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Structure of the C-terminal phosphotyrosine interaction domain of Fe65L1 complexed with the cytoplasmic tail of amyloid precursor protein reveals a novel peptide binding mode.

Li H, Koshiba S, Hayashi F, Tochio N, Tomizawa T, Kasai T, Yabuki T, Motoda Y, Harada T, Watanabe S, Inoue M, Hayashizaki Y, Tanaka A, Kigawa T, Yokoyama S
J Biol Chem 283 27165-78 (2008)
Related entries: 2roz, 2ysz, 2yt0, 2yt1

Cited: 17 times
EuropePMC logo PMID: 18650440

Abstract

Fe65L1, a member of the Fe65 family, is an adaptor protein that interacts with the cytoplasmic domain of Alzheimer amyloid precursor protein (APP) through its C-terminal phosphotyrosine interaction/phosphotyrosine binding (PID/PTB) domain. In the present study, the solution structures of the C-terminal PID domain of mouse Fe65L1, alone and in complex with a 32-mer peptide (DAAVTPEERHLSKMQQNGYENPTYKFFEQMQN) derived from the cytoplasmic domain of APP, were determined using NMR spectroscopy. The C-terminal PID domain of Fe65L1 alone exhibits a canonical PID/PTB fold, whereas the complex structure reveals a novel mode of peptide binding. In the complex structure, the NPTY motif forms a type-I beta-turn, and the residues immediately N-terminal to the NPTY motif form an antiparallel beta-sheet with the beta5 strand of the PID domain, the binding mode typically observed in the PID/PTB.peptide complex. On the other hand, the N-terminal region of the peptide forms a 2.5-turn alpha-helix and interacts extensively with the C-terminal alpha-helix and the peripheral regions of the PID domain, representing a novel mode of peptide binding that has not been reported previously for the PID/PTB.peptide complex. The indispensability of the N-terminal region of the peptide for the high affinity of the PID-peptide interaction is consistent with NMR titration and isothermal calorimetry data. The extensive binding features of the PID domain of Fe65L1 with the cytoplasmic domain of APP provide a framework for further understanding of the function, trafficking, and processing of APP modulated by adapter proteins.

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  2. Survey of the year 2008: applications of isothermal titration calorimetry. Falconer RJ, Penkova A, Jelesarov I, Collins BM. J Mol Recognit 23 395-413 (2010)
  3. Alzheimer's disease--a panorama glimpse. Zhao LN, Lu L, Chew LY, Mu Y. Int J Mol Sci 15 12631-12650 (2014)
  4. Structural Studies Providing Insights into Production and Conformational Behavior of Amyloid-β Peptide Associated with Alzheimer's Disease Development. Urban AS, Pavlov KV, Kamynina AV, Okhrimenko IS, Arseniev AS, Bocharov EV. Molecules 26 (2021)

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  2. Structure of the intracellular domain of the amyloid precursor protein in complex with Fe65-PTB2. Radzimanowski J, Simon B, Sattler M, Beyreuther K, Sinning I, Wild K. EMBO Rep 9 1134-1140 (2008)
  3. Contribution of E3-ubiquitin ligase activity to HIV-1 restriction by TRIM5alpha(rh): structure of the RING domain of TRIM5alpha. Lienlaf M, Hayashi F, Di Nunzio F, Tochio N, Kigawa T, Yokoyama S, Diaz-Griffero F. J Virol 85 8725-8737 (2011)
  4. Structure of the minimal interface between ApoE and LRP. Guttman M, Prieto JH, Handel TM, Domaille PJ, Komives EA. J Mol Biol 398 306-319 (2010)
  5. The PTB domain of ShcA couples receptor activation to the cytoskeletal regulator IQGAP1. Smith MJ, Hardy WR, Li GY, Goudreault M, Hersch S, Metalnikov P, Starostine A, Pawson T, Ikura M. EMBO J 29 884-896 (2010)
  6. The apoptotic engulfment protein Ced-6 participates in clathrin-mediated yolk uptake in Drosophila egg chambers. Jha A, Watkins SC, Traub LM. Mol Biol Cell 23 1742-1764 (2012)
  7. Structural and functional characterization of the NHR1 domain of the Drosophila neuralized E3 ligase in the notch signaling pathway. He F, Saito K, Kobayashi N, Harada T, Watanabe S, Kigawa T, Güntert P, Ohara O, Tanaka A, Unzai S, Muto Y, Yokoyama S. J Mol Biol 393 478-495 (2009)
  8. Dab1 binds to Fe65 and diminishes the effect of Fe65 or LRP1 on APP processing. Kwon OY, Hwang K, Kim JA, Kim K, Kwon IC, Song HK, Jeon H. J Cell Biochem 111 508-519 (2010)
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  10. Novel functions of CCM1 delimit the relationship of PTB/PH domains. Zhang J, Dubey P, Padarti A, Zhang A, Patel R, Patel V, Cistola D, Badr A. Biochim Biophys Acta Proteins Proteom 1865 1274-1286 (2017)
  11. Secondary structure, a missing component of sequence-based minimotif definitions. Sargeant DP, Gryk MR, Maciejewski MW, Thapar V, Kundeti V, Rajasekaran S, Romero P, Dunker K, Li SC, Kaneko T, Schiller MR. PLoS One 7 e49957 (2012)
  12. A pre-metazoan origin of the CRK gene family and co-opted signaling network. Shigeno-Nakazawa Y, Kasai T, Ki S, Kostyanovskaya E, Pawlak J, Yamagishi J, Okimoto N, Taiji M, Okada M, Westbrook J, Satta Y, Kigawa T, Imamoto A. Sci Rep 6 34349 (2016)
  13. Structural basis for the interaction between the first SURP domain of the SF3A1 subunit in U2 snRNP and the human splicing factor SF1. Nameki N, Takizawa M, Suzuki T, Tani S, Kobayashi N, Sakamoto T, Muto Y, Kuwasako K. Protein Sci 31 e4437 (2022)


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