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Regulated intramembrane proteolysis of the p75 neurotrophin receptor modulates its association with the TrkA receptor.

The generation of biologically active proteins by regulated intramembrane proteolysis is a highly conserved mechanism in cell signaling. Presenilin-dependent gamma -secretase activity is responsible for the intramembrane proteolysis of selected type I membrane proteins, including beta -amyloid precu... Full description

Journal Title: The Journal of biological chemistry October 24, 2003, Vol.278(43), pp.42161-42169
Main Author: Jung, Kwang-Mook
Other Authors: Tan, Serena , Landman, Natalie , Petrova, Kseniya , Murray, Simon , Lewis, Renee , Kim, Peter K , Kim, Dae Sup , Ryu, Sung Ho , Chao, Moses V , Kim, Tae-Wan
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: ISSN: 0021-9258
Link: http://search.proquest.com/docview/71331101/?pq-origsite=primo
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title: Regulated intramembrane proteolysis of the p75 neurotrophin receptor modulates its association with the TrkA receptor.
format: Article
creator:
  • Jung, Kwang-Mook
  • Tan, Serena
  • Landman, Natalie
  • Petrova, Kseniya
  • Murray, Simon
  • Lewis, Renee
  • Kim, Peter K
  • Kim, Dae Sup
  • Ryu, Sung Ho
  • Chao, Moses V
  • Kim, Tae-Wan
subjects:
  • Amino Acid Sequence–Metabolism
  • Amyloid Precursor Protein Secretases–Analysis
  • Animals–Metabolism
  • Aspartic Acid Endopeptidases–Genetics
  • Binding Sites–Metabolism
  • Cell Line–Genetics
  • Endopeptidases–Metabolism
  • Humans–Metabolism
  • Immunohistochemistry–Metabolism
  • Membrane Proteins–Metabolism
  • Peptide Fragments–Metabolism
  • Precipitin Tests–Metabolism
  • Presenilin-1–Metabolism
  • Presenilin-2–Metabolism
  • Protein Binding–Metabolism
  • Protein Structure, Tertiary–Metabolism
  • Rats–Metabolism
  • Receptor, Nerve Growth Factor–Metabolism
  • Receptor, Trka–Metabolism
  • Receptors, Nerve Growth Factor–Metabolism
  • Transfection–Metabolism
  • Membrane Proteins
  • Psen1 Protein, Human
  • Psen2 Protein, Human
  • Peptide Fragments
  • Presenilin-1
  • Presenilin-2
  • Receptor, Nerve Growth Factor
  • Receptors, Nerve Growth Factor
  • Receptor, Trka
  • Amyloid Precursor Protein Secretases
  • Endopeptidases
  • Aspartic Acid Endopeptidases
  • Bace1 Protein, Human
ispartof: The Journal of biological chemistry, October 24, 2003, Vol.278(43), pp.42161-42169
description: The generation of biologically active proteins by regulated intramembrane proteolysis is a highly conserved mechanism in cell signaling. Presenilin-dependent gamma -secretase activity is responsible for the intramembrane proteolysis of selected type I membrane proteins, including beta -amyloid precursor protein (APP) and Notch. A small fraction of intracellular domains derived from both APP and Notch translocates to and appears to function in the nucleus, suggesting a generic role for gamma -secretase cleavage in nuclear signaling. Here we show that the p75 neurotrophin receptor (p75 super(NTR)) undergoes presenilin-dependent intramembrane proteolysis to yield the soluble p75-intracellular domain. The p75 super(NTR) is a multifunctional type I membrane protein that promotes neurotrophin-induced neuronal survival and differentiation by forming a heteromeric co-receptor complex with the Trk receptors. Mass spectrometric analysis revealed that gamma -secretase-mediated cleavage of p75 super(NTR) occurs at a position located in the middle of the transmembrane (TM) domain, which is reminiscent of the amyloid beta -peptide 40 (A beta 40) cleavage of APP and is topologically distinct from the major TM cleavage site of Notch 1. Size exclusion chromatography and co-immunoprecipitation analyses revealed that TrkA forms a molecular complex together with either full-length p75 or membrane-tethered C-terminal fragments. The p75-ICD was not recruited into the TrkA-containing high molecular weight complex, indicating that gamma -secretase-mediated removal of the p75 TM domain may perturb the interaction with TrkA. Independent of the possible nuclear function, our studies suggest that gamma -secretase-mediated p75 super(NTR) proteolysis plays a role in the formation/disassembly of the p75-TrkA receptor complex by regulating the availability of the p75 TM domain that is required for this interaction.
language: eng
source:
identifier: ISSN: 0021-9258
fulltext: fulltext
issn:
  • 00219258
  • 0021-9258
url: Link


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titleRegulated intramembrane proteolysis of the p75 neurotrophin receptor modulates its association with the TrkA receptor.
creatorJung, Kwang-Mook ; Tan, Serena ; Landman, Natalie ; Petrova, Kseniya ; Murray, Simon ; Lewis, Renee ; Kim, Peter K ; Kim, Dae Sup ; Ryu, Sung Ho ; Chao, Moses V ; Kim, Tae-Wan
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ispartofThe Journal of biological chemistry, October 24, 2003, Vol.278(43), pp.42161-42169
identifierISSN: 0021-9258
subjectAmino Acid Sequence–Metabolism ; Amyloid Precursor Protein Secretases–Analysis ; Animals–Metabolism ; Aspartic Acid Endopeptidases–Genetics ; Binding Sites–Metabolism ; Cell Line–Genetics ; Endopeptidases–Metabolism ; Humans–Metabolism ; Immunohistochemistry–Metabolism ; Membrane Proteins–Metabolism ; Peptide Fragments–Metabolism ; Precipitin Tests–Metabolism ; Presenilin-1–Metabolism ; Presenilin-2–Metabolism ; Protein Binding–Metabolism ; Protein Structure, Tertiary–Metabolism ; Rats–Metabolism ; Receptor, Nerve Growth Factor–Metabolism ; Receptor, Trka–Metabolism ; Receptors, Nerve Growth Factor–Metabolism ; Transfection–Metabolism ; Membrane Proteins ; Psen1 Protein, Human ; Psen2 Protein, Human ; Peptide Fragments ; Presenilin-1 ; Presenilin-2 ; Receptor, Nerve Growth Factor ; Receptors, Nerve Growth Factor ; Receptor, Trka ; Amyloid Precursor Protein Secretases ; Endopeptidases ; Aspartic Acid Endopeptidases ; Bace1 Protein, Human
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descriptionThe generation of biologically active proteins by regulated intramembrane proteolysis is a highly conserved mechanism in cell signaling. Presenilin-dependent gamma -secretase activity is responsible for the intramembrane proteolysis of selected type I membrane proteins, including beta -amyloid precursor protein (APP) and Notch. A small fraction of intracellular domains derived from both APP and Notch translocates to and appears to function in the nucleus, suggesting a generic role for gamma -secretase cleavage in nuclear signaling. Here we show that the p75 neurotrophin receptor (p75 super(NTR)) undergoes presenilin-dependent intramembrane proteolysis to yield the soluble p75-intracellular domain. The p75 super(NTR) is a multifunctional type I membrane protein that promotes neurotrophin-induced neuronal survival and differentiation by forming a heteromeric co-receptor complex with the Trk receptors. Mass spectrometric analysis revealed that gamma -secretase-mediated cleavage of p75 super(NTR) occurs at a position located in the middle of the transmembrane (TM) domain, which is reminiscent of the amyloid beta -peptide 40 (A beta 40) cleavage of APP and is topologically distinct from the major TM cleavage site of Notch 1. Size exclusion chromatography and co-immunoprecipitation analyses revealed that TrkA forms a molecular complex together with either full-length p75 or membrane-tethered C-terminal fragments. The p75-ICD was not recruited into the TrkA-containing high molecular weight complex, indicating that gamma -secretase-mediated removal of the p75 TM domain may perturb the interaction with TrkA. Independent of the possible nuclear function, our studies suggest that gamma -secretase-mediated p75 super(NTR) proteolysis plays a role in the formation/disassembly of the p75-TrkA receptor complex by regulating the availability of the p75 TM domain that is required for this interaction.
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30Amyloid Precursor Protein Secretases
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32Aspartic Acid Endopeptidases
33Bace1 Protein, Human
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titleRegulated intramembrane proteolysis of the p75 neurotrophin receptor modulates its association with the TrkA receptor.
authorJung, Kwang-Mook ; Tan, Serena ; Landman, Natalie ; Petrova, Kseniya ; Murray, Simon ; Lewis, Renee ; Kim, Peter K ; Kim, Dae Sup ; Ryu, Sung Ho ; Chao, Moses V ; Kim, Tae-Wan
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1Amyloid Precursor Protein Secretases–Analysis
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5Cell Line–Genetics
6Endopeptidases–Metabolism
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8Immunohistochemistry–Metabolism
9Membrane Proteins–Metabolism
10Peptide Fragments–Metabolism
11Precipitin Tests–Metabolism
12Presenilin-1–Metabolism
13Presenilin-2–Metabolism
14Protein Binding–Metabolism
15Protein Structure, Tertiary–Metabolism
16Rats–Metabolism
17Receptor, Nerve Growth Factor–Metabolism
18Receptor, Trka–Metabolism
19Receptors, Nerve Growth Factor–Metabolism
20Transfection–Metabolism
21Membrane Proteins
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23Psen2 Protein, Human
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26Presenilin-2
27Receptor, Nerve Growth Factor
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30Amyloid Precursor Protein Secretases
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