Pen‐2 is dispensable for endoproteolysis of presenilin 1, and nicastrin‐Aph subcomplex is important for both γ‐secretase assembly and substrate recruitment

No abstract is available for this paper.

• Publication year

  2012

• Venue

  Journal of Neurochemistry

• Publication date

  2012-12-01

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1111/jnc.12016PMID 22973949PMCID PMC3509485
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Trafficking and proteolytic processing of APP.

  2012cited by this paper
• γ-Secretase Catalyzes Sequential Cleavages of the AβPP Transmembrane Domain

  2009cited by this paper
• The GxxxG Motif in the Transmembrane Domain of AβPP Plays an Essential Role in the Interaction of CTFβ with the γ-secretase Complex and the Formation of Amyloid-β

  2009cited by this paper
• Assembly, maturation, and trafficking of the gamma-secretase complex in Alzheimer's disease.

  2008cited by this paper
• Molecular and cellular mechanisms for Alzheimer's disease: understanding APP metabolism.

  2007cited by this paper
• The generation and function of soluble apoE receptors in the CNS

  2006cited by this paper
• Pathological and physiological functions of presenilins

  2006cited by this paper
• γ-Cleavage Is Dependent on ζ-Cleavage during the Proteolytic Processing of Amyloid Precursor Protein within Its Transmembrane Domain*

  2005influential reference
• Nicastrin functions as a gamma-secretase-substrate receptor.

  2005cited by this paper
• APH-1a Is the Principal Mammalian APH-1 Isoform Present in γ-Secretase Complexes during Embryonic Development

  2005cited by this paper
• Nicastrin Functions as a γ-Secretase-Substrate Receptor

  2005cited by this paper
• gamma-Cleavage is dependent on zeta-cleavage during the proteolytic processing of amyloid precursor protein within its transmembrane domain.

  2005cited by this paper
• Identification of a New Presenilin-dependent ζ-Cleavage Site within the Transmembrane Domain of Amyloid Precursor Protein*♦

  2004influential reference
• Detergent-dependent dissociation of active gamma-secretase reveals an interaction between Pen-2 and PS1-NTF and offers a model for subunit organization within the complex.

  2004cited by this paper
• Assembly of the γ-Secretase Complex Involves Early Formation of an Intermediate Subcomplex of Aph-1 and Nicastrin*

  2003cited by this paper
• PEN-2 and APH-1 Coordinately Regulate Proteolytic Processing of Presenilin 1*

  2003cited by this paper
• The role of presenilin cofactors in the γ-secretase complex

  2003cited by this paper
• The role of presenilin cofactors in the gamma-secretase complex.

  2003cited by this paper
• Nicastrin Is Required for Assembly of Presenilin/γ-Secretase Complexes to Mediate Notch Signaling and for Processing and Trafficking of β-Amyloid Precursor Protein in Mammals

  2003influential reference
• Faculty Opinions recommendation of PEN-2 is an integral component of the gamma-secretase complex required for coordinated expression of presenilin and nicastrin.

  2002cited by this paper
• The Novel Presenilin-1-associated Protein Is a Proapoptotic Mitochondrial Protein*

  2002cited by this paper
• Mammalian APH-1 Interacts with Presenilin and Nicastrin and Is Required for Intramembrane Proteolysis of Amyloid-β Precursor Protein and Notch*

  2002cited by this paper
• PEN-2 Is an Integral Component of the γ-Secretase Complex Required for Coordinated Expression of Presenilin and Nicastrin*

  2002cited by this paper
• aph-1 and pen-2 are required for Notch pathway signaling, gamma-secretase cleavage of betaAPP, and presenilin protein accumulation.

  2002cited by this paper
• aph-1 and pen-2 Are Required for Notch Pathway Signaling, γ-Secretase Cleavage of βAPP, and Presenilin Protein Accumulation

  2002cited by this paper
• Proteolytic processing and cell biological functions of the amyloid precursor protein.

  2000cited by this paper
• Presenilins are required for γ-secretase cleavage of β-APP and transmembrane cleavage of Notch-1

  2000cited by this paper
• Total inactivation of gamma-secretase activity in presenilin-deficient embryonic stem cells.

  2000cited by this paper
• The transmembrane aspartates in presenilin 1 and 2 are obligatory for gamma-secretase activity and amyloid beta-protein generation.

  2000cited by this paper
• Presenilins are required for gamma-secretase cleavage of beta-APP and transmembrane cleavage of Notch-1.

  2000cited by this paper
• Total inactivation of γ–secretase activity in presenilin-deficient embryonic stem cells

  2000cited by this paper
• The Transmembrane Aspartates in Presenilin 1 and 2 Are Obligatory for γ-Secretase Activity and Amyloid β-Protein Generation*

  2000cited by this paper
• Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and γ-secretase activity

  1999cited by this paper
• Deficiency of presenilin-1 inhibits the normal cleavage of amyloid precursor protein

  1998cited by this paper
• Presenilin proteins undergo heterogeneous endoproteolysis between Thr291 and Ala299 and occur as stable N- and C-terminal fragments in normal and Alzheimer brain tissue.

  1997cited by this paper
• Familial Alzheimer's Disease–Linked Presenilin 1 Variants Elevate Aβ1–42/1–40 Ratio In Vitro and In Vivo

  1996cited by this paper
• Endoproteolysis of presenilin 1 and accumulation of processed derivatives in vivo.

  1996cited by this paper
• Familial Alzheimer's disease-linked presenilin 1 variants elevate Abeta1-42/1-40 ratio in vitro and in vivo.

  1996cited by this paper

• Notch signaling without the APH-2/Nicastrin subunit of Gamma Secretase in C. elegans germline stem cells.

  2024cites this paper
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  2020cites this paper
• Exploring the Role of PSEN Mutations in the Pathogenesis of Alzheimer’s Disease

  2020cites this paper
• Huannao Yicong Formula (还脑益聪方) regulates γ-secretase activity through APH-1 and PEN-2 gene ragulation pathways in hippocampus of APP/PS1 double transgenic mice

  2017cites this paper
• The regulation of L-selectin activity by proteolysis

  2017cites this paper
• Structural and Chemical Biology of Presenilin Complexes.

  2017cites this paper
• Pen-2 and Presenilin are Sufficient to Catalyze Notch Processing

  2017influential citation
• The use of nuclear magnetic resonance in study of structurally dynamic membrane proteins

  2016cites this paper
• Nicastrin is required for amyloid precursor protein (APP) but not Notch processing, while anterior pharynx‐defective 1 is dispensable for processing of both APP and Notch

  2016influential citation
• Propylthiouracil Attenuates Experimental Pulmonary Hypertension via Suppression of Pen-2, a Key Component of Gamma-Secretase

  2015cites this paper
• Structural biology of presenilin 1 complexes

  2014cites this paper
• This Provisional PDF corresponds to the article as it appeared upon acceptance. Fully formatted PDF and full text (HTML) versions will be made available soon.

  2014cites this paper
• Etude du maintien de l'homéostasie tissulaire après induction d'un stress chronique du RE

  2014cites this paper
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  2014cites this paper
• Molecular genetic analysis of hidradenitis suppurativa (acne inversa)

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• Effects of Aluminium on β-Amyloid (1–42) and Secretases (APP-Cleaving Enzymes) in Rat Brain

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• Functional analysis and purification of a Pen‐2 fusion protein for γ‐secretase structural studies

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• Identification and characterization of innate immune receptor substrates of γ-secretase enzyme complex

  2013cites this paper
• The very many faces of presenilins and the γ-secretase complex

  2013influential citation
• Different types of γ-secretes complexes and their effect on substrate processing

  2012cites this paper