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Study identified the dual specificity tyrosine-phosphorylation-regulated kinase 3 (DYRK3) as a protein with the ability to condense P-granule-like speckles in the cytosol and to prevent stress granule dissolution via its N-terminal domain when it is in a kinase-inactive form.
the lipid raft-dependent endocytosis process mediates C. neoformans internalization into HBMEC and the CD44 (show CD44 Proteins) protein of the hosts, cytoskeleton, and intracellular kinase-DYRK3 are involved in this process
DYRK1A (show DYRK1A Proteins) and DYRK3 promote cell survival through phosphorylation and activation of SIRT1 (show SIRT1 Proteins).
DYRK3 has roles in kinase activation, binding to CREB (show CREB1 Proteins), and hematopoietic progenitor cell survival
DYRK3, expression is strong in erythroid cells and testis, but is also detected in adult kidney and liver
DYRK3 dual-specificity kinase attenuates erythropoiesis during anemia
These results indicate that HIF-mediated induction of Insig-2 (show INSIG2 Proteins) and degradation of HMGCR (show HMGCR Proteins) are physiologically relevant events that guard against wasteful oxygen consumption and inappropriate cell growth during hypoxia.
these studies designate sterol-accelerated degradation of HMGCR (show HMGCR Proteins) as a potential therapeutic target for prevention of atherosclerosis and associated cardiovascular disease.
To eludicate the mechanisms underlying statin myotoxicity and HMGCR (show HMGCR Proteins) function in skeletal muscle, we developed the skeletal muscle-specific (show EIF3K Proteins) HMGCR (show HMGCR Proteins) knockout mice.
High-dose simvastatin inhibits HMGCoA reductase (show HMGCR Proteins) and prevents experimental hyperinflation lung injury by angioprotective and anti-inflammatory effects.
TSH can regulate the phosphorylation of HMGCR (show HMGCR Proteins) via AMPK (show PRKAA1 Proteins).
HMGCR (show HMGCR Proteins) proteasomal-degradation by IFN strictly requires the synthesis of endogenous 25-Hydroxycholesterol.
Increased cholesterol synthesis mediated by HMGCoA (show HMGCS2 Proteins)-R under inflammatory stress may be one of the mechanisms for intracellular lipid accumulation and statin resistance.
we consistently observe involvement of gp78 (show AMFR Proteins) in Insig-1 degradation, we find no substantive evidence to support roles for either gp78 (show AMFR Proteins) or TRC8 (show RNF139 Proteins) in the robust sterol-accelerated degradation of HMG-CoA reductase (show HMGCR Proteins).
Hepatocyte HMGCR (show HMGCR Proteins) is essential for the survival of mice, and its abrogation elicits hepatic steatosis with jaundice and hypoglycemia.
This gene product belongs to the DYRK family of dual-specificity protein kinases that catalyze autophosphorylation on serine/threonine and tyrosine residues. The members of this family share structural similarity, however, differ in their substrate specificity, suggesting their involvement in different cellular functions. The encoded protein has been shown to autophosphorylate on tyrosine residue and catalyze phosphorylation of histones H3 and H2B in vitro. Alternatively spliced transcript variants encoding different isoforms have been identified.
dual specificity tyrosine-phosphorylation-regulated kinase 3
, dual-specificity tyrosine-(Y)-phosphorylation regulated kinase 5
, protein kinase Dyrk3
, regulatory erythroid kinase
, 3-hydroxy-3-methylglutaryl-CoA reductase
, 3-hydroxy-3-methylglutaryl-coenzyme A reductase
, HMG-CoA reductase
, dual-specificity tyrosine-(Y)-phosphorylation regulated kinase 3
, ual-specificity tyrosine-(Y)-phosphorylation regulated kinase 3