메뉴 건너뛰기




Volumn 355, Issue 1, 2006, Pages 8-18

Application of phosphoinositide-binding domains for the detection and quantification of specific phosphoinositides

Author keywords

ELISA; FYVE finger domain; Phosphoinositide; PI 3 kinase; Pleckstrin homology domain; PTEN

Indexed keywords

CONTROLLED DRUG DELIVERY; DIAGNOSIS; ENZYME IMMOBILIZATION; LIPOSOMES; MAMMALS; METABOLISM; PHOSPHATASES; PHOSPHOLIPIDS;

EID: 33745926546     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2006.05.014     Document Type: Article
Times cited : (28)

References (35)
  • 1
    • 0036015164 scopus 로고    scopus 로고
    • Phosphoinositide-binding domains: functional units for temporal and spatial regulation of intracellular signalling
    • Itoh T., and Takenawa T. Phosphoinositide-binding domains: functional units for temporal and spatial regulation of intracellular signalling. Cell. Signal. 14 (2002) 733-743
    • (2002) Cell. Signal. , vol.14 , pp. 733-743
    • Itoh, T.1    Takenawa, T.2
  • 2
    • 0038650888 scopus 로고    scopus 로고
    • Dynamics of phosphoinositides in membrane retrieval and insertion
    • Czech M.P. Dynamics of phosphoinositides in membrane retrieval and insertion. Annu. Rev. Physiol. 65 (2003) 791-815
    • (2003) Annu. Rev. Physiol. , vol.65 , pp. 791-815
    • Czech, M.P.1
  • 3
    • 0038281249 scopus 로고    scopus 로고
    • Phosphoinositide recognition domains
    • Lemmon M.A. Phosphoinositide recognition domains. Traffic 4 (2003) 201-213
    • (2003) Traffic , vol.4 , pp. 201-213
    • Lemmon, M.A.1
  • 4
    • 0035975965 scopus 로고    scopus 로고
    • Modular phosphoinositide-binding domains-their role in signalling and membrane trafficking
    • Cullen P.J., Cozier G.E., Banting G., and Mellor H. Modular phosphoinositide-binding domains-their role in signalling and membrane trafficking. Curr. Biol. 11 (2001) R882-R893
    • (2001) Curr. Biol. , vol.11
    • Cullen, P.J.1    Cozier, G.E.2    Banting, G.3    Mellor, H.4
  • 5
    • 0035980759 scopus 로고    scopus 로고
    • Phosphoinositides, key molecules for regulation of actin cytoskeletal organization and membrane traffic from the plasma membrane
    • Takenawa T., and Itoh T. Phosphoinositides, key molecules for regulation of actin cytoskeletal organization and membrane traffic from the plasma membrane. Biochim. Biophys. Acta 1533 (2001) 190-206
    • (2001) Biochim. Biophys. Acta , vol.1533 , pp. 190-206
    • Takenawa, T.1    Itoh, T.2
  • 8
    • 0035134328 scopus 로고    scopus 로고
    • Role of the ENTH domain in phosphatidylinositol-4,5-bisphosphate binding and endocytosis
    • Itoh T., Koshiba S., Kigawa T., Kikuchi A., Yokoyama S., and Takenawa T. Role of the ENTH domain in phosphatidylinositol-4,5-bisphosphate binding and endocytosis. Science 291 (2001) 1047-1051
    • (2001) Science , vol.291 , pp. 1047-1051
    • Itoh, T.1    Koshiba, S.2    Kigawa, T.3    Kikuchi, A.4    Yokoyama, S.5    Takenawa, T.6
  • 9
    • 0035871081 scopus 로고    scopus 로고
    • Cellular functions of phosphatidylinositol 3-phosphate and FYVE domain proteins
    • Gillooly D.J., Simonsen A., and Stenmark H. Cellular functions of phosphatidylinositol 3-phosphate and FYVE domain proteins. Biochem. J. 355 (2001) 249-258
    • (2001) Biochem. J. , vol.355 , pp. 249-258
    • Gillooly, D.J.1    Simonsen, A.2    Stenmark, H.3
  • 10
    • 0034283003 scopus 로고    scopus 로고
    • Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domain
    • Hamada K., Shimizu T., Matsui T., Tsukita S., and Hakoshima T. Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domain. EMBO J. 19 (2000) 4449-4462
    • (2000) EMBO J. , vol.19 , pp. 4449-4462
    • Hamada, K.1    Shimizu, T.2    Matsui, T.3    Tsukita, S.4    Hakoshima, T.5
  • 11
    • 0034306454 scopus 로고    scopus 로고
    • GRAM, a novel domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins
    • Doerks T., Strauss M., Brendel M., and Bork P. GRAM, a novel domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins. Trends Biochem. Sci. 25 (2000) 483-485
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 483-485
    • Doerks, T.1    Strauss, M.2    Brendel, M.3    Bork, P.4
  • 12
    • 0032547744 scopus 로고    scopus 로고
    • Visualization of phosphoinositides that bind pleckstrin homology domains: calcium- and agonist-induced dynamic changes and relationship to myo-[3H]inositol-labeled phosphoinositide pools
    • Varnai P., and Balla T. Visualization of phosphoinositides that bind pleckstrin homology domains: calcium- and agonist-induced dynamic changes and relationship to myo-[3H]inositol-labeled phosphoinositide pools. J. Cell Biol. 143 (1998) 501-510
    • (1998) J. Cell Biol. , vol.143 , pp. 501-510
    • Varnai, P.1    Balla, T.2
  • 13
    • 0033572662 scopus 로고    scopus 로고
    • The pleckstrin homology domains of protein kinase B and GRP1 (general receptor for phosphoinositides-1) are sensitive and selective probes for the cellular detection of phosphatidylinositol 3,4-bisphosphate and/or phosphatidylinositol 3,4,5-trisphosphate in vivo
    • Gray A., Van Der Kaay J., and Downes C.P. The pleckstrin homology domains of protein kinase B and GRP1 (general receptor for phosphoinositides-1) are sensitive and selective probes for the cellular detection of phosphatidylinositol 3,4-bisphosphate and/or phosphatidylinositol 3,4,5-trisphosphate in vivo. Biochem. J. 344 Pt 3 (1999) 929-936
    • (1999) Biochem. J. , vol.344 PART 3 , pp. 929-936
    • Gray, A.1    Van Der Kaay, J.2    Downes, C.P.3
  • 15
    • 0034306455 scopus 로고    scopus 로고
    • Identification of pleckstrin-homology-domain-containing proteins with novel phosphoinositide-binding specificities
    • Dowler S., Currie R.A., Campbell D.G., Deak M., Kular G., Downes C.P., and Alessi D.R. Identification of pleckstrin-homology-domain-containing proteins with novel phosphoinositide-binding specificities. Biochem. J. 351 (2000) 19-31
    • (2000) Biochem. J. , vol.351 , pp. 19-31
    • Dowler, S.1    Currie, R.A.2    Campbell, D.G.3    Deak, M.4    Kular, G.5    Downes, C.P.6    Alessi, D.R.7
  • 16
    • 0142027784 scopus 로고    scopus 로고
    • Membrane association of myotubularin-related protein 2 is mediated by a pleckstrin homology-GRAM domain and a coiled-coil dimerization module
    • Berger P., Schaffitzel C., Berger I., Ban N., and Suter U. Membrane association of myotubularin-related protein 2 is mediated by a pleckstrin homology-GRAM domain and a coiled-coil dimerization module. Proc. Natl. Acad. Sci. USA 100 (2003) 12177-12182
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 12177-12182
    • Berger, P.1    Schaffitzel, C.2    Berger, I.3    Ban, N.4    Suter, U.5
  • 17
    • 1842690628 scopus 로고    scopus 로고
    • Myotubularin regulates the function of the late endosome through the gram domain-phosphatidylinositol 3,5-bisphosphate interaction
    • Tsujita K., Itoh T., Ijuin T., Yamamoto A., Shisheva A., Laporte J., and Takenawa T. Myotubularin regulates the function of the late endosome through the gram domain-phosphatidylinositol 3,5-bisphosphate interaction. J. Biol. Chem. 279 (2004) 13817-13824
    • (2004) J. Biol. Chem. , vol.279 , pp. 13817-13824
    • Tsujita, K.1    Itoh, T.2    Ijuin, T.3    Yamamoto, A.4    Shisheva, A.5    Laporte, J.6    Takenawa, T.7
  • 19
    • 0033551070 scopus 로고    scopus 로고
    • New insights into tumor suppression: PTEN suppresses tumor formation by restraining the phosphoinositide 3-kinase/AKT pathway
    • Cantley L.C., and Neel B.G. New insights into tumor suppression: PTEN suppresses tumor formation by restraining the phosphoinositide 3-kinase/AKT pathway. Proc. Natl. Acad. Sci. USA 96 (1999) 4240-4245
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 4240-4245
    • Cantley, L.C.1    Neel, B.G.2
  • 20
    • 0036181869 scopus 로고    scopus 로고
    • PTEN: the down side of PI 3-kinase signalling
    • Leslie N.R., and Downes C.P. PTEN: the down side of PI 3-kinase signalling. Cell. Signal. 14 (2002) 285-295
    • (2002) Cell. Signal. , vol.14 , pp. 285-295
    • Leslie, N.R.1    Downes, C.P.2
  • 22
  • 24
    • 0033615538 scopus 로고    scopus 로고
    • Crystal structure of the PTEN tumor suppressor: implications for its phosphoinositide phosphatase activity and membrane association
    • Lee J.O., Yang H., Georgescu M.M., Di Cristofano A., Maehama T., Shi Y., Dixon J.E., Pandolfi P., and Pavletich N.P. Crystal structure of the PTEN tumor suppressor: implications for its phosphoinositide phosphatase activity and membrane association. Cell 99 (1999) 323-334
    • (1999) Cell , vol.99 , pp. 323-334
    • Lee, J.O.1    Yang, H.2    Georgescu, M.M.3    Di Cristofano, A.4    Maehama, T.5    Shi, Y.6    Dixon, J.E.7    Pandolfi, P.8    Pavletich, N.P.9
  • 25
    • 2642534538 scopus 로고    scopus 로고
    • Cloning, expression, purification, and characterization of the human Class Ia phosphoinositide 3-kinase isoforms
    • Meier T.I., Cook J.A., Thomas J.E., Radding J.A., Horn C., Lingaraj T., and Smith M.C. Cloning, expression, purification, and characterization of the human Class Ia phosphoinositide 3-kinase isoforms. Protein Expr. Purif. 35 (2004) 218-224
    • (2004) Protein Expr. Purif. , vol.35 , pp. 218-224
    • Meier, T.I.1    Cook, J.A.2    Thomas, J.E.3    Radding, J.A.4    Horn, C.5    Lingaraj, T.6    Smith, M.C.7
  • 27
    • 0026512750 scopus 로고
    • Formation of supported planar bilayers by fusion of vesicles to supported phospholipid monolayers
    • Kalb E., Frey S., and Tamm L.K. Formation of supported planar bilayers by fusion of vesicles to supported phospholipid monolayers. Biochim. Biophys. Acta 1103 (1992) 307-316
    • (1992) Biochim. Biophys. Acta , vol.1103 , pp. 307-316
    • Kalb, E.1    Frey, S.2    Tamm, L.K.3
  • 28
    • 1942501586 scopus 로고    scopus 로고
    • Novel mechanism of PTEN regulation by its phosphatidylinositol 4,5-bisphosphate binding motif is critical for chemotaxis
    • Iijima M., Huang Y.E., Luo H.R., Vazquez F., and Devreotes P.N. Novel mechanism of PTEN regulation by its phosphatidylinositol 4,5-bisphosphate binding motif is critical for chemotaxis. J. Biol. Chem. 279 (2004) 16606-16613
    • (2004) J. Biol. Chem. , vol.279 , pp. 16606-16613
    • Iijima, M.1    Huang, Y.E.2    Luo, H.R.3    Vazquez, F.4    Devreotes, P.N.5
  • 29
    • 0035877577 scopus 로고    scopus 로고
    • Activation loop sequences confer substrate specificity to phosphoinositide 3-kinase alpha (PI3Kalpha). Functions of lipid kinase-deficient PI3Kalpha in signaling
    • Pirola L., Zvelebil M.J., Bulgarelli-Leva G., Van Obberghen E., Waterfield M.D., and Wymann M.P. Activation loop sequences confer substrate specificity to phosphoinositide 3-kinase alpha (PI3Kalpha). Functions of lipid kinase-deficient PI3Kalpha in signaling. J. Biol. Chem. 276 (2001) 21544-21554
    • (2001) J. Biol. Chem. , vol.276 , pp. 21544-21554
    • Pirola, L.1    Zvelebil, M.J.2    Bulgarelli-Leva, G.3    Van Obberghen, E.4    Waterfield, M.D.5    Wymann, M.P.6
  • 30
    • 0033634827 scopus 로고    scopus 로고
    • Structural determinants of phosphoinositide 3-kinase inhibition by wortmannin, LY294002, quercetin, myricetin, and staurosporine
    • Walker E.H., Pacold M.E., Perisic O., Stephens L., Hawkins P.T., Wymann M.P., and Williams R.L. Structural determinants of phosphoinositide 3-kinase inhibition by wortmannin, LY294002, quercetin, myricetin, and staurosporine. Mol. Cell 6 (2000) 909-919
    • (2000) Mol. Cell , vol.6 , pp. 909-919
    • Walker, E.H.1    Pacold, M.E.2    Perisic, O.3    Stephens, L.4    Hawkins, P.T.5    Wymann, M.P.6    Williams, R.L.7
  • 31
    • 0000629930 scopus 로고
    • Selection of successive tumour lines for metastasis
    • Fidler I.J. Selection of successive tumour lines for metastasis. Nat. New Biol. 242 (1973) 148-149
    • (1973) Nat. New Biol. , vol.242 , pp. 148-149
    • Fidler, I.J.1
  • 32
    • 0037195815 scopus 로고    scopus 로고
    • Type II phosphatidylinositol 4-kinase beta is a cytosolic and peripheral membrane protein that is recruited to the plasma membrane and activated by Rac-GTP
    • Wei Y.J., Sun H.Q., Yamamoto M., Wlodarski P., Kunii K., Martinez M., Barylko B., Albanesi J.P., and Yin H.L. Type II phosphatidylinositol 4-kinase beta is a cytosolic and peripheral membrane protein that is recruited to the plasma membrane and activated by Rac-GTP. J. Biol. Chem. 277 (2002) 46586-46593
    • (2002) J. Biol. Chem. , vol.277 , pp. 46586-46593
    • Wei, Y.J.1    Sun, H.Q.2    Yamamoto, M.3    Wlodarski, P.4    Kunii, K.5    Martinez, M.6    Barylko, B.7    Albanesi, J.P.8    Yin, H.L.9
  • 33
    • 14844318496 scopus 로고    scopus 로고
    • Rac-WAVE2 signaling is involved in the invasive and metastatic phenotypes of murine melanoma cells
    • Kurisu S., Suetsugu S., Yamazaki D., Yamaguchi H., and Takenawa T. Rac-WAVE2 signaling is involved in the invasive and metastatic phenotypes of murine melanoma cells. Oncogene 24 (2005) 1309-1319
    • (2005) Oncogene , vol.24 , pp. 1309-1319
    • Kurisu, S.1    Suetsugu, S.2    Yamazaki, D.3    Yamaguchi, H.4    Takenawa, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.