Human Molecular Genetics, Vol 5, 1589-1598, Copyright © 1996 by Oxford University Press
SL Bressler, MD Gray, BL Sopher, Q Hu, MG Hearn, DG Pham, MB Dinulos, K Fukuchi, SS Sisodia, MA Miller, CM Disteche and GM Martin
Using the yeast two hybrid system, a mouse embryo cDNA library was screened
for proteins that interact with the C-terminus of the human beta-amyloid
precursor protein (beta PP). A fusion protein was identified that interacts
specifically with the cytoplasmic domain of beta PP and does not interact
with the beta-amyloid region. The protein encoded by this partial mouse
cDNA is identical to the C-terminus of the rat Fe65 protein. This mouse
protein also interacts with the homologous C-terminal domains of the mouse
amyloid precursor-like proteins, APLP1 and APLP2. These conserved
cytoplasmic regions contain a common amino acid motif, Asn-Pro-Thr-Tyr,
which has previously been shown to influence both the secretion and
internalization of beta PP. Fe65 has been implicated in regulatory and cell
signaling mechanisms because it contains two different motifs involved in
protein binding, a WW domain (a variant of Src homology 3 domains) and a
phosphotyrosine interaction domain (PID). Interestingly, the PID domain
binds to the same motif present in the conserved cytoplasmic domains of the
beta PP and beta PP-like proteins. RNA analyses reveal that Fe65 is
predominantly expressed in brain and in the regions most affected by
Alzheimer's disease (AD)-associated neuropathology. The human Fe65 mRNA was
cloned from a fetal brain cDNA library. The message encodes a protein of
735 amino acids that is 95% identical to the rat Fe65 protein. The human
Fe65 gene was mapped on human metaphase chromosomes to band 11p15 using
fluorescence in situ hybridization.
ARTICLES
cDNA cloning and chromosome mapping of the human Fe65 gene: interaction of the conserved cytoplasmic domains of the human beta-amyloid precursor protein and its homologues with the mouse Fe65 protein
Department of Pathology, University of Washington School of Medicine, Seattle 98195-7470, USA.
![]()
CiteULike
Connotea
Del.icio.us What's this?
This article has been cited by other articles:
![]() |
Y. Wang, M. Zhang, C. Moon, Q. Hu, B. Wang, G. Martin, Z. Sun, and H. Wang The APP-interacting protein FE65 is required for hippocampus-dependent learning and long-term potentiation Learn. Mem., August 27, 2009; 16(9): 537 - 544. [Abstract] [Full Text] [PDF] |
||||
![]() |
K.-F. Lau, W.-M. Chan, M. S. Perkinton, E. L. Tudor, R. C. C. Chang, H.-Y. E. Chan, D. M. McLoughlin, and C. C. J. Miller Dexras1 Interacts with FE65 to Regulate FE65-Amyloid Precursor Protein-dependent Transcription J. Biol. Chem., December 12, 2008; 283(50): 34728 - 34737. [Abstract] [Full Text] [PDF] |
||||
![]() |
J. C. Wiley, E. A. Smith, M. P. Hudson, W. C. Ladiges, and M. Bothwell Fe65 Stimulates Proteolytic Liberation of the beta-Amyloid Precursor Protein Intracellular Domain J. Biol. Chem., November 16, 2007; 282(46): 33313 - 33325. [Abstract] [Full Text] [PDF] |
||||
![]() |
H.-S. Hoe, T. S. Tran, Y. Matsuoka, B. W. Howell, and G. W. Rebeck DAB1 and Reelin Effects on Amyloid Precursor Protein and ApoE Receptor 2 Trafficking and Processing J. Biol. Chem., November 17, 2006; 281(46): 35176 - 35185. [Abstract] [Full Text] [PDF] |
||||
![]() |
H.-S. Hoe, L. A. Magill, S. Guenette, Z. Fu, S. Vicini, and G. W. Rebeck FE65 Interaction with the ApoE Receptor ApoEr2 J. Biol. Chem., August 25, 2006; 281(34): 24521 - 24530. [Abstract] [Full Text] [PDF] |
||||
![]() |
S. Neumann, S. Schobel, S. Jager, A. Trautwein, C. Haass, C. U. Pietrzik, and S. F. Lichtenthaler Amyloid Precursor-like Protein 1 Influences Endocytosis and Proteolytic Processing of the Amyloid Precursor Protein J. Biol. Chem., March 17, 2006; 281(11): 7583 - 7594. [Abstract] [Full Text] [PDF] |
||||
![]() |
Z. Yang, B. H. Cool, G. M. Martin, and Q. Hu A Dominant Role for FE65 (APBB1) in Nuclear Signaling J. Biol. Chem., February 17, 2006; 281(7): 4207 - 4214. [Abstract] [Full Text] [PDF] |
||||
![]() |
Q. Hu, L. Wang, Z. Yang, B. H. Cool, G. Zitnik, and G. M. Martin Endoproteolytic Cleavage of FE65 Converts the Adaptor Protein to a Potent Suppressor of the sAPP{alpha} Pathway in Primates J. Biol. Chem., April 1, 2005; 280(13): 12548 - 12558. [Abstract] [Full Text] [PDF] |
||||
![]() |
J.-H. Lee, K.-F. Lau, M. S. Perkinton, C. L. Standen, B. Rogelj, A. Falinska, D. M. McLoughlin, and C. C. J. Miller The Neuronal Adaptor Protein X11{beta} Reduces Amyloid {beta}-Protein Levels and Amyloid Plaque Formation in the Brains of Transgenic Mice J. Biol. Chem., November 19, 2004; 279(47): 49099 - 49104. [Abstract] [Full Text] [PDF] |
||||
![]() |
M. S. Perkinton, C. L. Standen, K.-F. Lau, S. Kesavapany, H. L. Byers, M. Ward, D. M. McLoughlin, and C. C. J. Miller The c-Abl Tyrosine Kinase Phosphorylates the Fe65 Adaptor Protein to Stimulate Fe65/Amyloid Precursor Protein Nuclear Signaling J. Biol. Chem., May 21, 2004; 279(21): 22084 - 22091. [Abstract] [Full Text] [PDF] |
||||
![]() |
C. M. Sondag and C. K. Combs Amyloid Precursor Protein Mediates Proinflammatory Activation of Monocytic Lineage Cells J. Biol. Chem., April 2, 2004; 279(14): 14456 - 14463. [Abstract] [Full Text] [PDF] |
||||
![]() |
J.-H. Lee, K.-F. Lau, M. S. Perkinton, C. L. Standen, S. J. A. Shemilt, L. Mercken, J. D. Cooper, D. M. McLoughlin, and C. C. J. Miller The Neuronal Adaptor Protein X11{alpha} Reduces A{beta} Levels in the Brains of Alzheimer's APPswe Tg2576 Transgenic Mice J. Biol. Chem., November 21, 2003; 278(47): 47025 - 47029. [Abstract] [Full Text] [PDF] |
||||
![]() |
P. Bruni, G. Minopoli, T. Brancaccio, M. Napolitano, R. Faraonio, N. Zambrano, U. Hansen, and T. Russo Fe65, a Ligand of the Alzheimer's beta -Amyloid Precursor Protein, Blocks Cell Cycle Progression by Down-regulating Thymidylate Synthase Expression J. Biol. Chem., September 13, 2002; 277(38): 35481 - 35488. [Abstract] [Full Text] [PDF] |
||||
![]() |
P. May, Y. K. Reddy, and J. Herz Proteolytic Processing of Low Density Lipoprotein Receptor-related Protein Mediates Regulated Release of Its Intracellular Domain J. Biol. Chem., May 17, 2002; 277(21): 18736 - 18743. [Abstract] [Full Text] [PDF] |
||||
![]() |
Q. Hu, B. H. Cool, B. Wang, M. G. Hearn, and G. M. Martin A candidate molecular mechanism for the association of an intronic polymorphism of FE65 with resistance to very late onset dementia of the Alzheimer type Hum. Mol. Genet., February 1, 2002; 11(4): 465 - 475. [Abstract] [Full Text] [PDF] |
||||
![]() |
K. Ando, K.-i. Iijima, J. I. Elliott, Y. Kirino, and T. Suzuki Phosphorylation-dependent Regulation of the Interaction of Amyloid Precursor Protein with Fe65 Affects the Production of beta -Amyloid J. Biol. Chem., October 19, 2001; 276(43): 40353 - 40361. [Abstract] [Full Text] [PDF] |
||||
![]() |
S. L. Sabo, A. F. Ikin, J. D. Buxbaum, and P. Greengard The Alzheimer Amyloid Precursor Protein (APP) and Fe65, an APP-Binding Protein, Regulate Cell Movement J. Cell Biol., June 25, 2001; 153(7): 1403 - 1414. [Abstract] [Full Text] [PDF] |
||||
![]() |
B. Delatour, L. Mercken, K. H. El Hachimi, M.-A. Colle, L. Pradier, and C. Duyckaerts FE65 in Alzheimer's Disease : Neuronal Distribution and Association with Neurofibrillary Tangles Am. J. Pathol., May 1, 2001; 158(5): 1585 - 1591. [Abstract] [Full Text] [PDF] |
||||
![]() |
B. T. Hyman, D. Strickland, and G. W. Rebeck Role of the Low-density Lipoprotein Receptor-Related Protein in {beta}-Amyloid Metabolism and Alzheimer Disease Arch Neurol, May 1, 2000; 57(5): 646 - 650. [Abstract] [Full Text] [PDF] |
||||
![]() |
D. S. Rice and T. Curran Mutant mice with scrambled brains: understanding the signaling pathways that control cell positioning in the CNS Genes & Dev., November 1, 1999; 13(21): 2758 - 2773. [Full Text] |
||||
![]() |
R. Homayouni, D. S. Rice, M. Sheldon, and T. Curran Disabled-1 Binds to the Cytoplasmic Domain of Amyloid Precursor-Like Protein 1 J. Neurosci., September 1, 1999; 19(17): 7507 - 7515. [Abstract] [Full Text] [PDF] |
||||
![]() |
B. W. Howell, L. M. Lanier, R. Frank, F. B. Gertler, and J. A. Cooper The Disabled 1 Phosphotyrosine-Binding Domain Binds to the Internalization Signals of Transmembrane Glycoproteins and to Phospholipids Mol. Cell. Biol., July 1, 1999; 19(7): 5179 - 5188. [Abstract] [Full Text] [PDF] |
||||
![]() |
S. L. Sabo, L. M. Lanier, A. F. Ikin, O. Khorkova, S. Sahasrabudhe, P. Greengard, and J. D. Buxbaum Regulation of beta -Amyloid Secretion by FE65, an Amyloid Protein Precursor-binding Protein J. Biol. Chem., March 19, 1999; 274(12): 7952 - 7957. [Abstract] [Full Text] [PDF] |
||||
![]() |
N. N. Dewji and S. J. Singer Specific intercellular binding of the beta -amyloid precursor protein to the presenilins induces intercellular signaling: Its significance for Alzheimer's disease PNAS, December 8, 1998; 95(25): 15055 - 15060. [Abstract] [Full Text] [PDF] |
||||
![]() |
M. Sastre, R. S. Turner, and E. Levy X11 Interaction with beta -Amyloid Precursor Protein Modulates Its Cellular Stabilization and Reduces Amyloid beta -Protein Secretion J. Biol. Chem., August 28, 1998; 273(35): 22351 - 22357. [Abstract] [Full Text] [PDF] |
||||
![]() |
G. Minopoli, P. de Candia, A. Bonetti, R. Faraonio, N. Zambrano, and T. Russo The beta -Amyloid Precursor Protein Functions as a Cytosolic Anchoring Site That Prevents Fe65 Nuclear Translocation J. Biol. Chem., February 23, 2001; 276(9): 6545 - 6550. [Abstract] [Full Text] [PDF] |
||||
![]() |
N. Zambrano, P. Bruni, G. Minopoli, R. Mosca, D. Molino, C. Russo, G. Schettini, M. Sudol, and T. Russo The beta -Amyloid Precursor Protein APP Is Tyrosine-phosphorylated in Cells Expressing a Constitutively Active Form of the Abl Protoncogene J. Biol. Chem., June 1, 2001; 276(23): 19787 - 19792. [Abstract] [Full Text] [PDF] |
||||









