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CAMK2_complex phosphorylates PLN at T17

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Status
Unreviewed
Relation
PhosphorylationatT17
Participants
CAMK2_complex FPLX:CAMK2_complexPLN HGNC:9080
Source
INDRA text mining, 44 sentences from 30 papers, admitted by jev:all_grounded3>=0.8
In projects
PLN mechanism map · Dilated cardiomyopathy 1P

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Evidence

Sentences as extracted by INDRA's readers, with the verifier's score.

Sentence Paper JEV
CaMKII phosphorylates PLN at Thr 17 , thereby relieving its inhibitory effect on the SERCA pump [ xref , xref ]. PMID 34073033 0.97
The first associations of Ser2814 phosphorylation (the CaMKII site) with SR Ca 2+ leak in diabetic cardiomyopathy were almost simultaneously made by Shao et al. [ xref ], who also described an increase in RyR2 phosphorylation at Ser2808/9 site (mainly phosphorylated by PKA), and Stolen et al. [ xref ], who described an increase in Ser2814 site phosphorylation and in CaMKII-dependent phosphorylation of Thr17 site of PLN. 0.96
It was discovered that during β-AR stimulation of mouse SANC, CaMKII was implicated in: the increase of SR Ca load via CaMKII-dependent phosphorylation of PLB at Thr 17 site; increase in diastolic RyR Ca release; increase in the DD rate and increase in SA node beating rate [ xref ]. PMID 19573534 0.96
It was discovered that during beta-AR stimulation of mouse SANC, CaMKII was implicated in : the increase of SR Ca load via CaMKII dependent phosphorylation of PLB at Thr 17 site; increase in diastolic RyR Ca release; increase in the DD rate and increase in SA node beating rate [XREF_BIBR]. PMID 19573534 0.96
An unexpected but rather interesting finding of our study was that following exposure to CyA, CaMKII-dependent phosphorylation of PLB at Thr 17 increases rapidly, whereas at Ser 16 , the PKA-dependent site, the increase in phosphorylation occurs gradually ( xref ). 0.96
When PLB becomes phosphorylated at Thr-17 by CaMKII, the inhibition is relieved, and Ca 2+ uptake of SR is accelerated [ xref ]. PMID 21876643 0.96
When PLB becomes phosphorylated at Thr-17 by CaMKII, the inhibition is relieved, and Ca2+ uptake of SR is accelerated [10]. PMID 21876643 0.95
Ca 2+ also activates CaMKII ( xref – xref ), which phosphorylates PLB at Thr 17 ( xref , xref ) and RyR ( xref – xref ). PMID 23362239 0.95
In healthy cardiac myocytes, CaMKII phosphorylates PLB at Thr-17 thereby partially reactivating depressed SR Ca 2+ -reuptake, which leads to an increase in SR Ca 2+ -content. PMID 23473775 0.95
Western blot results show that Ad-Kv4.3 transfection significantly reduced CaMKII autophosphorylation, CaMKII-dependent PLB phosphorylation at Thr17, and protein expression of NFATc3 and ANP ( xref ). PMID 30462989 0.95
A widely accepted sequential model of dual site PLB phosphorylation states that PKA-dependent phosphorylation of Ser(16) is obligatory to phosphorylation of Thr(17) by Ca(2+)/calmodulin-dependent kinase II, and mainly accounts for beta-adrenergic receptor mediated cardiac relaxation. PMID 11852250 0.95
PLB is phosphorylated by PKA on Ser16 and by CaMKII on Thr17. PMID 21345340 0.95
CaMKII, whose activation relies also on the exchange protein directly activated by cAMP (Epac) pathway, is able to phosphorylate PLB at Thr 17, leading also in this case to an acceleration of SR Ca 2+ uptake. PMID 28956314 0.95
PKA- and CaMKII-dependent phosphorylation of PLN at Ser16 and Thr17, respectively, relieves the inhibition and allows for increased Ca 2+ pumping into the SR. PMID 19481088 0.95
Ca 2+ also activates CaMKII, which phosphorylates PLB at Thr 17 and RyR. PMID 23362239 0.95
SERCA is maximally active at high, systolic [Ca 2+] or when PLB is phosphorylated at S16 or T17 by PKA or CaMKII, respectively. PMID 24436077 0.95
PLB is also phosphorylated by CaMKII (at Thr17) and this may synergize with PKA dependent SERCA stimulation in the overall beta-AR stimulation of the heart (XREF_FIG). PMID 19818946 0.94
181 Cardiac phospholamban is phosphorylated at Ser16 by PKA and at Thr17 by CaMKII, but the relative importance of these dual phosphorylation sites in the regulation of cardiac contractility is difficult to assess. PMID 23090087 0.94
There was a general agreement that CaMKII phosphorylates PLB at Thr-17. PMID 28578382 0.94
Dephosphorylated PLN inhibits SERCA2a, whereas phosphorylation of PLN at either the Ser16 site by PKA or the Thr17 site by CaMKII reverses this inhibition, thus increasing SERCA2a activity and the rate of Ca2+ uptake by the SR.. PMID 16648892 0.94
We will review here the role of CaMKII-dependent phosphorylation of PLN at Thr 17 on cardiac function under physiological and pathological conditions. PMID 24550830 0.94
There was a general agreement that CaMKII phosphorylates PLB at Thr 17 46. PMID 28578382 0.94
The results showed a progressive increase in the level of CaMKII autophosphorylation and CaMKII-dependent phospholamban (PLB) phosphorylation at Thr-17 with unchanged total proteins, indicating an increased overall and membrane-localized CaMKII activation. PMID 30462989 0.93
Likewise, CaMKII activity and CaMKII-dependent phosphorylation of PLN at Thr17 were both decreased and to comparable levels. PMID 25149095 0.93
The present study was undertaken to examine the status of PLB phosphorylation after ischemia and reperfusion and to provide evidence about the possible role of the phosphorylation of Thr(17) PLB residue on the recovery of contractility and relaxation after a period of ischemia. Experiments were performed in Langendorff perfused hearts from Wistar rats. Hearts were submitted to a protocol of global normothermic ischemia and reperfusion. The results showed that (1) the phosphorylation of Ser(16) and Thr(17) residues of PLB increased at the end of the ischemia and the onset of reperfusion, respectively. The increase in Thr(17) phosphorylation was associated with a recovery of relaxation to preischemic values. This recovery occurred in spite of the fact that contractility was depressed. (2) The reperfusion-induced increase in Thr(17) phosphorylation was dependent on Ca(2+) entry to the cardiac cell. This Ca(2+) influx would mainly occur by the coupled activation of the Na(+)/H(+) exchanger and the Na(+)/Ca(2+) exchanger working in the reverse mode, since phosphorylation of Thr(17) was decreased by inhibition of these exchangers and not affected by blockade of the L-type Ca(2+) channels. (3) Specific inhibition of CaMKII by KN93 significantly decreased Thr(17) phosphorylation. PMID 27520671 0.93
In addition, PPM1L specifically dephosphorylates CaMKII dependent Thr-17 phosphorylation on PLB but shows no effect on the neighboring PKA dependent Ser-16 phosphorylation [ xref ]. PMID 34091011 0.93
The present study was undertaken to examine the status of PLB phosphorylation after ischemia and reperfusion and to provide evidence about the possible role of the phosphorylation of Thr17 PLB residue on the recovery of contractility and relaxation after a period of ischemia. Experiments were performed in Langendorff perfused hearts from Wistar rats. Hearts were submitted to a protocol of global normothermic ischemia and reperfusion. The results showed that (1) the phosphorylation of Ser16 and Thr17 residues of PLB increased at the end of the ischemia and the onset of reperfusion, respectively. The increase in Thr17 phosphorylation was associated with a recovery of relaxation to preischemic values. This recovery occurred in spite of the fact that contractility was depressed. (2) The reperfusion-induced increase in Thr17 phosphorylation was dependent on Ca2+ entry to the cardiac cell. This Ca2+ influx would mainly occur by the coupled activation of the Na+ / H+ exchanger and the Na+ / Ca2+ exchanger working in the reverse mode, since phosphorylation of Thr17 was decreased by inhibition of these exchangers and not affected by blockade of the L-type Ca2+ channels. (3) Specific inhibition of CaMKII by KN93 significantly decreased Thr17 phosphorylation. PMID 15524173 0.92
Collectively, our data indicates that chronic aldosterone infusion decreased PKA-dependent phosphorylation of PLN at Ser16 and CaMKII-dependent phosphorylation of PLN at Thr17, presumably followed by β-adrenergic signaling downregulation, and subsequently suppressed SERCA2a protein expression. PMID 25149095 0.92
In addition, CaMKII phosphorylates the sarcoplasmic reticulum (SR) membrane protein-complex phospholamban (PLN) at Thr17 [ xref ], leading to increased calcium reuptake from the cytosol into the SR via SERCA2a [ xref ]. PMID 29905892 0.92
However, as noted above, PLN is not only phosphorylated by PKA, at Ser 16, but also by CaMKII at Thr 17, during beta1-adrenergic stimulation. PMID 24550830 0.92
Aldosterone infusion also increased myocardial oxidative stress, decreased SERCA2a protein expression, decreased PKA-dependent PLN phosphorylation at Ser16, and decreased CaMKII-dependent phosphorylation of PLN at Thr17. PMID 25149095 0.92
Collectively, our data indicates that chronic aldosterone infusion decreased PKA dependent phosphorylation of PLN at Ser16 and CaMKII dependent phosphorylation of PLN at Thr17, presumably followed by beta-adrenergic signaling downregulation, and subsequently suppressed SERCA2a protein expression. PMID 25149095 0.92
Elevated levels of cytosolic Ca 2+ result in the activation of CaMKII, which phosphorylates the residue Thr 17 of PLN. PMID 19365280 0.91
The effect of CaMKII-dependent PLN-T17 phosphorylation on SERCA2a activity seems to be rather minor in atrial CMs as Ca 2+ elimination kinetics are even accelerated upon an inhibition of CaMKII in the setting of an elevated late I Na . PMID 25990311 0.90
Although total phospholamban (PLN) protein expression was unchanged, there was decreased expression of PKA-dependent PLN phosphorylation at Ser16 and CaMKII-dependent PLN phosphorylation at Thr17. PMID 25149095 0.89
Earlier reports demonstrated that the presence of the inhibitor of CaMKII, KN-93 reduced the phosphorylation of PLN at Thr 17 during early reperfusion which was associated with a better mechanical recovery after ischemia [35,36]. PMID 29407107 0.89
We observed that RARalpha deletion induced decrease in the phosphorylation of PLB at Ser16 was restored by 8-Br-cAMP, and the reduced phosphorylation of PLB at Thr17 was restored by activated CaMKII and SC79 (XREF_SUPPLEMENTARY). PMID 27539860 0.89
Phosphorylation of PLN by CaMKII at Thr17 site will relieve its inhibition on SERCA2 and consequently increase SERCA2 calcium uptake activity. PMID 28662005 0.84
Another study, in a rabbit model of aortic constriction, measured increases of 63% in total CaMKII protein and 43% in autophosphorylated CaMKII with an increase in phosphorylation of PLB at T17 (and decreased phosphorylation of S16) and both S2809 and S2815 of RyR2 were phosphorylated (Ai et al., 2005). PMID 19345240 0.84
Because BPA has been shown to influence SR Ca 2+ reuptake via increasing CAMKII phosphorylation of PLN at threonine 17 ( xref ), we examined the dose-dependent effect of BPA (2-min exposure) on CAMKII phosphorylation of PLN. PMID 24569941 0.84
PLN phosphorylation by CaMKII at Thr17 stimulates SERCA, increasing Ca 2+ uptake into the SR [XREF_BIBR - XREF_BIBR]. PMID 21443856 0.82
PLN phosphorylation by CaMKII at Thr17 stimulates SERCA, increasing Ca 2+ uptake into the SR [ xref – xref ]. PMID 21443856 0.82
Phosphorylation of PLN by cAMP dependent protein kinase (PKA) or cGMP dependent protein kinase (PKG) at Ser16, or by CaMKII at Thr17 removes its inhibitory effects on SERCA, thereby increasing Ca 2+ uptake into the SR and contributing to relaxation [XREF_BIBR - XREF_BIBR]. PMID 21443856 0.81
CaMKII also phosphorylates PLN at Thr 17 and this site is the most commonly used marker of endogenous CaMKII activity. PMID 23789646 0.81