메뉴 건너뛰기




Volumn 140, Issue 6, 2017, Pages 955-962

Alanine substitutions in the GXXXG motif alter C99 cleavage by γ-secretase but not its dimerization

Author keywords

Alzheimer disease; amyloid ; dimerization; enzyme processing; gamma secretase; transmembrane domain

Indexed keywords

ALANINE; AMYLOID PRECURSOR PROTEIN; GAMMA SECRETASE; POLYACRYLAMIDE GEL; AMYLOID BETA PROTEIN; AMYLOID BETA-PROTEIN PRECURSOR C-TERMINAL FRAGMENT BETA, HUMAN; PEPTIDE FRAGMENT; SECRETASE;

EID: 85011268731     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/jnc.13942     Document Type: Article
Times cited : (14)

References (34)
  • 1
    • 43049163813 scopus 로고    scopus 로고
    • Substrate specificity of gamma-secretase and other intramembrane proteases
    • Beel A. J. and Sanders C. R. (2008) Substrate specificity of gamma-secretase and other intramembrane proteases. Cell. Mol. Life Sci. 65, 1311–1334.
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 1311-1334
    • Beel, A.J.1    Sanders, C.R.2
  • 2
    • 84861194622 scopus 로고    scopus 로고
    • The mechanism of γ-secretase dysfunction in familial Alzheimer disease
    • Chávez-Gutiérrez L., Bammens L., Benilova I. et al. (2012) The mechanism of γ-secretase dysfunction in familial Alzheimer disease. EMBO J. 31, 2261–2274.
    • (2012) EMBO J. , vol.31 , pp. 2261-2274
    • Chávez-Gutiérrez, L.1    Bammens, L.2    Benilova, I.3
  • 3
    • 84893421984 scopus 로고    scopus 로고
    • Substrate ectodomain is critical for substrate preference and inhibition of γ-secretase
    • Funamoto S., Sasaki T., Ishihara S. et al. (2013) Substrate ectodomain is critical for substrate preference and inhibition of γ-secretase. Nat. Commun. 2529, 1–12. doi:10.1038/ncomms3529.
    • (2013) Nat. Commun. , vol.2529 , pp. 1-12
    • Funamoto, S.1    Sasaki, T.2    Ishihara, S.3
  • 4
    • 0021256895 scopus 로고
    • Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • Glenner G. G. and Wong C. W. (1984a) Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem. Biophys. Res. Commun. 120, 885–890.
    • (1984) Biochem. Biophys. Res. Commun. , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 5
    • 0021207461 scopus 로고
    • Alzheimer's disease and Down's syndrome: sharing of a unique cerebrovascular amyloid fibril protein
    • Glenner G. G. and Wong C. W. (1984b) Alzheimer's disease and Down's syndrome: sharing of a unique cerebrovascular amyloid fibril protein. Biochem. Biophys. Res. Commun. 122, 1131–1135.
    • (1984) Biochem. Biophys. Res. Commun. , vol.122 , pp. 1131-1135
    • Glenner, G.G.1    Wong, C.W.2
  • 6
    • 0026597063 scopus 로고
    • Alzheimer's disease: the amyloid cascade hypothesis
    • Hardy J. A. and Higgins G. A. (1992) Alzheimer's disease: the amyloid cascade hypothesis. Science 256, 184–185.
    • (1992) Science , vol.256 , pp. 184-185
    • Hardy, J.A.1    Higgins, G.A.2
  • 8
    • 33750151419 scopus 로고    scopus 로고
    • Assembly, trafficking and function of γ-secretase
    • Kaether C., Haass C. and Steiner H. (2006) Assembly, trafficking and function of γ-secretase. Neurodegener. Dis. 3, 275–283.
    • (2006) Neurodegener. Dis. , vol.3 , pp. 275-283
    • Kaether, C.1    Haass, C.2    Steiner, H.3
  • 9
    • 33744957163 scopus 로고    scopus 로고
    • Equimolar production of amyloid β-protein and amyloid precursor protein intracellular domain from β-carboxyl-terminal fragment by γ-secretase
    • Kakuda N., Funamoto S., Yagishita S., Takami M., Osawa S., Dohmae E. and Ihara Y. (2006) Equimolar production of amyloid β-protein and amyloid precursor protein intracellular domain from β-carboxyl-terminal fragment by γ-secretase. J. Biol. Chem. 281, 14776–14786.
    • (2006) J. Biol. Chem. , vol.281 , pp. 14776-14786
    • Kakuda, N.1    Funamoto, S.2    Yagishita, S.3    Takami, M.4    Osawa, S.5    Dohmae, E.6    Ihara, Y.7
  • 10
    • 84859379937 scopus 로고    scopus 로고
    • Altered γ-secretase activity in mild cognitive impairment and Alzheimer's disease
    • Kakuda N., Shoji M., Arai H. et al. (2012) Altered γ-secretase activity in mild cognitive impairment and Alzheimer's disease. EMBO Mol. Med. 4, 344–352.
    • (2012) EMBO Mol. Med. , vol.4 , pp. 344-352
    • Kakuda, N.1    Shoji, M.2    Arai, H.3
  • 12
    • 43149088724 scopus 로고    scopus 로고
    • Amyloidgenic processing but not amyloid precursor protein (APP) intracellular c-terminal domain production requires a precisely oriented APP dimer assembles by transmembrane GXXXG motifs
    • Kienlen-Campard P., Tasiaux B., Van Hees J. et al. (2008) Amyloidgenic processing but not amyloid precursor protein (APP) intracellular c-terminal domain production requires a precisely oriented APP dimer assembles by transmembrane GXXXG motifs. J. Biol. Chem. 283, 7733–7744.
    • (2008) J. Biol. Chem. , vol.283 , pp. 7733-7744
    • Kienlen-Campard, P.1    Tasiaux, B.2    Van Hees, J.3
  • 13
    • 0037076540 scopus 로고    scopus 로고
    • GXXXG and AXXXA: common alpha-helical interaction motifs in proteins, particularly in extremophiles
    • Kleiger G., Grothe R., Mallick P. and Eisenberg D. (2002) GXXXG and AXXXA: common alpha-helical interaction motifs in proteins, particularly in extremophiles. Biochemistry 41, 5990–5997.
    • (2002) Biochemistry , vol.41 , pp. 5990-5997
    • Kleiger, G.1    Grothe, R.2    Mallick, P.3    Eisenberg, D.4
  • 14
    • 85016380485 scopus 로고    scopus 로고
    • The A673T mutation in the amyloid precursor protein reduces the production of β-amyloid protein from its β-carboxyl terminal fragment in cells
    • Kokawa A., Ishihara S., Fujiwara H., Nobuhara M., Iwata M., Ihara Y. and Funamoto S. (2015) The A673T mutation in the amyloid precursor protein reduces the production of β-amyloid protein from its β-carboxyl terminal fragment in cells. Acta Neuropathol. Commun. 3, 66. doi:10.1186/s40478-015-0247-6.
    • (2015) Acta Neuropathol. Commun. , vol.3 , pp. 66
    • Kokawa, A.1    Ishihara, S.2    Fujiwara, H.3    Nobuhara, M.4    Iwata, M.5    Ihara, Y.6    Funamoto, S.7
  • 15
    • 84904560883 scopus 로고    scopus 로고
    • Three-dimensional structure of human secretase
    • Lu P., Bai X. C., Ma D. et al. (2014) Three-dimensional structure of human secretase. Nature 512, 166–170.
    • (2014) Nature , vol.512 , pp. 166-170
    • Lu, P.1    Bai, X.C.2    Ma, D.3
  • 16
    • 84939600856 scopus 로고    scopus 로고
    • Role of GxxxG motifs in transmembrane domain interactions
    • Mark G. T. and Dieter L. (2015) Role of GxxxG motifs in transmembrane domain interactions. Biochemistry 54, 5125–5135.
    • (2015) Biochemistry , vol.54 , pp. 5125-5135
    • Mark, G.T.1    Dieter, L.2
  • 20
    • 0031808074 scopus 로고    scopus 로고
    • A helix propensity scale based on experimental studies of peptides and proteins
    • Pace C. N. and Scholtz J. M. (1998) A helix propensity scale based on experimental studies of peptides and proteins. Biophys. J. 75, 422–427.
    • (1998) Biophys. J. , vol.75 , pp. 422-427
    • Pace, C.N.1    Scholtz, J.M.2
  • 21
    • 0034711953 scopus 로고    scopus 로고
    • The GxxxG motif: a frame work for transmembrane helix-helix association
    • Russ W. P. and Engelman D. M. (2000) The GxxxG motif: a frame work for transmembrane helix-helix association. J. Mol. Biol. 296, 911–919.
    • (2000) J. Mol. Biol. , vol.296 , pp. 911-919
    • Russ, W.P.1    Engelman, D.M.2
  • 22
    • 0035222647 scopus 로고    scopus 로고
    • Blue-native gels to isolate protein complex from mitochondria
    • Schägger H. (2001) Blue-native gels to isolate protein complex from mitochondria. Methods Cell Biol. 65, 231–244.
    • (2001) Methods Cell Biol. , vol.65 , pp. 231-244
    • Schägger, H.1
  • 23
    • 0026409298 scopus 로고
    • Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form
    • Schägger H. and von Jagow G. (1991) Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form. Anal. Biochem. 199, 223–231.
    • (1991) Anal. Biochem. , vol.199 , pp. 223-231
    • Schägger, H.1    von Jagow, G.2
  • 24
    • 0028214450 scopus 로고
    • Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis
    • Schägger H., Cramer W. A. and von Jagow G. (1994) Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis. Anal. Biochem. 217, 220–230.
    • (1994) Anal. Biochem. , vol.217 , pp. 220-230
    • Schägger, H.1    Cramer, W.A.2    von Jagow, G.3
  • 25
    • 0041355557 scopus 로고    scopus 로고
    • Notch and presenilin: regulated intramembrane proteolysis links development and degeneration
    • Selkoe D. and Kopan R. (2003) Notch and presenilin: regulated intramembrane proteolysis links development and degeneration. Annu. Rev. Neurosci. 6, 565–597.
    • (2003) Annu. Rev. Neurosci. , vol.6 , pp. 565-597
    • Selkoe, D.1    Kopan, R.2
  • 26
    • 40949159198 scopus 로고    scopus 로고
    • Building γ-secretase: the bits and pieces
    • Spasic D. and Annaert W. (2008) Building γ-secretase: the bits and pieces. J. Cell Sci. 121, 413–420.
    • (2008) J. Cell Sci. , vol.121 , pp. 413-420
    • Spasic, D.1    Annaert, W.2
  • 27
    • 85014317159 scopus 로고    scopus 로고
    • Chemical cross-linking provides a model of the γ-secertase complex subunit architecture and evidence for close proximity of the C-terminal fragment of presenilin with APH-1
    • Steiner H., Winkler E. and Haass C. (2004) Chemical cross-linking provides a model of the γ-secertase complex subunit architecture and evidence for close proximity of the C-terminal fragment of presenilin with APH-1. J. Biol. Chem. 279, 41340–41345.
    • (2004) J. Biol. Chem. , vol.279 , pp. 41340-41345
    • Steiner, H.1    Winkler, E.2    Haass, C.3
  • 28
    • 57649174625 scopus 로고    scopus 로고
    • Intramembrane proteolysis by γ-secretase
    • Steiner H., Fluhrer R. and Haass C. (2008) Intramembrane proteolysis by γ-secretase. J. Biol. Chem. 283, 29627–29631.
    • (2008) J. Biol. Chem. , vol.283 , pp. 29627-29631
    • Steiner, H.1    Fluhrer, R.2    Haass, C.3
  • 29
    • 84872812991 scopus 로고    scopus 로고
    • γ-Secretase-dependent proteolysis of transmembrane domain of amyloid precursor protein: successive tri- and tetrapeptide release in amyloid β-protein production
    • Takami M. and Funamoto S. (2012) γ-Secretase-dependent proteolysis of transmembrane domain of amyloid precursor protein: successive tri- and tetrapeptide release in amyloid β-protein production. Int. J. Alzheimers Dis. 2012, 1–7. doi:10.1155/2012/591392.
    • (2012) Int. J. Alzheimers Dis. , vol.2012 , pp. 1-7
    • Takami, M.1    Funamoto, S.2
  • 30
    • 70350451482 scopus 로고    scopus 로고
    • gamma-Secretase: successive tripeptide and tetrapeptide release from the transmembrane domain of beta-carboxyl terminal fragment
    • Takami M., Nagashima Y., Sano Y., Ishihara S., Morishima-Kawashima M., Funamoto S. and Ihara Y. (2009) gamma-Secretase: successive tripeptide and tetrapeptide release from the transmembrane domain of beta-carboxyl terminal fragment. J. Neurosci. 29, 13042–13052.
    • (2009) J. Neurosci. , vol.29 , pp. 13042-13052
    • Takami, M.1    Nagashima, Y.2    Sano, Y.3    Ishihara, S.4    Morishima-Kawashima, M.5    Funamoto, S.6    Ihara, Y.7
  • 31
    • 57649221135 scopus 로고    scopus 로고
    • Amyloid precursor protein trafficking, processing, and function
    • Thinakaran G. and Koo E. H. (2008) Amyloid precursor protein trafficking, processing, and function. J. Biol. Chem. 283, 29615–29619.
    • (2008) J. Biol. Chem. , vol.283 , pp. 29615-29619
    • Thinakaran, G.1    Koo, E.H.2
  • 33
    • 38149056617 scopus 로고    scopus 로고
    • Abeta46 is processed to Abeta40 and Abeta43, but not to Abeta42, in the low density membrane domains
    • Yagishita S., Morishima-Kawashima M., Ishiura S. and Ihara Y. (2008) Abeta46 is processed to Abeta40 and Abeta43, but not to Abeta42, in the low density membrane domains. J. Biol. Chem. 283, 733–738.
    • (2008) J. Biol. Chem. , vol.283 , pp. 733-738
    • Yagishita, S.1    Morishima-Kawashima, M.2    Ishiura, S.3    Ihara, Y.4
  • 34
    • 0028945660 scopus 로고
    • Evidence that Aβ42 is the real culprit in alzheimer's disease
    • Younkin S. G. (1995) Evidence that Aβ42 is the real culprit in alzheimer's disease. Ann. Neurol. 37, 287–288.
    • (1995) Ann. Neurol. , vol.37 , pp. 287-288
    • Younkin, S.G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.