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Volumn 8, Issue 8, 2007, Pages 743-748

Endoplasmic reticulum retention of the γ-secretase complex component Pen2 by Rer1

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINE; CELL PROTEIN; CLUSTER OF DIFFERENTIATION 4; GAMMA SECRETASE; MEMBRANE PROTEIN; PS ENHANCER 2; RETENTION IN ENDOPLASMIC RETICULUM 1; UNCLASSIFIED DRUG;

EID: 34547628712     PISSN: 1469221X     EISSN: 14693178     Source Type: Journal    
DOI: 10.1038/sj.embor.7401027     Document Type: Article
Times cited : (73)

References (20)
  • 1
    • 1642336602 scopus 로고    scopus 로고
    • Pen-2 is sequestered in the endoplasmic reticulum and subjected to ubiquitylation and proteasome-mediated degradation in the absence of presenilin
    • Bergman A, Hansson EM, Pursglove SE, Farmery MR, Lannfelt L, Lendahl U, Lundkvist J, Naslund J (2004) Pen-2 is sequestered in the endoplasmic reticulum and subjected to ubiquitylation and proteasome-mediated degradation in the absence of presenilin. J Biol Chem 279: 16744-16753
    • (2004) J Biol Chem , vol.279 , pp. 16744-16753
    • Bergman, A.1    Hansson, E.M.2    Pursglove, S.E.3    Farmery, M.R.4    Lannfelt, L.5    Lendahl, U.6    Lundkvist, J.7    Naslund, J.8
  • 2
    • 0027968228 scopus 로고
    • Kex2-dependent invertase secretion as a tool to study the targeting of transmembrane proteins which are involved in ER → Golgi transport in yeast
    • Boehm J, Ulrich HD, Ossig R, Schmitt HD (1994) Kex2-dependent invertase secretion as a tool to study the targeting of transmembrane proteins which are involved in ER → Golgi transport in yeast. EMBO J 13 3696-3710
    • (1994) EMBO J , vol.13 , pp. 3696-3710
    • Boehm, J.1    Ulrich, H.D.2    Ossig, R.3    Schmitt, H.D.4
  • 3
    • 0025885341 scopus 로고
    • Role of potentially charged transmembrane residues in targeting proteins for retention and degradation within the endoplasmic reticulum
    • Bonifacino JS, Cosson P, Shah N, Klausner RD (1991) Role of potentially charged transmembrane residues in targeting proteins for retention and degradation within the endoplasmic reticulum. EMBO J 10: 2783-2793
    • (1991) EMBO J , vol.10 , pp. 2783-2793
    • Bonifacino, J.S.1    Cosson, P.2    Shah, N.3    Klausner, R.D.4
  • 7
    • 1842410168 scopus 로고    scopus 로고
    • Human Rer1 is localized to the Golgi apparatus and complements the deletion of the homologous Rer1 protein of Saccharomyces cerevisiae
    • Füllekrug J, Boehm J, Rottger S, Nilsson T, Mieskes G, Schmitt HD (1997) Human Rer1 is localized to the Golgi apparatus and complements the deletion of the homologous Rer1 protein of Saccharomyces cerevisiae. Eur J Cell Biol 74: 31-40
    • (1997) Eur J Cell Biol , vol.74 , pp. 31-40
    • Füllekrug, J.1    Boehm, J.2    Rottger, S.3    Nilsson, T.4    Mieskes, G.5    Schmitt, H.D.6
  • 8
    • 1442264828 scopus 로고    scopus 로고
    • Take five-BACE and the γ-secretase quartet conduct Alzheimer's amyloid β-peptide generation
    • Haass C (2004) Take five-BACE and the γ-secretase quartet conduct Alzheimer's amyloid β-peptide generation. EMBO J 23: 483-488
    • (2004) EMBO J , vol.23 , pp. 483-488
    • Haass, C.1
  • 9
    • 0027372586 scopus 로고
    • Role of transmembrane domains in assembly and intracellular transport of the CD8 molecule
    • Hennecke S, Cosson P (1993) Role of transmembrane domains in assembly and intracellular transport of the CD8 molecule. J Biol Chem 268: 26607-26612
    • (1993) J Biol Chem , vol.268 , pp. 26607-26612
    • Hennecke, S.1    Cosson, P.2
  • 10
    • 0036327098 scopus 로고    scopus 로고
    • Presenilin-1 affects trafficking and processing of βAPP and is targeted in a complex with nicastrin to the plasma membrane
    • Kaether C, Lammich S, Edbauer D, Ertl M, Rietdorf J, Capell A, Steiner H, Haass C (2002) Presenilin-1 affects trafficking and processing of βAPP and is targeted in a complex with nicastrin to the plasma membrane. J Cell Biol 158: 551-561
    • (2002) J Cell Biol , vol.158 , pp. 551-561
    • Kaether, C.1    Lammich, S.2    Edbauer, D.3    Ertl, M.4    Rietdorf, J.5    Capell, A.6    Steiner, H.7    Haass, C.8
  • 11
    • 11244272819 scopus 로고    scopus 로고
    • The presenilin C-terminus is required for ER-retention, nicastrin-binding and γ-secretase activity
    • Kaether C, Capell A, Edbauer D, Winkler E, Novak B, Steiner H, Haas C 2004) The presenilin C-terminus is required for ER-retention, nicastrin-binding and γ-secretase activity. EMBO J 23: 4738-4748
    • (2004) EMBO J , vol.23 , pp. 4738-4748
    • Kaether, C.1    Capell, A.2    Edbauer, D.3    Winkler, E.4    Novak, B.5    Steiner, H.6    Haas, C.7
  • 12
    • 33750151419 scopus 로고    scopus 로고
    • Assembly, trafficking and function of γ-secretase
    • Kaether C, Haass C, 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
  • 13
    • 10344243551 scopus 로고    scopus 로고
    • Evidence that assembly of an active γ-secretase complex occurs in the early compartments of the secretory pathway
    • Kim SH, Yin YI, Li YM, Sisodia SS (2004) Evidence that assembly of an active γ-secretase complex occurs in the early compartments of the secretory pathway. J Biol Chem 279: 48615-48619
    • (2004) J Biol Chem , vol.279 , pp. 48615-48619
    • Kim, S.H.1    Yin, Y.I.2    Li, Y.M.3    Sisodia, S.S.4
  • 15
    • 2542454942 scopus 로고    scopus 로고
    • Requirement of PEN-2 for stabilization of the presenilin N-/C-terminal fragment heterodimer within the γ-secretase complex
    • Prokop S, Shirotani K, Edbauer D, Haass C, Steiner H (2004) Requirement of PEN-2 for stabilization of the presenilin N-/C-terminal fragment heterodimer within the γ-secretase complex. J Biol Chem 279 23255-23261
    • (2004) J Biol Chem , vol.279 , pp. 23255-23261
    • Prokop, S.1    Shirotani, K.2    Edbauer, D.3    Haass, C.4    Steiner, H.5
  • 17
    • 0141856357 scopus 로고    scopus 로고
    • Rer 1 p, a retrieval receptor for ER membrane protins, recognizes transmembrane domains in multiple modes
    • Sato K, Sato M, Nakano A,(2003) Rer 1 p, a retrieval receptor for ER membrane protins, recognizes transmembrane domains in multiple modes. Mol Biol Cell 14: 3605-3616
    • (2003) Mol Biol Cell , vol.14 , pp. 3605-3616
    • Sato, K.1    Sato, M.2    Nakano, A.3
  • 18
    • 33847389291 scopus 로고    scopus 로고
    • Rer 1p competes with APH-1 for binding to nicastrin and regulates γ-secretase complex assembly in the early secretory pathway
    • Spasic D, Raemaekers T, Dillèn K, Declerck I, Baert V, Serneels L, Fullekrug J, Annaert W (2007) Rer 1p competes with APH-1 for binding to nicastrin and regulates γ-secretase complex assembly in the early secretory pathway. J Cell Biol 176: 629-640
    • (2007) J Cell Biol , vol.176 , pp. 629-640
    • Spasic, D.1    Raemaekers, T.2    Dillèn, K.3    Declerck, I.4    Baert, V.5    Serneels, L.6    Fullekrug, J.7    Annaert, W.8
  • 20
    • 0033103174 scopus 로고    scopus 로고
    • A new ER trafficking signal regulates the subunit stoichiometry of plasma membrane K(ATP) channels
    • Zerangue N, Schwappach B, Jan YN, Jan LY (1999) A new ER trafficking signal regulates the subunit stoichiometry of plasma membrane K(ATP) channels. Neuron 22: 537-548
    • (1999) Neuron , vol.22 , pp. 537-548
    • Zerangue, N.1    Schwappach, B.2    Jan, Y.N.3    Jan, L.Y.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.