PMID- 30408515
OWN - NLM
STAT- MEDLINE
DCOM- 20200226
LR  - 20200226
IS  - 1873-3913 (Electronic)
IS  - 0898-6568 (Linking)
VI  - 53
DP  - 2019 Jan
TI  - Nitric oxide mediated redox regulation of protein homeostasis.
PG  - 348-356
LID - S0898-6568(18)30268-7 [pii]
LID - 10.1016/j.cellsig.2018.10.019 [doi]
AB  - Nitric oxide is a versatile diffusible signaling molecule, whose biosynthesis by 
      three NO synthases (NOS) is tightly regulated at transcriptional and 
      posttranslational levels, availability of co-factors, and calcium binding. Above 
      normal levels of NO have beneficial protective effects for example in the 
      cardiovascular system, but also contribute to the pathophysiology in the context 
      of inflammatory diseases, and to aging and neurodegeneration in the nervous 
      system. The effect specificity relies on the functional and spatial specificity 
      of the NOS isoenzymes, and on the duality of two major signaling mechanisms (i) 
      activation of soluble guanylycylase (sGC)-dependent cGMP production and (ii) 
      direct S-nitrosylation of redox sensitive cysteines of susceptible proteins. The 
      present review summarizes the functional implications of S-nitrosylation in the 
      context of proteostasis, and focuses on two NO target proteins, heat shock 
      cognate of 70 kDa (Hsc70/HSPA8) and the ubiquitin 2 ligase (UBE2D), because both 
      are modified on functionally critical cysteines and are key regulators of 
      chaperone mediated and assisted autophagy and proteasomal protein degradation. 
      SNO modifications of these candidates are associated with protein accumulations 
      and adoption of a senescent phenotype of neuronal cells suggesting that 
      S-nitrosylations of protein homeostatic machineries contribute to aging 
      phenomena.
CI  - Copyright (c) 2018 Elsevier Inc. All rights reserved.
FAU - Tegeder, Irmgard
AU  - Tegeder I
AD  - Institute of Clinical Pharmacology, Goethe University Hospital Frankfurt, Theodor 
      Stern Kai 7, 60590 Frankfurt, Germany. Electronic address: 
      tegeder@em.uni-frankfurt.de.
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Review
DEP - 20181105
PL  - England
TA  - Cell Signal
JT  - Cellular signalling
JID - 8904683
RN  - 0 (HSC70 Heat-Shock Proteins)
RN  - 0 (Ubiquitin)
RN  - 31C4KY9ESH (Nitric Oxide)
RN  - EC 2.3.2.27 (Ubiquitin-Protein Ligases)
SB  - IM
MH  - Aging
MH  - Animals
MH  - HSC70 Heat-Shock Proteins/metabolism
MH  - Humans
MH  - Nitric Oxide/*metabolism
MH  - Oxidation-Reduction
MH  - *Proteostasis
MH  - Ubiquitin/metabolism
MH  - Ubiquitin-Protein Ligases/metabolism
OTO - NOTNLM
OT  - Aging
OT  - Chaperone
OT  - Nitric oxide
OT  - Nitrosylation
OT  - Proteostasis
OT  - Ubiquitin
EDAT- 2018/11/09 06:00
MHDA- 2020/02/27 06:00
CRDT- 2018/11/09 06:00
PHST- 2018/10/09 00:00 [received]
PHST- 2018/10/27 00:00 [revised]
PHST- 2018/10/29 00:00 [accepted]
PHST- 2018/11/09 06:00 [pubmed]
PHST- 2020/02/27 06:00 [medline]
PHST- 2018/11/09 06:00 [entrez]
AID - S0898-6568(18)30268-7 [pii]
AID - 10.1016/j.cellsig.2018.10.019 [doi]
PST - ppublish
SO  - Cell Signal. 2019 Jan;53:348-356. doi: 10.1016/j.cellsig.2018.10.019. Epub 2018 
      Nov 5.