Two waves of proteasome-dependent protein degradation in the hippocampus are required for recognition memory consolidation

2015 ◽  
Vol 120 ◽  
pp. 1-6 ◽  
Author(s):  
Luciana S. Figueiredo ◽  
Arethuza S. Dornelles ◽  
Fernanda S. Petry ◽  
Lucio Falavigna ◽  
Vinicius A. Dargél ◽  
...  
Keyword(s):  
Recognition Memory ◽  
Protein Degradation ◽  
Memory Consolidation ◽  
Dependent Protein

Class I HDAC inhibition improves object recognition memory consolidation through BDNF/TrkB pathway in a time-dependent manner

2021 ◽  
Vol 187 ◽  
pp. 108493
Author(s):  
Gerardo Ramirez-Mejia ◽  
Elvi Gil-Lievana ◽  
Oscar Urrego-Morales ◽  
Ernesto Soto-Reyes ◽  
Federico Bermúdez-Rattoni
Keyword(s):  
Object Recognition ◽  
Recognition Memory ◽  
Memory Consolidation ◽  
Time Dependent ◽  
Class I ◽  
Dependent Manner ◽  
Hdac Inhibition ◽  
Object Recognition Memory

scholarly journals Role of proteasome-dependent protein degradation in long-term operant memory inAplysia

2016 ◽  
Vol 24 (1) ◽  
pp. 59-64 ◽  
Author(s):  
Lisa C. Lyons ◽  
Jacob S. Gardner ◽  
Catherine E. Gandour ◽  
Harini C. Krishnan
Keyword(s):  
Protein Degradation ◽  
Dependent Protein

scholarly journals Inhibition of Protein Ubiquitination by Paraquat and 1-Methyl-4-Phenylpyridinium Impairs Ubiquitin-Dependent Protein Degradation Pathways

2015 ◽  
Vol 53 (8) ◽  
pp. 5229-5251 ◽  
Author(s):  
Juliana Navarro-Yepes ◽  
Annadurai Anandhan ◽  
Erin Bradley ◽  
Iryna Bohovych ◽  
Bo Yarabe ◽  
...  
Keyword(s):  
Protein Degradation ◽  
Degradation Pathways ◽  
Protein Ubiquitination ◽  
Dependent Protein

scholarly journals Domains required for dimerization of yeast Rad6 ubiquitin-conjugating enzyme and Rad18 DNA binding protein.

1997 ◽  
Vol 17 (8) ◽  
pp. 4536-4543 ◽  
Author(s):  
V Bailly ◽  
S Prakash ◽  
L Prakash
Keyword(s):  
Dna Binding ◽  
Protein Degradation ◽  
Binding Activity ◽  
Helix Loop Helix ◽  
Dna Binding Activity ◽  
C Terminus ◽  
Rad6 Gene ◽  
Ubiquitin Conjugating Enzyme ◽  
Dependent Protein ◽  
Conjugating Enzyme

The RAD6 gene of Saccharomyces cerevisiae encodes a ubiquitin-conjugating enzyme required for postreplicational repair of UV-damaged DNA and for damage-induced mutagenesis. In addition, Rad6 functions in the N end rule pathway of protein degradation. Rad6 mediates its DNA repair role via its association with Rad18, whose DNA binding activity may target the Rad6-Rad18 complex to damaged sites in DNA. In its role in N end-dependent protein degradation, Rad6 interacts with the UBR1-encoded ubiquitin protein ligase (E3) enzyme. Previous studies have indicated the involvement of N-terminal and C-terminal regions of Rad6 in interactions with Ubr1. Here, we identify the regions of Rad6 and Rad18 that are involved in the dimerization of these two proteins. We show that a region of 40 amino acids towards the C terminus of Rad18 (residues 371 to 410) is sufficient for interaction with Rad6. This region of Rad18 contains a number of nonpolar residues that have been conserved in helix-loop-helix motifs of other proteins. Our studies indicate the requirement for residues 141 to 149 at the C terminus, and suggest the involvement of residues 10 to 22 at the N terminus of Rad6, in the interaction with Rad18. Each of these regions of Rad6 is indicated to form an amphipathic helix.

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