메뉴 건너뛰기




Volumn 182, Issue , 2014, Pages 29-37

The C2 domains of Granuphilin are high-affinity sensors for plasma membrane lipids

Author keywords

Inositol polyphosphate signaling; Insulin secretion; Phosphatidylinositol (4,5) bisphosphate; Protein lipid interaction; Secretory granule docking; Slp4

Indexed keywords

GRANUPHILIN; INOSITOL; INOSITOL DERIVATIVE; LIPOSOME; MEMBRANE LIPID; PHOSPHATIDYLINOSITOL; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE; RAB PROTEIN; SYNAPTOTAGMIN; UNCLASSIFIED DRUG; INSULIN; PHOSPHATIDYLINOSITOL 3,4,5-TRIPHOSPHATE; PHYTIC ACID; POLYPHOSPHOINOSITIDE; PROTEIN BINDING; SYTL4 PROTEIN, HUMAN; VESICULAR TRANSPORT PROTEIN;

EID: 84905169006     PISSN: 00093084     EISSN: 18732941     Source Type: Journal    
DOI: 10.1016/j.chemphyslip.2013.10.009     Document Type: Article
Times cited : (15)

References (48)
  • 1
    • 21044443928 scopus 로고    scopus 로고
    • Inositol-lipid binding motifs: Signal integrators through protein-lipid and protein-protein interactions
    • DOI 10.1242/jcs.02387
    • T. Balla Inositol-lipid binding motifs: signal integrators through protein-lipid and protein-protein interactions J. Cell Sci. 118 2005 2093 2104 (Pubitemid 40872833)
    • (2005) Journal of Cell Science , vol.118 , Issue.10 , pp. 2093-2104
    • Balla, T.1
  • 2
    • 51349151673 scopus 로고    scopus 로고
    • A key role for phosphorylated inositol compounds in pancreatic beta-cell stimulus-secretion coupling
    • P.O. Berggren, and C.J. Barker A key role for phosphorylated inositol compounds in pancreatic beta-cell stimulus-secretion coupling Adv. Enzyme Regul. 48 2008 276 294
    • (2008) Adv. Enzyme Regul. , vol.48 , pp. 276-294
    • Berggren, P.O.1    Barker, C.J.2
  • 3
    • 52049100831 scopus 로고    scopus 로고
    • Analysis of the synaptotagmin family during reconstituted membrane fusion. Uncovering a class of inhibitory isoforms
    • A. Bhalla, M.C. Chicka, and E.R. Chapman Analysis of the synaptotagmin family during reconstituted membrane fusion. Uncovering a class of inhibitory isoforms J. Biol. Chem. 283 2008 21799 21807
    • (2008) J. Biol. Chem. , vol.283 , pp. 21799-21807
    • Bhalla, A.1    Chicka, M.C.2    Chapman, E.R.3
  • 5
    • 84867077527 scopus 로고    scopus 로고
    • Hydrophobic contributions to the membrane docking of synaptotagmin 7 C2A domain: Mechanistic contrast between isoforms 1 and 7
    • D.S. Brandt, M.D. Coffman, J.J. Falke, and J.D. Knight Hydrophobic contributions to the membrane docking of synaptotagmin 7 C2A domain: mechanistic contrast between isoforms 1 and 7 Biochemistry 51 2012 7654 7664
    • (2012) Biochemistry , vol.51 , pp. 7654-7664
    • Brandt, D.S.1    Coffman, M.D.2    Falke, J.J.3    Knight, J.D.4
  • 6
    • 20544475665 scopus 로고    scopus 로고
    • Membrane-protein interactions in cell signaling and membrane trafficking
    • DOI 10.1146/annurev.biophys.33.110502.133337
    • W. Cho, and R.V. Stahelin Membrane-protein interactions in cell signaling and membrane trafficking Annu. Rev. Biophys. Biomol. Struct. 34 2005 119 151 (Pubitemid 40847721)
    • (2005) Annual Review of Biophysics and Biomolecular Structure , vol.34 , pp. 119-151
    • Cho, W.1    Stahelin, R.V.2
  • 9
    • 11144292734 scopus 로고    scopus 로고
    • GRP1 Pleckstrin homology domain: Activation parameters and novel search mechanism for rare target lipid
    • DOI 10.1021/bi049017a
    • J.A. Corbin, R.A. Dirkx, and J.J. Falke GRP1 pleckstrin homology domain: Activation parameters and novel search mechanism for rare target lipid Biochemistry 43 2004 16161 16173 (Pubitemid 40041029)
    • (2004) Biochemistry , vol.43 , Issue.51 , pp. 16161-16173
    • Corbin, J.A.1    Dirkx, R.A.2    Falke, J.J.3
  • 11
    • 33749836234 scopus 로고    scopus 로고
    • Phosphoinositides in cell regulation and membrane dynamics
    • DOI 10.1038/nature05185, PII NATURE05185
    • G. Di Paolo, and P. De Camilli Phosphoinositides in cell regulation and membrane dynamics Nature 443 2006 651 657 (Pubitemid 44564702)
    • (2006) Nature , vol.443 , Issue.7112 , pp. 651-657
    • Di Paolo, G.1    De Camilli, P.2
  • 13
    • 33751290691 scopus 로고    scopus 로고
    • Rab27 and its effectors in secretory granule exocytosis: A novel docking machinery composed of a Rab27 · effector complex
    • DOI 10.1042/BST0340691
    • M. Fukuda Rab27 and its effectors in secretory granule exocytosis: a novel docking machinery composed of a Rab27.effector complex Biochem. Soc. Trans. 34 2006 691 695 (Pubitemid 44796400)
    • (2006) Biochemical Society Transactions , vol.34 , Issue.5 , pp. 691-695
    • Fukuda, M.1
  • 14
    • 0034805325 scopus 로고    scopus 로고
    • Synaptotagmin-like protein 1-3: A novel family of c-terminal-type tandem c2 proteins
    • DOI 10.1006/bbrc.2001.4512
    • M. Fukuda, and K. Mikoshiba Synaptotagmin-like protein 1-3: a novel family of C-terminal-type tandem C2 proteins Biochem. Biophys. Res. Commun. 281 2001 1226 1233 (Pubitemid 32924550)
    • (2001) Biochemical and Biophysical Research Communications , vol.281 , Issue.5 , pp. 1226-1233
    • Fukuda, M.1    Mikoshiba, K.2
  • 16
    • 26444479437 scopus 로고    scopus 로고
    • Granuphilin molecularly docks insulin granules to the fusion machinery
    • DOI 10.1083/jcb.200505179
    • H. Gomi, S. Mizutani, K. Kasai, S. Itohara, and T. Izumi Granuphilin molecularly docks insulin granules to the fusion machinery J. Cell Biol. 171 2005 99 109 (Pubitemid 41434605)
    • (2005) Journal of Cell Biology , vol.171 , Issue.1 , pp. 99-109
    • Gomi, H.1    Mizutani, S.2    Kasai, K.3    Itohara, S.4    Izumi, T.5
  • 17
    • 70349560095 scopus 로고    scopus 로고
    • Calcium-sensing beyond neurotransmitters: Functions of synaptotagmins in neuroendocrine and endocrine secretion
    • N. Gustavsson, and W. Han Calcium-sensing beyond neurotransmitters: functions of synaptotagmins in neuroendocrine and endocrine secretion Biosci. Rep. 29 2009 245 259
    • (2009) Biosci. Rep. , vol.29 , pp. 245-259
    • Gustavsson, N.1    Han, W.2
  • 18
    • 17044369192 scopus 로고    scopus 로고
    • Three distinct kinetic groupings of the synaptotagmin family: Candidate sensors for rapid and delayed exocytosis
    • E. Hui, J. Bai, P. Wang, M. Sugimori, R.R. Llinas, and E.R. Chapman Three distinct kinetic groupings of the synaptotagmin family: candidate sensors for rapid and delayed exocytosis Proc. Natl. Acad. Sci. U. S. A. 102 2005 5210 5214
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 5210-5214
    • Hui, E.1    Bai, J.2    Wang, P.3    Sugimori, M.4    Llinas, R.R.5    Chapman, E.R.6
  • 20
    • 79955039913 scopus 로고    scopus 로고
    • Heterogeneous modes of insulin granule exocytosis: Molecular determinants
    • T. Izumi Heterogeneous modes of insulin granule exocytosis: molecular determinants Front. Biosci. 16 2011 360 367
    • (2011) Front. Biosci. , vol.16 , pp. 360-367
    • Izumi, T.1
  • 22
    • 58849094579 scopus 로고    scopus 로고
    • Single-molecule fluorescence studies of a PH domain: New insights into the membrane docking reaction
    • J.D. Knight, and J.J. Falke Single-molecule fluorescence studies of a PH domain: new insights into the membrane docking reaction Biophys. J. 96 2009 566 582
    • (2009) Biophys. J. , vol.96 , pp. 566-582
    • Knight, J.D.1    Falke, J.J.2
  • 23
    • 56749168073 scopus 로고    scopus 로고
    • Molecular mechanism of an oncogenic mutation that alters membrane targeting: Glu17Lys modifies the PIP lipid specificity of the AKT1 PH domain
    • K.E. Landgraf, C. Pilling, and J.J. Falke Molecular mechanism of an oncogenic mutation that alters membrane targeting: Glu17Lys modifies the PIP lipid specificity of the AKT1 PH domain Biochemistry 47 2008 12260 12269
    • (2008) Biochemistry , vol.47 , pp. 12260-12269
    • Landgraf, K.E.1    Pilling, C.2    Falke, J.J.3
  • 25
    • 38549092474 scopus 로고    scopus 로고
    • Membrane recognition by phospholipid-binding domains
    • DOI 10.1038/nrm2328, PII NRM2328
    • M.A. Lemmon Membrane recognition by phospholipid-binding domains Nat. Rev. Mol. Cell Biol. 9 2008 99 111 (Pubitemid 351158910)
    • (2008) Nature Reviews Molecular Cell Biology , vol.9 , Issue.2 , pp. 99-111
    • Lemmon, M.A.1
  • 27
    • 76449120031 scopus 로고    scopus 로고
    • Role of C2 domain proteins during synaptic vesicle exocytosis
    • S. Martens Role of C2 domain proteins during synaptic vesicle exocytosis Biochem. Soc. Trans. 38 2010 213 216
    • (2010) Biochem. Soc. Trans. , vol.38 , pp. 213-216
    • Martens, S.1
  • 28
    • 0036161583 scopus 로고    scopus 로고
    • Electrostatic control of the membrane targeting of C2 domains
    • DOI 10.1016/S1097-2765(01)00426-9
    • D. Murray, and B. Honig Electrostatic control of the membrane targeting of C2 domains Mol. Cell 9 2002 145 154 (Pubitemid 34127778)
    • (2002) Molecular Cell , vol.9 , Issue.1 , pp. 145-154
    • Murray, D.1    Honig, B.2
  • 29
    • 0030467967 scopus 로고    scopus 로고
    • The C2 domain calcium-binding motif: Structural and functional diversity
    • E.A. Nalefski, and J.J. Falke The C2 domain calcium-binding motif: structural and functional diversity Protein Sci. 5 1996 2375 2390 (Pubitemid 26424851)
    • (1996) Protein Science , vol.5 , Issue.12 , pp. 2375-2390
    • Nalefski, E.A.1    Falke, J.J.2
  • 31
    • 0030612437 scopus 로고    scopus 로고
    • 2+-signaling cycle of a membrane-docking C2 domain
    • DOI 10.1021/bi9717340
    • 2+-signaling cycle of a membrane-docking C2 domain Biochemistry 36 1997 12011 12018 (Pubitemid 27440938)
    • (1997) Biochemistry , vol.36 , Issue.40 , pp. 12011-12018
    • Nalefski, E.A.1    Slazas, M.M.2    Falke, J.J.3
  • 33
    • 70350025513 scopus 로고    scopus 로고
    • 2+ affinity of synaptotagmin 1 is markedly increased by a specific interaction of its C2B domain with phosphatidylinositol 4,5-bisphosphate
    • 2+ affinity of synaptotagmin 1 is markedly increased by a specific interaction of its C2B domain with phosphatidylinositol 4,5-bisphosphate J. Biol. Chem. 284 2009 25749 25760
    • (2009) J. Biol. Chem. , vol.284 , pp. 25749-25760
    • Radhakrishnan, A.1    Stein, A.2    Jahn, R.3    Fasshauer, D.4
  • 34
    • 43749112983 scopus 로고    scopus 로고
    • Crystal structure of lactadherin C2 domain at 1.7 Å resolution with mutational and computational analyses of its membrane-binding motif
    • C. Shao, V.A. Novakovic, J.F. Head, B.A. Seaton, and G.E. Gilbert Crystal structure of lactadherin C2 domain at 1.7 Å resolution with mutational and computational analyses of its membrane-binding motif J. Biol. Chem. 283 2008 7230 7241
    • (2008) J. Biol. Chem. , vol.283 , pp. 7230-7241
    • Shao, C.1    Novakovic, V.A.2    Head, J.F.3    Seaton, B.A.4    Gilbert, G.E.5
  • 35
    • 0037040890 scopus 로고    scopus 로고
    • Synaptotagmins: Why so many
    • T.C. Sudhof Synaptotagmins: why so many J. Biol. Chem. 277 2002 7629 7632
    • (2002) J. Biol. Chem. , vol.277 , pp. 7629-7632
    • Sudhof, T.C.1
  • 36
    • 0031565953 scopus 로고    scopus 로고
    • Distinct specificity in the binding of inositol phosphates by pleckstrin homology domains of pleckstrin, RAC-protein kinase, diacylglycerol kinase and a new 130 kDa protein
    • DOI 10.1016/S0167-4889(97)00109-2, PII S0167488997001092
    • H. Takeuchi, T. Kanematsu, Y. Misumi, F. Sakane, H. Konishi, U. Kikkawa, Y. Watanabe, M. Katan, and M. Hirata Distinct specificity in the binding of inositol phosphates by pleckstrin homology domains of pleckstrin, RAC-protein kinase, diacylglycerol kinase and a new 130 kDa protein Biochim. Biophys. Acta 1359 1997 275 285 (Pubitemid 28027125)
    • (1997) Biochimica et Biophysica Acta - Molecular Cell Research , vol.1359 , Issue.3 , pp. 275-285
    • Takeuchi, H.1    Kanematsu, T.2    Misumi, Y.3    Sakane, F.4    Konishi, H.5    Kikkawa, U.6    Watanabe, Y.7    Katan, M.8    Hirata, M.9
  • 37
    • 33847395452 scopus 로고    scopus 로고
    • 2+ and the ATP-to-ADP ratio
    • DOI 10.2337/db06-0843
    • 2+ and the ATP-to-ADP ratio Diabetes 56 2007 818 826 (Pubitemid 46348456)
    • (2007) Diabetes , vol.56 , Issue.3 , pp. 818-826
    • Thore, S.1    Wuttke, A.2    Tengholm, A.3
  • 38
    • 41849102063 scopus 로고    scopus 로고
    • Munc 18-1 and granuphilin collaborate during insulin granule exocytosis
    • DOI 10.1111/j.1600-0854.2008.00709.x
    • A. Tomas, P. Meda, R. Regazzi, J.E. Pessin, and P.A. Halban Munc 18-1 and granuphilin collaborate during insulin granule exocytosis Traffic 9 2008 813 832 (Pubitemid 351494309)
    • (2008) Traffic , vol.9 , Issue.5 , pp. 813-832
    • Tomas, A.1    Meda, P.2    Regazzi, R.3    Pessin, J.E.4    Halban, P.A.5
  • 39
    • 2542463861 scopus 로고    scopus 로고
    • Rab27 effector granuphilin promotes the plasma membrane targeting of insulin granules via interaction with syntaxin 1a
    • DOI 10.1074/jbc.M400600200
    • S. Torii, T. Takeuchi, S. Nagamatsu, and T. Izumi Rab27 effector granuphilin promotes the plasma membrane targeting of insulin granules via interaction with syntaxin 1a J. Biol. Chem. 279 2004 22532 22538 (Pubitemid 38679453)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.21 , pp. 22532-22538
    • Torii, S.1    Takeuchi, T.2    Nagamatsu, S.3    Izumi, T.4
  • 40
    • 58149484915 scopus 로고    scopus 로고
    • Molecular mechanism of attachment process of dense-core vesicles to the plasma membrane in neuroendocrine cells
    • T. Tsuboi Molecular mechanism of attachment process of dense-core vesicles to the plasma membrane in neuroendocrine cells Neurosci. Res. 63 2009 83 88
    • (2009) Neurosci. Res. , vol.63 , pp. 83-88
    • Tsuboi, T.1
  • 41
    • 33745761013 scopus 로고    scopus 로고
    • The Slp4-a linker domain controls exocytosis through interaction with Munc18-1·syntaxin-1a complex
    • DOI 10.1091/mbc.E05-11-1047
    • T. Tsuboi, and M. Fukuda The Slp4-a linker domain controls exocytosis through interaction with Munc18-1.syntaxin-1a complex Mol. Biol. Cell 17 2006 2101 2112 (Pubitemid 44011727)
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.5 , pp. 2101-2112
    • Tsuboi, T.1    Fukuda, M.2
  • 43
    • 82055202917 scopus 로고    scopus 로고
    • Lipid assembly into cell membranes
    • D.E. Vance, J.E. Vance, 5th ed. Elsevier Amsterdam
    • D.R. Voelker Lipid assembly into cell membranes D.E. Vance, J.E. Vance, Biochemistry of Lipids, Lipoproteins and Membranes 5th ed. 2008 Elsevier Amsterdam 441 484
    • (2008) Biochemistry of Lipids, Lipoproteins and Membranes , pp. 441-484
    • Voelker, D.R.1
  • 44
    • 84873332366 scopus 로고    scopus 로고
    • The Rab27a effector exophilin7 promotes fusion of secretory granules that have not been docked to the plasma membrane
    • H. Wang, R. Ishizaki, J. Xu, K. Kasai, E. Kobayashi, H. Gomi, and T. Izumi The Rab27a effector exophilin7 promotes fusion of secretory granules that have not been docked to the plasma membrane Mol. Biol. Cell 24 2013 319 330
    • (2013) Mol. Biol. Cell , vol.24 , pp. 319-330
    • Wang, H.1    Ishizaki, R.2    Xu, J.3    Kasai, K.4    Kobayashi, E.5    Gomi, H.6    Izumi, T.7
  • 45
    • 0033214974 scopus 로고    scopus 로고
    • Novel rabphilin-3-like protein associates with insulin-containing granules in pancreatic beta cells
    • J. Wang, T. Takeuchi, H. Yokota, and T. Izumi Novel rabphilin-3-like protein associates with insulin-containing granules in pancreatic beta cells J. Biol. Chem. 274 1999 28542 28548 (Pubitemid 129504725)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.40 , pp. 28542-28548
    • Wang, J.1    Takeuchi, T.2    Yokota, H.3    Izumi, T.4
  • 47


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.