Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
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Gene/Protein
Disease
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Target Concepts:
Gene/Protein
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Query: UMLS:C0162871 (
abdominal aortic aneurysm
)
8,664
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Plants rely on different immune receptors to recognize pathogens and defend against pathogen attacks. Nucleotide-binding domain and leucine-rich repeat (NLR) proteins play a major role as intracellular immune receptors. Their homeostasis must be maintained at optimal levels in order to effectively recognize pathogens without causing autoimmunity. Previous studies have shown that the activity of the ubiquitin-proteasome system is essential to prevent excessive accumulation of NLR proteins such as Suppressor of
NPR1
, Constitutive 1 (SNC1). Attenuation of the ubiquitin E3 ligase SCF
CPR1
(Constitutive expressor of Pathogenesis Related genes 1) or the E4 protein MUSE3 (Mutant, SNC1-Enhancing 3) leads to NLR accumulation and autoimmunity. In the current study, we report the identification of AtCDC48A as a negative regulator of NLR-mediated immunity. Plants carrying Atcdc48A-4, a partial loss-of-function allele of AtCDC48A, exhibit dwarf morphology and enhanced disease resistance to the oomycete pathogen Hyaloperonospora arabidopsidis (H.a.) Noco2. The SNC1 level is increased in Atcdc48A-4 plants and AtCDC48A interacts with MUSE3 in co-immunoprecipitation experiments, supporting a role for AtCDC48A in NLR turnover. While Arabidopsis contains four other paralogs of AtCDC48A, knockout mutants of these genes do not show obvious immunity-related phenotypes, suggesting functional divergence within this family. As an
AAA
-ATPase, AtCDC48A likely serves to process the poly-ubiquitinated NLR substrate for final protein degradation by the 26S proteasome.
...
PMID:AtCDC48A is involved in the turnover of an NLR immune receptor. 2734 Sep 41
Mitochondria and autophagy play important roles in the networks that regulate plant leaf senescence and cell death. However, the molecular mechanisms underlying the interactions between mitochondrial signaling and autophagy are currently not well understood. This study characterized the function of the Arabidopsis (
Arabidopsis thaliana
) mitochondrial
AAA
-protease gene
FtSH4
in regulating autophagy and senescence, finding that FtSH4 mediates WRKY-dependent salicylic acid (SA) accumulation and signaling. Knockout of
FtSH4
in the
ftsh4-4
mutant resulted in severe leaf senescence, cell death, and high autophagy levels. The level of SA increased dramatically in the
ftsh4-4
mutant. Expression of
nahG
in the
ftsh4-4
mutant led to decreased SA levels and suppressed the leaf senescence and cell death phenotypes. The transcript levels of several SA synthesis and signaling genes, including
SALICYLIC ACID
INDUCTION DEFICIENT2
(
SID2
),
NON-RACE-SPECIFIC DISEASE RESISTANCE1
(
NDR1
), and
NONEXPRESSOR OF PATHOGENESIS-RELATED PROTEINS1
(
NPR1
), increased significantly in the
ftsh4-4
mutants compared with the wild type. Loss of function of
SID2
,
NDR1
, or
NPR1
in the
ftsh4-4
mutant reversed the
ftsh4-4
senescence and autophagy phenotypes. Furthermore,
ftsh4-4
mutants had elevated levels of transcripts of several
WRKY
genes, including
WRKY40
,
WRKY46
,
WRKY51
,
WRKY60
,
WRKY63
, and
WRKY75
; all of these WRKY proteins can bind to the promoter of
SID2
Loss of function of
WRKY75
in the
ftsh4-4
mutants decreased the levels of SA and reversed the senescence phenotype. Taken together, these results suggest that the mitochondrial ATP-dependent protease FtSH4 may regulate the expression of
WRKY
genes by modifying the level of reactive oxygen species and the WRKY transcription factors that control SA synthesis and signaling in autophagy and senescence.
...
PMID:The Arabidopsis Mitochondrial Protease FtSH4 Is Involved in Leaf Senescence via Regulation of WRKY-Dependent Salicylic Acid Accumulation and Signaling. 2825 67
