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231224s2014 xx |||||o 00| ||eng c |
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|a 10.1093/jxb/eru147
|2 doi
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|a pubmed24n0791.xml
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|a (DE-627)NLM237279150
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|a (NLM)24723404
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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| 100 |
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|a Smolarkiewicz, Michalina
|e verfasserin
|4 aut
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|a Gamma-secretase subunits associate in intracellular membrane compartments in Arabidopsis thaliana
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|c 2014
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
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|2 rdacarrier
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|a Date Completed 23.02.2015
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|a Date Revised 21.10.2021
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a © The Author 2014. Published by Oxford University Press on behalf of the Society for Experimental Biology.
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|a Gamma-secretase is a multisubunit complex with intramembrane proteolytic activity. In humans it was identified in genetic screens of patients suffering from familial forms of Alzheimer's disease, and since then it was shown to mediate cleavage of more than 80 substrates, including amyloid precursor protein or Notch receptor. Moreover, in animals, γ-secretase was shown to be involved in regulation of a wide range of cellular events, including cell signalling, regulation of endocytosis of membrane proteins, their trafficking, and degradation. Here we show that genes coding for γ-secretase homologues are present in plant genomes. Also, amino acid motifs crucial for γ-secretase activity are conserved in plants. Moreover, all γ-secretase subunits: PS1/PS2, APH-1, PEN-2, and NCT colocalize and interact with each other in Arabidopsis thaliana protoplasts. The intracellular localization of γ-secretase subunits in Arabidopsis protoplasts revealed a distribution in endomembrane system compartments that is consistent with data from animal studies. Together, our data may be considered as a starting point for analysis of γ-secretase in plants
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Authophagy
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|a complex assembly
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|a endomembrane system
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|a gamma-secretase
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|a intramembrane protease
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|a localization
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|a presenilin
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|a senescence
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|a vesicular trafficking.
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|a Arabidopsis Proteins
|2 NLM
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|a Amyloid Precursor Protein Secretases
|2 NLM
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| 650 |
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|a EC 3.4.-
|2 NLM
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| 700 |
1 |
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|a Skrzypczak, Tomasz
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Michalak, Michał
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Leśniewicz, Krzysztof
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Walker, J Ross
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Ingram, Gwyneth
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Wojtaszek, Przemysław
|e verfasserin
|4 aut
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| 773 |
0 |
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|i Enthalten in
|t Journal of experimental botany
|d 1985
|g 65(2014), 12 vom: 05. Juli, Seite 3015-27
|w (DE-627)NLM098182706
|x 1460-2431
|7 nnns
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| 773 |
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|g volume:65
|g year:2014
|g number:12
|g day:05
|g month:07
|g pages:3015-27
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|u http://dx.doi.org/10.1093/jxb/eru147
|3 Volltext
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