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Volumn 115, Issue 2, 2005, Pages 388-396

Rab27a mediates the tight docking of insulin granules onto the plasma membrane during glucose stimulation

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ION; GLUCOSE; INSULIN; PHORBOL ESTER; POTASSIUM ION; RAB27A PROTEIN; CARCINOGEN; FORSKOLIN; PHORBOL 13 ACETATE 12 MYRISTATE; POTASSIUM; RAB PROTEIN; RAB27A PROTEIN, MOUSE;

EID: 20144373742     PISSN: 00219738     EISSN: None     Source Type: Journal    
DOI: 10.1172/JCI200522955     Document Type: Article
Times cited : (148)

References (31)
  • 1
    • 1342310841 scopus 로고    scopus 로고
    • The roles of Rab27 and its effectors in the regulated secretory pathways
    • Izumi, T., Gomi, H., Kasai, K., Mizutani, S., and Torii, S. 2003. The roles of Rab27 and its effectors in the regulated secretory pathways. Cell Struct. Funct. 28:465-474.
    • (2003) Cell Struct. Funct. , vol.28 , pp. 465-474
    • Izumi, T.1    Gomi, H.2    Kasai, K.3    Mizutani, S.4    Torii, S.5
  • 2
    • 0346729920 scopus 로고    scopus 로고
    • A general role for Rab27a in secretory cells
    • Tolmachova, T., et al. 2004. A general role for Rab27a in secretory cells. Mol. Biol. Cell. 15:332-344.
    • (2004) Mol. Biol. Cell. , vol.15 , pp. 332-344
    • Tolmachova, T.1
  • 3
    • 0038050215 scopus 로고    scopus 로고
    • Regulated exocytosis and SNARE function
    • Söllner, T.H. 2003. Regulated exocytosis and SNARE function. Mol. Membr. Biol. 20:209-220.
    • (2003) Mol. Membr. Biol. , vol.20 , pp. 209-220
    • Söllner, T.H.1
  • 5
    • 0037165662 scopus 로고    scopus 로고
    • Melanophilin directly links Rab27a and myosin Va through its distinct coiled-coil regions
    • Nagashima, K., et al. 2002. Melanophilin directly links Rab27a and myosin Va through its distinct coiled-coil regions. FEBS Lett. 517:233-238.
    • (2002) FEBS Lett. , vol.517 , pp. 233-238
    • Nagashima, K.1
  • 6
    • 0037088641 scopus 로고    scopus 로고
    • The Slp homology domain of synaptotagmin-like proteins 1-4 and Slac2 functions as a novel Rab27A binding domain
    • Kuroda, T.S., Fukuda, M., Ariga, H., and Mikoshiba, K. 2002. The Slp homology domain of synaptotagmin-like proteins 1-4 and Slac2 functions as a novel Rab27A binding domain. J. Biol. Chem. 277:9212-9218.
    • (2002) J. Biol. Chem. , vol.277 , pp. 9212-9218
    • Kuroda, T.S.1    Fukuda, M.2    Ariga, H.3    Mikoshiba, K.4
  • 7
    • 0344002689 scopus 로고    scopus 로고
    • Mutations in RAB27A cause Griscelli syndrome associated with haemophagocytic syndrome
    • Ménasché, G., et al. 2000. Mutations in RAB27A cause Griscelli syndrome associated with haemophagocytic syndrome. Nat. Genet. 25:173-176.
    • (2000) Nat. Genet. , vol.25 , pp. 173-176
    • Ménasché, G.1
  • 8
    • 12944255844 scopus 로고    scopus 로고
    • A mutation in Rab27A causes the vesicle transport defects observed in ashen mice
    • Wilson, S.M., et al. 2000. A mutation in Rab27A causes the vesicle transport defects observed in ashen mice. Proc. Natl. Acad. Sci. U. S. A. 97:7933-7938.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 7933-7938
    • Wilson, S.M.1
  • 9
    • 0036181537 scopus 로고    scopus 로고
    • The Rab27a/granuphilin complex regulates the exocytosis of insulin-containing dense-core granules
    • Yi, Z., et al. 2002. The Rab27a/granuphilin complex regulates the exocytosis of insulin-containing dense-core granules. Mol. Cell. Biol. 22:1858-1867.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 1858-1867
    • Yi, Z.1
  • 10
    • 0033214974 scopus 로고    scopus 로고
    • Novel rabphilin-3-like protein associates with insulin-containing granules in pancreatic beta cells
    • Wang, J., Takeuchi, T., Yokota, H., and Izumi, T. 1999. Novel rabphilin-3-like protein associates with insulin-containing granules in pancreatic beta cells. J. Biol. Chem. 274:28542-28548.
    • (1999) J. Biol. Chem. , vol.274 , pp. 28542-28548
    • Wang, J.1    Takeuchi, T.2    Yokota, H.3    Izumi, T.4
  • 11
    • 0036314198 scopus 로고    scopus 로고
    • Granuphilin modulates the exocytosis of secretory granules through the interaction with syntaxin 1a
    • Torii, S., et al. 2002. Granuphilin modulates the exocytosis of secretory granules through the interaction with syntaxin 1a. Mol. Cell. Biol. 22:5518-5526.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 5518-5526
    • Torii, S.1
  • 12
    • 2542463861 scopus 로고    scopus 로고
    • Rab27 effector granuphilin promotes the plasma membrane targeting of insulin granules via interaction with syntaxin 1a
    • Torii, S., Takeuchi, T., Nagamatsu, S., and Izumi, T. 2004. Rab27 effector granuphilin promotes the plasma membrane targeting of insulin granules via interaction with syntaxin 1a. J. Biol. Chem. 279:22532-22538.
    • (2004) J. Biol. Chem. , vol.279 , pp. 22532-22538
    • Torii, S.1    Takeuchi, T.2    Nagamatsu, S.3    Izumi, T.4
  • 13
    • 0035911150 scopus 로고    scopus 로고
    • Defective granule exocytosis in Rab27a-deficient lymphocytes from ashen mice
    • Haddad, E.K., Wu, X., Hammer, J.A., III, and Henkart, P.A. 2001. Defective granule exocytosis in Rab27a-deficient lymphocytes from ashen mice. J. Cell Biol. 152:835-841.
    • (2001) J. Cell Biol. , vol.152 , pp. 835-841
    • Haddad, E.K.1    Wu, X.2    Hammer III, J.A.3    Henkart, P.A.4
  • 14
    • 0035911160 scopus 로고    scopus 로고
    • Rab27a is required for regulated secretion in cytotoxic T lymphocytes
    • Stinchcombe, J.C., et al. 2001. Rab27a is required for regulated secretion in cytotoxic T lymphocytes. J. Cell Biol. 152:825-833.
    • (2001) J. Cell Biol. , vol.152 , pp. 825-833
    • Stinchcombe, J.C.1
  • 15
    • 0036073806 scopus 로고    scopus 로고
    • Functional redundancy of Rab27 proteins and the pathogenesis of Griscelli syndrome
    • doi:10.1172/JCI200215058
    • Barral, D.C., et al. 2002. Functional redundancy of Rab27 proteins and the pathogenesis of Griscelli syndrome. J. Clin. Invest. 110:247-257. doi:10.1172/JCI200215058.
    • (2002) J. Clin. Invest. , vol.110 , pp. 247-257
    • Barral, D.C.1
  • 16
    • 0036230738 scopus 로고    scopus 로고
    • Involvement of Rab27b in the regulated secretion of pituitary hormones
    • Zhao, S., Torii, S., Yokota-Hashimoto, H., Takeuchi, T., and Izumi, T. 2002. Involvement of Rab27b in the regulated secretion of pituitary hormones. Endocrinology. 143:1817-1824.
    • (2002) Endocrinology , vol.143 , pp. 1817-1824
    • Zhao, S.1    Torii, S.2    Yokota-Hashimoto, H.3    Takeuchi, T.4    Izumi, T.5
  • 17
    • 0036226156 scopus 로고    scopus 로고
    • Identification of an organelle receptor for myosin-Va
    • Wu, X.S., et al. 2002. Identification of an organelle receptor for myosin-Va. Nat. Cell Biol. 4:271-278.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 271-278
    • Wu, X.S.1
  • 18
    • 0032954066 scopus 로고    scopus 로고
    • Genetic analysis of obese diabetes in the TSOD mouse
    • Hirayama, I., et al. 1999. Genetic analysis of obese diabetes in the TSOD mouse. Diabetes. 48:1183-1191.
    • (1999) Diabetes , vol.48 , pp. 1183-1191
    • Hirayama, I.1
  • 20
    • 0033760442 scopus 로고    scopus 로고
    • Triggering and amplifying pathways of regulation of insulin secretion by glucose
    • Henquin, J.-C. 2000. Triggering and amplifying pathways of regulation of insulin secretion by glucose. Diabetes. 49:1751-1760.
    • (2000) Diabetes , vol.49 , pp. 1751-1760
    • Henquin, J.-C.1
  • 21
    • 0037162886 scopus 로고    scopus 로고
    • Fusion pore dynamics and insulin granule exocytosis in the pancreatic islet
    • Takahashi, N., Kishimoto, T., Nemoto, T., Kadowaki, T., and Kasai, H. 2002. Fusion pore dynamics and insulin granule exocytosis in the pancreatic islet. Science. 297:1349-1352.
    • (2002) Science , vol.297 , pp. 1349-1352
    • Takahashi, N.1    Kishimoto, T.2    Nemoto, T.3    Kadowaki, T.4    Kasai, H.5
  • 22
    • 0035315984 scopus 로고    scopus 로고
    • A real-time view of life within 100 nm of the plasma membrane
    • Steyer, J.A., and Almers, W. 2001. A real-time view of life within 100 nm of the plasma membrane. Nat. Rev. Mol. Cell Biol. 2:268-276.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 268-276
    • Steyer, J.A.1    Almers, W.2
  • 23
    • 3142758492 scopus 로고    scopus 로고
    • TIRF imaging of docking and fusion of single insulin granule motion in primary rat pancreatic β-cells: Different behaviour of granule motion between normal and Goto-Kakizaki diabetic rat β-cells
    • Ohara-Imaizumi, M., et al. 2004. TIRF imaging of docking and fusion of single insulin granule motion in primary rat pancreatic β-cells: different behaviour of granule motion between normal and Goto-Kakizaki diabetic rat β-cells. Biochem. J. 381:13-18.
    • (2004) Biochem. J. , vol.381 , pp. 13-18
    • Ohara-Imaizumi, M.1
  • 24
    • 0036261251 scopus 로고    scopus 로고
    • Fast insulin secretion reflects exocytosis of docked granules in mouse pancreatic B-cells
    • Olofsson, C.S., et al. 2002. Fast insulin secretion reflects exocytosis of docked granules in mouse pancreatic B-cells. Pflügers Arch. 444:43-51.
    • (2002) Pflügers Arch. , vol.444 , pp. 43-51
    • Olofsson, C.S.1
  • 25
    • 0027364502 scopus 로고
    • Synaptic vesicle fusion complex contains unc-18 homologue bound to syntaxin
    • Hata, Y., Slaughter, C.A., and Südhof, T.C. 1993. Synaptic vesicle fusion complex contains unc-18 homologue bound to syntaxin. Nature. 366:347-351.
    • (1993) Nature , vol.366 , pp. 347-351
    • Hata, Y.1    Slaughter, C.A.2    Südhof, T.C.3
  • 26
    • 0030855088 scopus 로고    scopus 로고
    • Transport, docking and exocytosis of single secretory granules in live chromaffin cells
    • Steyer, J.A., Horstmann, H., and Almers, W. 1997. Transport, docking and exocytosis of single secretory granules in live chromaffin cells. Nature. 388:474-478.
    • (1997) Nature , vol.388 , pp. 474-478
    • Steyer, J.A.1    Horstmann, H.2    Almers, W.3
  • 27
    • 0031425428 scopus 로고    scopus 로고
    • Ultrastructural organization of bovine chromaffin cell cortex: Analysis by cryofixation and morphometry of aspects pertinent to exocytosis
    • Plattner, H., Artalejo, A.R., and Neher, E. 1997. Ultrastructural organization of bovine chromaffin cell cortex: analysis by cryofixation and morphometry of aspects pertinent to exocytosis. J. Cell Biol. 139:1709-1717.
    • (1997) J. Cell Biol. , vol.139 , pp. 1709-1717
    • Plattner, H.1    Artalejo, A.R.2    Neher, E.3
  • 28
    • 0038303159 scopus 로고    scopus 로고
    • Phosphatidylinositol 4-kinase serves as a metabolic sensor and regulates priming of secretory granules in pancreatic β cells
    • Olsen, H.L., et al. 2003. Phosphatidylinositol 4-kinase serves as a metabolic sensor and regulates priming of secretory granules in pancreatic β cells. Proc. Natl. Acad. Sci. U. S. A. 100:5187-5192.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 5187-5192
    • Olsen, H.L.1
  • 29
    • 1542319211 scopus 로고    scopus 로고
    • Site of docking and fusion of insulin secretory granules in live MIN6 β cells analyzed by TAT-conjugated anti-syntaxin 1 antibody and total internal reflection fluorescence microscopy
    • Ohara-Imaizumi, M., et al. 2004. Site of docking and fusion of insulin secretory granules in live MIN6 β cells analyzed by TAT-conjugated anti-syntaxin 1 antibody and total internal reflection fluorescence microscopy. J. Biol. Chem. 279:8403-8408.
    • (2004) J. Biol. Chem. , vol.279 , pp. 8403-8408
    • Ohara-Imaizumi, M.1
  • 30
    • 0028032845 scopus 로고
    • Partial albinism with immunodeficiency (Griscelli syndrome)
    • Klein, C., et al. 1994. Partial albinism with immunodeficiency (Griscelli syndrome). J. Pediatr. 125:886-895.
    • (1994) J. Pediatr. , vol.125 , pp. 886-895
    • Klein, C.1
  • 31
    • 0037312881 scopus 로고    scopus 로고
    • Dominant negative pathogenesis by mutant proinsulin in the Akita diabetic mouse
    • Izumi, T., et al. 2003. Dominant negative pathogenesis by mutant proinsulin in the Akita diabetic mouse. Diabetes. 52:409-416.
    • (2003) Diabetes , vol.52 , pp. 409-416
    • Izumi, T.1


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