysosomes - a special mechanism of regulated secretion in haemopoietic cells. Trends Cell Biol. 6 (1996) 329-332
    • (1996) Trends Cell Biol. , vol.6 , pp. 329-332
    • Griffiths, G.M.1
  • 59
    • 0037237001 scopus 로고    scopus 로고
    • Synaptotagmin III is a critical factor for the formation of the perinuclear endocytic recycling compartment and determination of secretory granules size
    • Grimberg E., Peng Z., Hammel I., and Sagi-Eisenberg R. Synaptotagmin III is a critical factor for the formation of the perinuclear endocytic recycling compartment and determination of secretory granules size. J. Cell Sci. 116 (2003) 145-154
    • (2003) J. Cell Sci. , vol.116 , pp. 145-154
    • Grimberg, E.1    Peng, Z.2    Hammel, I.3    Sagi-Eisenberg, R.4
  • 61
    • 0029005106 scopus 로고
    • A targeting signal in VAMP regulating transport to synaptic vesicles
    • Grote E., Hao J.C., Bennett M.K., and Kelly R.B. A targeting signal in VAMP regulating transport to synaptic vesicles. Cell 81 (1995) 581-589
    • (1995) Cell , vol.81 , pp. 581-589
    • Grote, E.1    Hao, J.C.2    Bennett, M.K.3    Kelly, R.B.4
  • 62
    • 0242720104 scopus 로고    scopus 로고
    • Synaptotagmin IX, a possible linker between the perinuclear endocytic recycling compartment and the microtubules
    • Haberman Y., Grimberg E., Fukuda M., and Sagi-Eisenberg R. Synaptotagmin IX, a possible linker between the perinuclear endocytic recycling compartment and the microtubules. J. Cell Sci. 116 (2003) 4307-4318
    • (2003) J. Cell Sci. , vol.116 , pp. 4307-4318
    • Haberman, Y.1    Grimberg, E.2    Fukuda, M.3    Sagi-Eisenberg, R.4
  • 63
    • 18844456346 scopus 로고    scopus 로고
    • Classical protein kinase C(s) regulates targeting of synaptotagmin IX to the endocytic recycling compartment
    • Haberman Y., Ziv I., Gorzalczany Y., Fukuda M., and Sagi-Eisenberg R. Classical protein kinase C(s) regulates targeting of synaptotagmin IX to the endocytic recycling compartment. J. Cell Sci. 118 (2005) 1641-1649
    • (2005) J. Cell Sci. , vol.118 , pp. 1641-1649
    • Haberman, Y.1    Ziv, I.2    Gorzalczany, Y.3    Fukuda, M.4    Sagi-Eisenberg, R.5
  • 64
    • 34147103471 scopus 로고    scopus 로고
    • Synaptotagmin (Syt) IX is an essential determinant for protein sorting to secretory granules in mast cells
    • Haberman Y., Ziv I., Gorzalczany Y., Hirschberg K., Mittleman L., Fukuda M., and Sagi-Eisenberg R. Synaptotagmin (Syt) IX is an essential determinant for protein sorting to secretory granules in mast cells. Blood 109 (2007) 3385-3392
    • (2007) Blood , vol.109 , pp. 3385-3392
    • Haberman, Y.1    Ziv, I.2    Gorzalczany, Y.3    Hirschberg, K.4    Mittleman, L.5    Fukuda, M.6    Sagi-Eisenberg, R.7
  • 66
    • 0030943923 scopus 로고    scopus 로고
    • Dynamic O-linked glycosylation of nuclear and cytoskeletal proteins
    • Hart G.W. Dynamic O-linked glycosylation of nuclear and cytoskeletal proteins. Annu. Rev. Biochem. 66 (1997) 315-335
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 315-335
    • Hart, G.W.1
  • 67
  • 69
    • 0030054178 scopus 로고    scopus 로고
    • Ubiquitination of a yeast plasma membrane receptor signals its ligand-stimulated endocytosis
    • Hicke L., and Riezman H. Ubiquitination of a yeast plasma membrane receptor signals its ligand-stimulated endocytosis. Cell 84 (1996) 277-287
    • (1996) Cell , vol.84 , pp. 277-287
    • Hicke, L.1    Riezman, H.2
  • 71
    • 0039109678 scopus 로고    scopus 로고
    • A di-leucine-based motif in the cytoplasmic tail of LIMP-II and tyrosinase mediates selective binding of AP-3
    • Honing S., Sandoval I., and von Figura K. A di-leucine-based motif in the cytoplasmic tail of LIMP-II and tyrosinase mediates selective binding of AP-3. EMBO J. 17 (1998) 1304-1314
    • (1998) EMBO J. , vol.17 , pp. 1304-1314
    • Honing, S.1    Sandoval, I.2    von Figura, K.3
  • 72
    • 33750555919 scopus 로고    scopus 로고
    • Ubiquitin-binding domains
    • Hurley J.H., Lee S., and Prag G. Ubiquitin-binding domains. Biochem. J. 399 (2006) 361-372
    • (2006) Biochem. J. , vol.399 , pp. 361-372
    • Hurley, J.H.1    Lee, S.2    Prag, G.3
  • 77
    • 0035958546 scopus 로고    scopus 로고
    • Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I
    • Katzmann D.J., Babst M., and Emr S.D. Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I. Cell 106 (2001) 145-155
    • (2001) Cell , vol.106 , pp. 145-155
    • Katzmann, D.J.1    Babst, M.2    Emr, S.D.3
  • 78
    • 0037155892 scopus 로고    scopus 로고
    • P-selectin targeting to secretory lysosomes of Rbl-2H3 cells
    • Kaur J., and Cutler D.F. P-selectin targeting to secretory lysosomes of Rbl-2H3 cells. J. Biol. Chem. 277 (2002) 10498-10505
    • (2002) J. Biol. Chem. , vol.277 , pp. 10498-10505
    • Kaur, J.1    Cutler, D.F.2
  • 79
    • 0034739837 scopus 로고    scopus 로고
    • Purification of clathrin assembly protein from rat liver
    • Kim H.L., and Kim J.A. Purification of clathrin assembly protein from rat liver. Exp. Mol. Med. 32 (2000) 222-226
    • (2000) Exp. Mol. Med. , vol.32 , pp. 222-226
    • Kim, H.L.1    Kim, J.A.2
  • 80
    • 0032970154 scopus 로고    scopus 로고
    • The high-affinity IgE receptor (Fc epsilon RI): from physiology to pathology
    • Kinet J.P. The high-affinity IgE receptor (Fc epsilon RI): from physiology to pathology. Annu. Rev. Immunol. 17 (1999) 931-972
    • (1999) Annu. Rev. Immunol. , vol.17 , pp. 931-972
    • Kinet, J.P.1
  • 81
    • 0033280324 scopus 로고    scopus 로고
    • Adaptors for clathrin-mediated traffic
    • Kirchhausen T. Adaptors for clathrin-mediated traffic. Annu. Rev. Cell Dev. Biol. 15 (1999) 705-732
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 705-732
    • Kirchhausen, T.1
  • 82
    • 0037123789 scopus 로고    scopus 로고
    • Clathrin adaptors really adapt
    • Kirchhausen T. Clathrin adaptors really adapt. Cell 109 (2002) 413-416
    • (2002) Cell , vol.109 , pp. 413-416
    • Kirchhausen, T.1
  • 83
    • 0026561901 scopus 로고
    • Brefeldin A: insights into the control of membrane traffic and organelle structure
    • Klausner R.D., Donaldson J.G., and Lippincott-Schwartz J. Brefeldin A: insights into the control of membrane traffic and organelle structure. J. Cell Biol. 116 (1992) 1071-1080
    • (1992) J. Cell Biol. , vol.116 , pp. 1071-1080
    • Klausner, R.D.1    Donaldson, J.G.2    Lippincott-Schwartz, J.3
  • 84
    • 10344266449 scopus 로고    scopus 로고
    • Rab27A-binding protein Slp2-a is required for peripheral melanosome distribution and elongated cell shape in melanocytes
    • Kuroda T.S., and Fukuda M. Rab27A-binding protein Slp2-a is required for peripheral melanosome distribution and elongated cell shape in melanocytes. Nat. Cell Biol. 6 (2004) 1195-1203
    • (2004) Nat. Cell Biol. , vol.6 , pp. 1195-1203
    • Kuroda, T.S.1    Fukuda, M.2
  • 86
    • 0034725650 scopus 로고    scopus 로고
    • The interaction of beta-arrestin with the AP-2 adaptor is required for the clustering of beta 2-adrenergic receptor into clathrin-coated pits
    • Laporte S.A., Oakley R.H., Holt J.A., Barak L.S., and Caron M.G. The interaction of beta-arrestin with the AP-2 adaptor is required for the clustering of beta 2-adrenergic receptor into clathrin-coated pits. J. Biol. Chem. 275 (2000) 23120-23126
    • (2000) J. Biol. Chem. , vol.275 , pp. 23120-23126
    • Laporte, S.A.1    Oakley, R.H.2    Holt, J.A.3    Barak, L.S.4    Caron, M.G.5
  • 87
    • 0027371853 scopus 로고
    • Binding of AP-1 Golgi adaptors to membranes requires phosphorylated cytoplasmic domains of the mannose 6-phosphate/insulin-like growth factor II receptor
    • Le Borgne R., Schmidt A., Mauxion F., Griffiths G., and Hoflack B. Binding of AP-1 Golgi adaptors to membranes requires phosphorylated cytoplasmic domains of the mannose 6-phosphate/insulin-like growth factor II receptor. J. Biol. Chem. 268 (1993) 22552-22556
    • (1993) J. Biol. Chem. , vol.268 , pp. 22552-22556
    • Le Borgne, R.1    Schmidt, A.2    Mauxion, F.3    Griffiths, G.4    Hoflack, B.5
  • 90
    • 34447286699 scopus 로고    scopus 로고
    • Endobrevin/VAMP8 mediates exocytotic release of hexosaminidase from rat basophilic leukaemia cells
    • Lippert U., Ferrari D.M., and Jahn R. Endobrevin/VAMP8 mediates exocytotic release of hexosaminidase from rat basophilic leukaemia cells. FEBS Lett. 581 (2007) 3479-3484
    • (2007) FEBS Lett. , vol.581 , pp. 3479-3484
    • Lippert, U.1    Ferrari, D.M.2    Jahn, R.3
  • 91
    • 0036170805 scopus 로고    scopus 로고
    • Expression of eosinophil target SNAREs as potential cognate receptors for vesicle-associated membrane protein-2 in exocytosis
    • Logan M.R., Lacy P., Bablitz B., and Moqbel R. Expression of eosinophil target SNAREs as potential cognate receptors for vesicle-associated membrane protein-2 in exocytosis. J. Allergy Clin. Immunol. 109 (2002) 299-306
    • (2002) J. Allergy Clin. Immunol. , vol.109 , pp. 299-306
    • Logan, M.R.1    Lacy, P.2    Bablitz, B.3    Moqbel, R.4
  • 92
    • 0034307682 scopus 로고    scopus 로고
    • Involvement of SNAP-23 and syntaxin 6 in human neutrophil exocytosis
    • Martin-Martin B., Nabokina S.M., Blasi J., Lazo P.A., and Mollinedo F. Involvement of SNAP-23 and syntaxin 6 in human neutrophil exocytosis. Blood 96 (2000) 2574-2583
    • (2000) Blood , vol.96 , pp. 2574-2583
    • Martin-Martin, B.1    Nabokina, S.M.2    Blasi, J.3    Lazo, P.A.4    Mollinedo, F.5
  • 94
    • 0035947775 scopus 로고    scopus 로고
    • Stonin 2: an adaptor-like protein that interacts with components of the endocytic machinery
    • Martina J.A., Bonangelino C.J., Aguilar R.C., and Bonifacino J.S. Stonin 2: an adaptor-like protein that interacts with components of the endocytic machinery. J. Cell Biol. 153 (2001) 1111-1120
    • (2001) J. Cell Biol. , vol.153 , pp. 1111-1120
    • Martina, J.A.1    Bonangelino, C.J.2    Aguilar, R.C.3    Bonifacino, J.S.4
  • 97
    • 33846974729 scopus 로고    scopus 로고
    • Synaptotagmin 3 deficiency in T cells impairs recycling of the chemokine receptor CXCR4 and thereby inhibits CXCL12 chemokine-induced migration
    • Masztalerz A., Zeelenberg I.S., Wijnands Y.M., de Bruijn R., Drager A.M., Janssen H., and Roos E. Synaptotagmin 3 deficiency in T cells impairs recycling of the chemokine receptor CXCR4 and thereby inhibits CXCL12 chemokine-induced migration. J. Cell Sci. 120 (2007) 219-228
    • (2007) J. Cell Sci. , vol.120 , pp. 219-228
    • Masztalerz, A.1    Zeelenberg, I.S.2    Wijnands, Y.M.3    de Bruijn, R.4    Drager, A.M.5    Janssen, H.6    Roos, E.7
  • 98
    • 0030022935 scopus 로고    scopus 로고
    • A casein kinase II phosphorylation site in the cytoplasmic domain of the cation-dependent mannose 6-phosphate receptor determines the high affinity interaction of the AP-1 Golgi assembly proteins with membranes
    • Mauxion F., Le Borgne R., Munier-Lehmann H., and Hoflack B. A casein kinase II phosphorylation site in the cytoplasmic domain of the cation-dependent mannose 6-phosphate receptor determines the high affinity interaction of the AP-1 Golgi assembly proteins with membranes. J. Biol. Chem. 271 (1996) 2171-2178
    • (1996) J. Biol. Chem. , vol.271 , pp. 2171-2178
    • Mauxion, F.1    Le Borgne, R.2    Munier-Lehmann, H.3    Hoflack, B.4
  • 100
    • 0034330540 scopus 로고    scopus 로고
    • Analysis of the lysosomal storage disease Chediak-Higashi syndrome
    • McVey Ward D., Griffiths G.M., Stinchcombe J.C., and Kaplan J. Analysis of the lysosomal storage disease Chediak-Higashi syndrome. Traffic 1 (2000) 816-822
    • (2000) Traffic , vol.1 , pp. 816-822
    • McVey Ward, D.1    Griffiths, G.M.2    Stinchcombe, J.C.3    Kaplan, J.4
  • 101
    • 0034663849 scopus 로고    scopus 로고
    • Binding kinetics, ligand specificity for the interactions of the C2B domain of synaptogmin II with inositol polyphosphates and phosphoinositides
    • Mehrotra B., Myszka D.G., and Prestwich G.D. Binding kinetics, ligand specificity for the interactions of the C2B domain of synaptogmin II with inositol polyphosphates and phosphoinositides. Biochemistry 39 (2000) 9679-9686
    • (2000) Biochemistry , vol.39 , pp. 9679-9686
    • Mehrotra, B.1    Myszka, D.G.2    Prestwich, G.D.3
  • 104
    • 0038107403 scopus 로고    scopus 로고
    • Biochemical and functional characterization of Rab27a mutations occurring in Griscelli syndrome patients
    • Menasche G., Feldmann J., Houdusse A., Desaymard C., Fischer A., Goud B., and de Saint Basile G. Biochemical and functional characterization of Rab27a mutations occurring in Griscelli syndrome patients. Blood 101 (2003) 2736-2742
    • (2003) Blood , vol.101 , pp. 2736-2742
    • Menasche, G.1    Feldmann, J.2    Houdusse, A.3    Desaymard, C.4    Fischer, A.5    Goud, B.6    de Saint Basile, G.7
  • 106
  • 108
    • 33847754590 scopus 로고    scopus 로고
    • Rab27a is a key component of the secretory machinery of azurophilic granules in granulocytes
    • Munafó D.B., Jennifer J.L., Ellis B.A., Rutschmann S., Beutler B., and Catz S.D. Rab27a is a key component of the secretory machinery of azurophilic granules in granulocytes. Biochem. J. 402 (2007) 229-239
    • (2007) Biochem. J. , vol.402 , pp. 229-239
    • Munafó, D.B.1    Jennifer, J.L.2    Ellis, B.A.3    Rutschmann, S.4    Beutler, B.5    Catz, S.D.6
  • 112
    • 0027319325 scopus 로고
    • Synaptic function is impaired but not eliminated in C. elegans mutants lacking synaptotagmin
    • Nonet M.L., Grundahl K., Meyer B.J., and Rand J.B. Synaptic function is impaired but not eliminated in C. elegans mutants lacking synaptotagmin. Cell 73 (1993) 1291-1305
    • (1993) Cell , vol.73 , pp. 1291-1305
    • Nonet, M.L.1    Grundahl, K.2    Meyer, B.J.3    Rand, J.B.4
  • 113
    • 33750365613 scopus 로고    scopus 로고
    • Clathrin-associated adaptor protein complexes
    • Ohno H. Clathrin-associated adaptor protein complexes. J. Cell Sci. 119 (2006) 3719-3721
    • (2006) J. Cell Sci. , vol.119 , pp. 3719-3721
    • Ohno, H.1
  • 114
    • 33645955916 scopus 로고    scopus 로고
    • Efficient sorting of TNF-alpha to rodent mast cell granules is dependent on N-linked glycosylation
    • Olszewski M.B., Trzaska D., Knol E.F., Adamczewska V., and Dastych J. Efficient sorting of TNF-alpha to rodent mast cell granules is dependent on N-linked glycosylation. Eur. J. Immunol. 36 (2006) 997-1008
    • (2006) Eur. J. Immunol. , vol.36 , pp. 997-1008
    • Olszewski, M.B.1    Trzaska, D.2    Knol, E.F.3    Adamczewska, V.4    Dastych, J.5
  • 115
    • 0032572560 scopus 로고    scopus 로고
    • ADP-Ribosylation Factor 1(ARF1) regulates recruitment of the AP-3 adaptor complex to membranes
    • Ooi C.E., Dell'Angelica E.C., and Bonifacino J.S. ADP-Ribosylation Factor 1(ARF1) regulates recruitment of the AP-3 adaptor complex to membranes. J. Cell Biol. 142 (1998) 391-402
    • (1998) J. Cell Biol. , vol.142 , pp. 391-402
    • Ooi, C.E.1    Dell'Angelica, E.C.2    Bonifacino, J.S.3
  • 116
    • 1842509099 scopus 로고    scopus 로고
    • Localization of the AP-3 adaptor complex defines a novel endosomal exit site for lysosomal membrane proteins
    • Peden A.A., Oorschot V., Hesser B.A., Austin C.D., Scheller R.H., and Klumperman J. Localization of the AP-3 adaptor complex defines a novel endosomal exit site for lysosomal membrane proteins. J. Cell Biol. 164 (2004) 1065-1076
    • (2004) J. Cell Biol. , vol.164 , pp. 1065-1076
    • Peden, A.A.1    Oorschot, V.2    Hesser, B.A.3    Austin, C.D.4    Scheller, R.H.5    Klumperman, J.6
  • 117
    • 2342640284 scopus 로고    scopus 로고
    • Membrane traffic: GGAs sort Ubiquitin
    • Pelham H.R. Membrane traffic: GGAs sort Ubiquitin. Curr. Biol. 14 (2004) R357
    • (2004) Curr. Biol. , vol.14
    • Pelham, H.R.1
  • 118
    • 0025270739 scopus 로고
    • Phospholipid binding by a synaptic vesicle protein homologous to the regulatory region of protein kinase C
    • Perin M.S., Fried V.A., Mignery G.A., Jahn R., and Sudhof T.C. Phospholipid binding by a synaptic vesicle protein homologous to the regulatory region of protein kinase C. Nature 345 (1990) 260-263
    • (1990) Nature , vol.345 , pp. 260-263
    • Perin, M.S.1    Fried, V.A.2    Mignery, G.A.3    Jahn, R.4    Sudhof, T.C.5
  • 119
    • 34547981932 scopus 로고    scopus 로고
    • Ubiquitin-dependent sorting of integral membrane proteins for degradation in lysosomes
    • Piper R.C., and Luzio J.P. Ubiquitin-dependent sorting of integral membrane proteins for degradation in lysosomes. Curr. Opin. Cell Biol. 19 (2007) 459-465
    • (2007) Curr. Opin. Cell Biol. , vol.19 , pp. 459-465
    • Piper, R.C.1    Luzio, J.P.2
  • 120
  • 123
    • 40649110538 scopus 로고    scopus 로고
    • Mast cells possess distinct secretory granule subsets whose exocytosis is regulated by different SNARE isoforms
    • Puri N., and Roche P.A. Mast cells possess distinct secretory granule subsets whose exocytosis is regulated by different SNARE isoforms. Proc. Natl. Acad. Sci. USA 105 (2008) 2580-2585
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 2580-2585
    • Puri, N.1    Roche, P.A.2
  • 124
    • 0242662821 scopus 로고    scopus 로고
    • Mast cell degranulation requires N-ethylmaleimide-sensitive factor-mediated SNARE disassembly
    • Puri N., Kruhlak M.J., Whiteheart S.W., and Roche P.A. Mast cell degranulation requires N-ethylmaleimide-sensitive factor-mediated SNARE disassembly. J. Immunol. 171 (2003) 5345-5352
    • (2003) J. Immunol. , vol.171 , pp. 5345-5352
    • Puri, N.1    Kruhlak, M.J.2    Whiteheart, S.W.3    Roche, P.A.4
  • 125
    • 0037005404 scopus 로고    scopus 로고
    • Hrs and endocytic sorting of ubiquitinated membrane proteins
    • Raiborg C., and Stenmark H. Hrs and endocytic sorting of ubiquitinated membrane proteins. Cell Struct. Funct. 27 (2002) 403-408
    • (2002) Cell Struct. Funct. , vol.27 , pp. 403-408
    • Raiborg, C.1    Stenmark, H.2
  • 127
    • 0030687649 scopus 로고    scopus 로고
    • Accumulation of major histocompatibility complex class II molecules in mast cell secretory granules and their release upon degranulation
    • Raposo G., Tenza D., Mecheri S., Peronet R., Bonnerot C., and Desaymard C. Accumulation of major histocompatibility complex class II molecules in mast cell secretory granules and their release upon degranulation. Mol. Biol. Cell 8 (1997) 2631-2645
    • (1997) Mol. Biol. Cell , vol.8 , pp. 2631-2645
    • Raposo, G.1    Tenza, D.2    Mecheri, S.3    Peronet, R.4    Bonnerot, C.5    Desaymard, C.6
  • 128
    • 27744484750 scopus 로고    scopus 로고
    • Identification of soluble N-ethylmaleimide-sensitive factor attachment protein receptor exocytotic machinery in human plasma cells: SNAP-23 is essential for antibody secretion
    • Reales E., Mora-Lopez F., Rivas V., Garcia-Poley A., Brieva J.A., and Campos-Caro A. Identification of soluble N-ethylmaleimide-sensitive factor attachment protein receptor exocytotic machinery in human plasma cells: SNAP-23 is essential for antibody secretion. J. Immunol. 175 (2005) 6686-6693
    • (2005) J. Immunol. , vol.175 , pp. 6686-6693
    • Reales, E.1    Mora-Lopez, F.2    Rivas, V.3    Garcia-Poley, A.4    Brieva, J.A.5    Campos-Caro, A.6
  • 129
    • 0026006536 scopus 로고
    • Newly synthesized synaptophysin is transported to synaptic-like microvesicles via constitutive secretory vesicles and the plasma membrane
    • Regnier V.A., Tooze S.A., and Huttner W.B. Newly synthesized synaptophysin is transported to synaptic-like microvesicles via constitutive secretory vesicles and the plasma membrane. EMBO J. 10 (1991) 3589-3601
    • (1991) EMBO J. , vol.10 , pp. 3589-3601
    • Regnier, V.A.1    Tooze, S.A.2    Huttner, W.B.3
  • 130
    • 0031571873 scopus 로고    scopus 로고
    • Involvement of the ras-like GTPase rab3d in RBL-2H3 mast cell exocytosis following stimulation via high affinity IgE receptors (Fc epsilonRI)
    • Roa M., Paumet F., Le Mao J., David B., and Blank U. Involvement of the ras-like GTPase rab3d in RBL-2H3 mast cell exocytosis following stimulation via high affinity IgE receptors (Fc epsilonRI). J. Immunol. 159 (1997) 2815-2823
    • (1997) J. Immunol. , vol.159 , pp. 2815-2823
    • Roa, M.1    Paumet, F.2    Le Mao, J.3    David, B.4    Blank, U.5
  • 135
    • 35048830834 scopus 로고    scopus 로고
    • Presence of SNAP-23 and syntaxin 4 in mouse and hamster peritoneal mast cells
    • Salinas E., Rodriguez G., and Quintanar J.L. Presence of SNAP-23 and syntaxin 4 in mouse and hamster peritoneal mast cells. Acta Histochem. 109 (2007) 454-460
    • (2007) Acta Histochem. , vol.109 , pp. 454-460
    • Salinas, E.1    Rodriguez, G.2    Quintanar, J.L.3
  • 136
    • 43649098258 scopus 로고    scopus 로고
    • Vesicle associated membrane protein (VAMP)-7 and VAMP-8, but not VAMP-2 or VAMP-3, are required for activation-induced degranulation of mature human mast cells
    • Sander L.E., Frank S.P., Bolat S., Galli T., Bigalke H., Bischoff S.C., and Lorens A. Vesicle associated membrane protein (VAMP)-7 and VAMP-8, but not VAMP-2 or VAMP-3, are required for activation-induced degranulation of mature human mast cells. Eur. J. Immunol. 38 (2008) 855-863
    • (2008) Eur. J. Immunol. , vol.38 , pp. 855-863
    • Sander, L.E.1    Frank, S.P.2    Bolat, S.3    Galli, T.4    Bigalke, H.5    Bischoff, S.C.6    Lorens, A.7
  • 137
    • 0018343194 scopus 로고
    • The heterophagic granules of mast cells: dipeptidyl aminopeptidase II activity and resistance to exocytosis
    • Sannes P.L., and Spicer S.S. The heterophagic granules of mast cells: dipeptidyl aminopeptidase II activity and resistance to exocytosis. Am. J. Pathol. 94 (1979) 447-457
    • (1979) Am. J. Pathol. , vol.94 , pp. 447-457
    • Sannes, P.L.1    Spicer, S.S.2
  • 140
    • 2942674409 scopus 로고    scopus 로고
    • Rab GTPases and myosin motors in organelle motility
    • Seabra M.C., and Coudrier E. Rab GTPases and myosin motors in organelle motility. Traffic 5 (2004) 393-399
    • (2004) Traffic , vol.5 , pp. 393-399
    • Seabra, M.C.1    Coudrier, E.2
  • 142
    • 0032538838 scopus 로고    scopus 로고
    • Neuroendocrine synaptic vesicles are formed in vitro by both clathrin-dependent and clathrin-independent pathways
    • Shi G., Faundez V., Roos J., Dell'Angelica E.C., and Kelly R.B. Neuroendocrine synaptic vesicles are formed in vitro by both clathrin-dependent and clathrin-independent pathways. J. Cell Biol. 143 (1998) 947-955
    • (1998) J. Cell Biol. , vol.143 , pp. 947-955
    • Shi, G.1    Faundez, V.2    Roos, J.3    Dell'Angelica, E.C.4    Kelly, R.B.5
  • 143
    • 2942682767 scopus 로고    scopus 로고
    • Insights into the phosphoregulation of beta-secretase sorting signal by the VHS domain of GGA1
    • Shiba T., Kametaka S., Kawasaki M., Shibata M., Waguri S., Uchiyama Y., and Wakatsuki S. Insights into the phosphoregulation of beta-secretase sorting signal by the VHS domain of GGA1. Traffic 5 (2004) 437-448
    • (2004) Traffic , vol.5 , pp. 437-448
    • Shiba, T.1    Kametaka, S.2    Kawasaki, M.3    Shibata, M.4    Waguri, S.5    Uchiyama, Y.6    Wakatsuki, S.7
  • 145
    • 0036428014 scopus 로고    scopus 로고
    • The molecular machinery for the biogenesis of lysosome-related organelles: lessons from Hermansky-Pudlak syndrome
    • Starcevic M., Nazarian R., and Dell'Angelica E.C. The molecular machinery for the biogenesis of lysosome-related organelles: lessons from Hermansky-Pudlak syndrome. Semin. Cell Dev. Biol. 13 (2002) 271-278
    • (2002) Semin. Cell Dev. Biol. , vol.13 , pp. 271-278
    • Starcevic, M.1    Nazarian, R.2    Dell'Angelica, E.C.3
  • 146
    • 3042793578 scopus 로고    scopus 로고
    • Linking albinism and immunity: the secrets of secretory lysosomes
    • Stinchcombe J., Bossi G., and Griffiths G.M. Linking albinism and immunity: the secrets of secretory lysosomes. Science 305 (2004) 55-59
    • (2004) Science , vol.305 , pp. 55-59
    • Stinchcombe, J.1    Bossi, G.2    Griffiths, G.M.3
  • 147
    • 0035655587 scopus 로고    scopus 로고
    • The immunological synapse of CTL contains a secretory domain and membrane bridges
    • Stinchcombe J.C., Bossi G., Booth S., and Griffiths G.M. The immunological synapse of CTL contains a secretory domain and membrane bridges. Immunity 15 (2001) 751-761
    • (2001) Immunity , vol.15 , pp. 751-761
    • Stinchcombe, J.C.1    Bossi, G.2    Booth, S.3    Griffiths, G.M.4
  • 148
    • 33749185296 scopus 로고    scopus 로고
    • Centrosome polarization delivers secretory granules to the immunological synapse
    • Stinchcombe J.C., Majorovits E., Bossi G., Fuller S., and Griffiths G.M. Centrosome polarization delivers secretory granules to the immunological synapse. Nature 443 (2006) 462-465
    • (2006) Nature , vol.443 , pp. 462-465
    • Stinchcombe, J.C.1    Majorovits, E.2    Bossi, G.3    Fuller, S.4    Griffiths, G.M.5
  • 149
  • 150
    • 33744913799 scopus 로고    scopus 로고
    • Regulation of microtubule formation in activated mast cells by complexes of {gamma}-tubulin with Fyn and Syk kinases
    • Sulimenko V., Draberova E., Sulimenko T., Macurek L., Richterova V., Draber P., and Draber P. Regulation of microtubule formation in activated mast cells by complexes of {gamma}-tubulin with Fyn and Syk kinases. J. Immunol. 176 (2006) 7243-7253
    • (2006) J. Immunol. , vol.176 , pp. 7243-7253
    • Sulimenko, V.1    Draberova, E.2    Sulimenko, T.3    Macurek, L.4    Richterova, V.5    Draber, P.6    Draber, P.7
  • 151
  • 152
    • 0029894198 scopus 로고    scopus 로고
    • The synaptic vesicle cycle: a single vesicle budding step involving clathrin and dynamin
    • Takei K., Mundigl O., Daniell L., and De C.P. The synaptic vesicle cycle: a single vesicle budding step involving clathrin and dynamin. J. Cell Biol. 133 (1996) 1237-1250
    • (1996) J. Cell Biol. , vol.133 , pp. 1237-1250
    • Takei, K.1    Mundigl, O.2    Daniell, L.3    De, C.P.4
  • 155
    • 0023008920 scopus 로고
    • Clathrin-coated vesicular transport of secretory proteins during the formation of ACTH-containing secretory granules in AtT20 cells
    • Tooze J., and Tooze S.A. Clathrin-coated vesicular transport of secretory proteins during the formation of ACTH-containing secretory granules in AtT20 cells. J. Cell Biol. 103 (1986) 839-850
    • (1986) J. Cell Biol. , vol.103 , pp. 839-850
    • Tooze, J.1    Tooze, S.A.2
  • 156
    • 0032516858 scopus 로고    scopus 로고
    • Biogenesis of secretory granules in the trans-Golgi network of neuroendocrine and endocrine cells
    • Tooze S.A. Biogenesis of secretory granules in the trans-Golgi network of neuroendocrine and endocrine cells. Biochim. Biophys. Acta 1404 (1998) 231-244
    • (1998) Biochim. Biophys. Acta , vol.1404 , pp. 231-244
    • Tooze, S.A.1
  • 157
    • 0242330147 scopus 로고    scopus 로고
    • Sorting it out: AP-2 and alternate clathrin adaptors in endocytic cargo selection
    • Traub L.M. Sorting it out: AP-2 and alternate clathrin adaptors in endocytic cargo selection. J. Cell Biol. 163 (2003) 203-208
    • (2003) J. Cell Biol. , vol.163 , pp. 203-208
    • Traub, L.M.1
  • 158
    • 20544465126 scopus 로고    scopus 로고
    • Common principles in clathrin-mediated sorting at the Golgi and the plasma membrane
    • Traub L.M. Common principles in clathrin-mediated sorting at the Golgi and the plasma membrane. Biochim. Biophys. Acta 1744 (2005) 415-437
    • (2005) Biochim. Biophys. Acta , vol.1744 , pp. 415-437
    • Traub, L.M.1
  • 162
    • 0035816668 scopus 로고    scopus 로고
    • The last exon of SNAP-23 regulates granule exocytosis from mast cells
    • Vaidyanathan V.V., Puri N., and Roche P.A. The last exon of SNAP-23 regulates granule exocytosis from mast cells. J. Biol. Chem. 276 (2001) 25101-25106
    • (2001) J. Biol. Chem. , vol.276 , pp. 25101-25106
    • Vaidyanathan, V.V.1    Puri, N.2    Roche, P.A.3
  • 165
    • 0035124102 scopus 로고    scopus 로고
    • Secretory granules of mast cells accumulate mature and immature MHC class II molecules
    • Vincent-Schneider H., Thery C., Mazzeo D., Tenza D., Raposo G., and Bonnerot C. Secretory granules of mast cells accumulate mature and immature MHC class II molecules. J. Cell Sci. 114 (2001) 323-334
    • (2001) J. Cell Sci. , vol.114 , pp. 323-334
    • Vincent-Schneider, H.1    Thery, C.2    Mazzeo, D.3    Tenza, D.4    Raposo, G.5    Bonnerot, C.6
  • 166
    • 0742288412 scopus 로고    scopus 로고
    • Functional dissection of the interactions of stonin 2 with the adaptor complex AP-2 and synaptotagmin
    • Walther K., Diril M.K., Jung N., and Haucke V. Functional dissection of the interactions of stonin 2 with the adaptor complex AP-2 and synaptotagmin. Proc. Natl. Acad. Sci. USA 101 (2004) 964-969
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 964-969
    • Walther, K.1    Diril, M.K.2    Jung, N.3    Haucke, V.4
  • 167
    • 32344432189 scopus 로고    scopus 로고
    • Assay and functional properties of Rab34 interaction with RILP in lysosome morphogenesis
    • Wang T., and Hong W. Assay and functional properties of Rab34 interaction with RILP in lysosome morphogenesis. Methods Enzymol. 403 (2005) 675-687
    • (2005) Methods Enzymol. , vol.403 , pp. 675-687
    • Wang, T.1    Hong, W.2
  • 168
    • 0034330540 scopus 로고    scopus 로고
    • Analysis of the lysosomal storage disease Chediak-Higashi syndrome
    • Ward D.M., Griffiths G.M., Stinchcombe J.C., and Kaplan J. Analysis of the lysosomal storage disease Chediak-Higashi syndrome. Traffic 1 (2000) 816-822
    • (2000) Traffic , vol.1 , pp. 816-822
    • Ward, D.M.1    Griffiths, G.M.2    Stinchcombe, J.C.3    Kaplan, J.4
  • 170
    • 34948901935 scopus 로고    scopus 로고
    • Differential targeting of secretory lysosomes and recycling endosomes in mast cells revealed by patterned antigen arrays
    • Wu M., Baumgart T., Hammond S., Holowka D., and Baird B. Differential targeting of secretory lysosomes and recycling endosomes in mast cells revealed by patterned antigen arrays. J. Cell Sci. 120 (2007) 3147-3154
    • (2007) J. Cell Sci. , vol.120 , pp. 3147-3154
    • Wu, M.1    Baumgart, T.2    Hammond, S.3    Holowka, D.4    Baird, B.5
  • 173
    • 0028168590 scopus 로고
    • Synaptotagmin I is a high affinity receptor for clathrin AP-2: implications for membrane recycling
    • Zhang J.Z., Davletov B.A., Sudhof T.C., and Anderson R.G. Synaptotagmin I is a high affinity receptor for clathrin AP-2: implications for membrane recycling. Cell 78 (1994) 751-760
    • (1994) Cell , vol.78 , pp. 751-760
    • Zhang, J.Z.1    Davletov, B.A.2    Sudhof, T.C.3    Anderson, R.G.4
  • 174
    • 0031843724 scopus 로고    scopus 로고
    • ADP-Ribosylation factor 1 transiently activates high-affinity adaptor protein complex AP-1 binding sites on Golgi membranes
    • Zhu Y., Traub L.M., and Kornfeld S. ADP-Ribosylation factor 1 transiently activates high-affinity adaptor protein complex AP-1 binding sites on Golgi membranes. Mol. Biol. Cell 9 (1998) 1323-1337
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1323-1337
    • Zhu, Y.1    Traub, L.M.2    Kornfeld, S.3
  • 175
    • 33846821720 scopus 로고    scopus 로고
    • Sorting of Fas ligand to secretory lysosomes is regulated by mono-ubiquitylation and phosphorylation
    • Zuccato E., Blott E.J., Holt O., Sigismund S., Shaw M., Bossi G., and Griffiths G.M. Sorting of Fas ligand to secretory lysosomes is regulated by mono-ubiquitylation and phosphorylation. J. Cell Sci. 120 (2007) 191-199
    • (2007) J. Cell Sci. , vol.120 , pp. 191-199
    • Zuccato, E.1    Blott, E.J.2    Holt, O.3    Sigismund, S.4    Shaw, M.5    Bossi, G.6    Griffiths, G.M.7


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