메뉴 건너뛰기




Volumn 9, Issue 2, 2008, Pages 215-229

Membrane targeting by APPL1 and APPL2: Dynamic scaffolds that oligomerize and bind phosphoinositides

Author keywords

APPL1; APPL2; BAR domain; Endocytosis; PH domain; Phosphoinositide binding; PTB domain; RAB5; Signaling endosome

Indexed keywords

ADAPTOR PROTEIN; ADAPTOR PROTEIN PHOSPHOTYROSINE INTERACTION PH DOMAIN AND LEUCINE ZIPPER CONTAINING 1; ADAPTOR PROTEIN PHOSPHOTYROSINE INTERACTION PH DOMAIN AND LEUCINE ZIPPER CONTAINING 2; HYBRID PROTEIN; OLIGOMER; PHOSPHATIDYLINOSITIDE; PHOSPHOTYROSINE; PLECKSTRIN; PROTEIN; RAB PROTEIN; RECEPTOR; UNCLASSIFIED DRUG; YELLOW FLUORESCENT PROTEIN;

EID: 38149031704     PISSN: 13989219     EISSN: 16000854     Source Type: Journal    
DOI: 10.1111/j.1600-0854.2007.00680.x     Document Type: Article
Times cited : (46)

References (46)
  • 4
    • 2942601056 scopus 로고    scopus 로고
    • Human follicle-stimulating hormone (FSH) receptor interacts with the adaptor protein APPL1 in HEK 293 cells: Potential involvement of the PI3K pathway in FSH signaling
    • Nechamen CA, Thomas RM, Cohen BD, Acevedo G, Poulikakos PI, Testa JR, Dias JA. Human follicle-stimulating hormone (FSH) receptor interacts with the adaptor protein APPL1 in HEK 293 cells: Potential involvement of the PI3K pathway in FSH signaling. Biol Reprod 2004; 71: 629-636.
    • (2004) Biol Reprod , vol.71 , pp. 629-636
    • Nechamen, C.A.1    Thomas, R.M.2    Cohen, B.D.3    Acevedo, G.4    Poulikakos, P.I.5    Testa, J.R.6    Dias, J.A.7
  • 5
    • 33751239461 scopus 로고    scopus 로고
    • APPL1, APPL2, Akt2 and FOXO1a interact with FSHR in a potential signaling complex
    • Nechamen CA, Thomas RM, Dias JA. APPL1, APPL2, Akt2 and FOXO1a interact with FSHR in a potential signaling complex. Mol Cell Endocrinol 2007; 260-262: 93-99.
    • (2007) Mol Cell Endocrinol , vol.260-262 , pp. 93-99
    • Nechamen, C.A.1    Thomas, R.M.2    Dias, J.A.3
  • 7
    • 34248147538 scopus 로고    scopus 로고
    • Adiponectin-induced eNOS activation and nitric oxide production are mediated by APPL1 in endothelial cells
    • Cheng KK, Lam KS, Wang Y, Yu H, Carling D, Wu D, Wong C, Xu A. Adiponectin-induced eNOS activation and nitric oxide production are mediated by APPL1 in endothelial cells. Diabetes 2007; 56: 1387-1394.
    • (2007) Diabetes , vol.56 , pp. 1387-1394
    • Cheng, K.K.1    Lam, K.S.2    Wang, Y.3    Yu, H.4    Carling, D.5    Wu, D.6    Wong, C.7    Xu, A.8
  • 8
    • 0033517348 scopus 로고    scopus 로고
    • Identification of a chromosome 3p14.3-21.1 gene, APPL, encoding an adaptor molecule that interacts with the oncoprotein-serine/threonine kinase AKT2
    • Mitsuuchi Y, Johnson SW, Sonoda G, Tanno S, Golemis EA, Testa JR. Identification of a chromosome 3p14.3-21.1 gene, APPL, encoding an adaptor molecule that interacts with the oncoprotein-serine/threonine kinase AKT2. Oncogene 1999; 18: 4891-4898.
    • (1999) Oncogene , vol.18 , pp. 4891-4898
    • Mitsuuchi, Y.1    Johnson, S.W.2    Sonoda, G.3    Tanno, S.4    Golemis, E.A.5    Testa, J.R.6
  • 9
    • 36148932174 scopus 로고    scopus 로고
    • The interaction of AKT with APPL1 is required for insulin-stimulated Glut4 translocation
    • Saito T, Jones CC, Huang S, Czech MP, Pilch PF. The interaction of AKT with APPL1 is required for insulin-stimulated Glut4 translocation. J Biol Chem 2007; 282: 32280-32287.
    • (2007) J Biol Chem , vol.282 , pp. 32280-32287
    • Saito, T.1    Jones, C.C.2    Huang, S.3    Czech, M.P.4    Pilch, P.F.5
  • 12
    • 0033580299 scopus 로고    scopus 로고
    • The Rab5 effector EEA1 is a core component of endosome docking
    • Christoforidis S, McBride HM, Burgoyne RD, Zerial M. The Rab5 effector EEA1 is a core component of endosome docking. Nature 1999; 397: 621-625.
    • (1999) Nature , vol.397 , pp. 621-625
    • Christoforidis, S.1    McBride, H.M.2    Burgoyne, R.D.3    Zerial, M.4
  • 13
    • 0347473801 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-phosphate is found in microdomains of early endosomes
    • Gillooly DJ, Raiborg C, Stenmark H. Phosphatidylinositol 3-phosphate is found in microdomains of early endosomes. Histochem Cell Biol 2003; 120: 445-453.
    • (2003) Histochem Cell Biol , vol.120 , pp. 445-453
    • Gillooly, D.J.1    Raiborg, C.2    Stenmark, H.3
  • 14
    • 24144442691 scopus 로고    scopus 로고
    • Rab conversion as a mechanism of progression from early to late endosomes
    • Rink J, Ghigo E, Kalaidzidis Y, Zerial M. Rab conversion as a mechanism of progression from early to late endosomes. Cell 2005; 122: 735-749.
    • (2005) Cell , vol.122 , pp. 735-749
    • Rink, J.1    Ghigo, E.2    Kalaidzidis, Y.3    Zerial, M.4
  • 15
    • 0037341806 scopus 로고    scopus 로고
    • RhoD regulates endosome dynamics through Diaphanous-related Formin and Src tyrosine kinase
    • Gasman S, Kalaidzidis Y, Zerial M. RhoD regulates endosome dynamics through Diaphanous-related Formin and Src tyrosine kinase. Nat Cell Biol 2003; 5: 195-204.
    • (2003) Nat Cell Biol , vol.5 , pp. 195-204
    • Gasman, S.1    Kalaidzidis, Y.2    Zerial, M.3
  • 17
  • 21
    • 22544482948 scopus 로고    scopus 로고
    • Crystal structure of the endophilin-A1 BAR domain
    • Weissenhorn W. Crystal structure of the endophilin-A1 BAR domain. J Mol Biol 2005; 351: 653-661.
    • (2005) J Mol Biol , vol.351 , pp. 653-661
    • Weissenhorn, W.1
  • 22
    • 33745559393 scopus 로고    scopus 로고
    • Endophilin BAR domain drives membrane curvature by two newly identified structure-based mechanisms
    • Masuda M, Takeda S, Sone M, Ohki T, Mori H, Kamioka Y, Mochizuki N. Endophilin BAR domain drives membrane curvature by two newly identified structure-based mechanisms. EMBO J 2006; 25: 2889-2897.
    • (2006) EMBO J , vol.25 , pp. 2889-2897
    • Masuda, M.1    Takeda, S.2    Sone, M.3    Ohki, T.4    Mori, H.5    Kamioka, Y.6    Mochizuki, N.7
  • 24
    • 6944255481 scopus 로고    scopus 로고
    • Sorting nexin-1 mediates tubular endosome-to-TGN transport through coincidence sensing of high-curvature membranes and 3-phosphoinositides
    • Carlton J, Bujny M, Peter BJ, Oorschot VM, Rutherford A, Mellor H, Klumperman J, McMahon HT, Cullen PJ. Sorting nexin-1 mediates tubular endosome-to-TGN transport through coincidence sensing of high-curvature membranes and 3-phosphoinositides. Curr Biol 2004; 14: 1791-1800.
    • (2004) Curr Biol , vol.14 , pp. 1791-1800
    • Carlton, J.1    Bujny, M.2    Peter, B.J.3    Oorschot, V.M.4    Rutherford, A.5    Mellor, H.6    Klumperman, J.7    McMahon, H.T.8    Cullen, P.J.9
  • 26
    • 8744219635 scopus 로고    scopus 로고
    • Pleckstrin homology domains: Not just for phosphoinositides
    • Lemmon MA. Pleckstrin homology domains: Not just for phosphoinositides. Biochem Soc Trans 2004; 32: 707-711.
    • (2004) Biochem Soc Trans , vol.32 , pp. 707-711
    • Lemmon, M.A.1
  • 28
    • 0029039613 scopus 로고
    • Pleckstrin homology domain-mediated membrane association and activation of the beta-adrenergic receptor kinase requires coordinate interaction with G beta gamma subunits and lipid
    • Pitcher JA, Touhara K, Payne ES, Lefkowitz RJ. Pleckstrin homology domain-mediated membrane association and activation of the beta-adrenergic receptor kinase requires coordinate interaction with G beta gamma subunits and lipid. J Biol Chem 1995; 270: 11707-11710.
    • (1995) J Biol Chem , vol.270 , pp. 11707-11710
    • Pitcher, J.A.1    Touhara, K.2    Payne, E.S.3    Lefkowitz, R.J.4
  • 29
    • 0037986355 scopus 로고    scopus 로고
    • Origins of peptide selectivity and phosphoinositide binding revealed by structures of disabled-1 PTB domain complexes
    • Stolt PC, Jeon H, Song HK, Herz J, Eck MJ, Blacklow SC. Origins of peptide selectivity and phosphoinositide binding revealed by structures of disabled-1 PTB domain complexes. Structure 2003; 11: 569-579.
    • (2003) Structure , vol.11 , pp. 569-579
    • Stolt, P.C.1    Jeon, H.2    Song, H.K.3    Herz, J.4    Eck, M.J.5    Blacklow, S.C.6
  • 31
    • 34247899039 scopus 로고    scopus 로고
    • Crystal structures of the BAR-PH and PTB domains of human APPL1
    • Li J, Mao X, Dong LQ, Liu F, Tong L. Crystal structures of the BAR-PH and PTB domains of human APPL1. Structure 2007; 15: 525-533.
    • (2007) Structure , vol.15 , pp. 525-533
    • Li, J.1    Mao, X.2    Dong, L.Q.3    Liu, F.4    Tong, L.5
  • 33
    • 3543025954 scopus 로고    scopus 로고
    • The BAR-domain family of proteins: A case of bending and binding?
    • Habermann B. The BAR-domain family of proteins: A case of bending and binding? EMBO Rep 2004; 5: 250-255.
    • (2004) EMBO Rep , vol.5 , pp. 250-255
    • Habermann, B.1
  • 34
  • 35
    • 2342661960 scopus 로고    scopus 로고
    • Phosphoinositides in constitutive membrane traffic
    • Roth MG. Phosphoinositides in constitutive membrane traffic. Physiol Rev 2004; 84: 699-730.
    • (2004) Physiol Rev , vol.84 , pp. 699-730
    • Roth, M.G.1
  • 38
    • 0027965262 scopus 로고
    • Compartmentalization of SHC, GRB2 and mSOS, and hyperphosphorylation of Raf-1 by EGF but not insulin in liver parenchyma
    • Di Guglielmo GM, Baass PC, Ou WJ, Posner BI, Bergeron JJ. Compartmentalization of SHC, GRB2 and mSOS, and hyperphosphorylation of Raf-1 by EGF but not insulin in liver parenchyma. EMBO J 1994; 13: 4269-4277.
    • (1994) EMBO J , vol.13 , pp. 4269-4277
    • Di Guglielmo, G.M.1    Baass, P.C.2    Ou, W.J.3    Posner, B.I.4    Bergeron, J.J.5
  • 39
    • 0030461226 scopus 로고    scopus 로고
    • Control of EGF receptor signaling by clathrin-mediated endocytosis
    • Vieira AV, Lamaze C, Schmid SL. Control of EGF receptor signaling by clathrin-mediated endocytosis. Science 1996; 274: 2086-2089.
    • (1996) Science , vol.274 , pp. 2086-2089
    • Vieira, A.V.1    Lamaze, C.2    Schmid, S.L.3
  • 41
    • 0029061444 scopus 로고
    • NGF-stimulated retrograde transport of trkA in the mammalian nervous system
    • Ehlers MD, Kaplan DR, Price DL, Koliatsos VE. NGF-stimulated retrograde transport of trkA in the mammalian nervous system. J Cell Biol 1995; 130: 149-156.
    • (1995) J Cell Biol , vol.130 , pp. 149-156
    • Ehlers, M.D.1    Kaplan, D.R.2    Price, D.L.3    Koliatsos, V.E.4
  • 42
    • 0033529564 scopus 로고    scopus 로고
    • Oligomeric complexes link Rab5 effectors with NSF and drive membrane fusion via interactions between EEA1 and syntaxin 13
    • McBride HM, Rybin V, Murphy C, Giner A, Teasdale R, Zerial M. Oligomeric complexes link Rab5 effectors with NSF and drive membrane fusion via interactions between EEA1 and syntaxin 13. Cell 1999; 98: 377-386.
    • (1999) Cell , vol.98 , pp. 377-386
    • McBride, H.M.1    Rybin, V.2    Murphy, C.3    Giner, A.4    Teasdale, R.5    Zerial, M.6
  • 43
    • 0035257013 scopus 로고    scopus 로고
    • Rab proteins as membrane organizers
    • Zerial M, McBride H. Rab proteins as membrane organizers. Nat Rev Mol Cell Biol 2001; 2: 107-117.
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 107-117
    • Zerial, M.1    McBride, H.2
  • 44
    • 0027362058 scopus 로고
    • Structure-function relationship of the small GTPase rab5
    • Li G, Stahl PD. Structure-function relationship of the small GTPase rab5. J Biol Chem 1993; 268: 24475-24480.
    • (1993) J Biol Chem , vol.268 , pp. 24475-24480
    • Li, G.1    Stahl, P.D.2
  • 46
    • 0034280113 scopus 로고    scopus 로고
    • Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing
    • Simpson JC, Wellenreuther R, Poustka A, Pepperkok R, Wiemann S. Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing. EMBO Rep 2000; 1: 287-292.
    • (2000) EMBO Rep , vol.1 , pp. 287-292
    • Simpson, J.C.1    Wellenreuther, R.2    Poustka, A.3    Pepperkok, R.4    Wiemann, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.