PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 15084589-4 2004 Here we show that oxidative stress induces PKC-dependent activation loop Ser(744) and Ser(748) phosphorylation to mediate dose- and time-dependent activation of PKD, both endogenously expressed in Swiss 3T3 cells and stably overexpressed in Swiss 3T3-GFP.PKD cells. Serine 73-76 protein kinase D1 Mus musculus 161-164 15623513-3 2005 Protein kinase D1 (PKD1) was activated after TCR engagement, interacted with HDAC7, and phosphorylated three serines (Ser155, Ser318, and Ser448) at its N terminus, leading to its export from the nucleus. Serine 109-116 protein kinase D1 Mus musculus 0-17 15623513-3 2005 Protein kinase D1 (PKD1) was activated after TCR engagement, interacted with HDAC7, and phosphorylated three serines (Ser155, Ser318, and Ser448) at its N terminus, leading to its export from the nucleus. Serine 109-116 protein kinase D1 Mus musculus 19-23 15084589-4 2004 Here we show that oxidative stress induces PKC-dependent activation loop Ser(744) and Ser(748) phosphorylation to mediate dose- and time-dependent activation of PKD, both endogenously expressed in Swiss 3T3 cells and stably overexpressed in Swiss 3T3-GFP.PKD cells. Serine 86-89 protein kinase D1 Mus musculus 161-164 15084589-12 2004 Taken together, these results indicate that PKC-mediated PKD Ser(744) and Ser(748) phosphorylation induced by oxidative stress integrates PKD activation with redistribution to the nucleus. Serine 61-64 protein kinase D1 Mus musculus 57-60 15084589-12 2004 Taken together, these results indicate that PKC-mediated PKD Ser(744) and Ser(748) phosphorylation induced by oxidative stress integrates PKD activation with redistribution to the nucleus. Serine 61-64 protein kinase D1 Mus musculus 138-141 15084589-12 2004 Taken together, these results indicate that PKC-mediated PKD Ser(744) and Ser(748) phosphorylation induced by oxidative stress integrates PKD activation with redistribution to the nucleus. Serine 74-77 protein kinase D1 Mus musculus 138-141 31591827-4 2019 Indeed, we find that the P2Y1 receptor agonists, MRS2365 and ATP induce, PKD1 phosphorylation at serine 916 in mouse islets. Serine 97-103 protein kinase D1 Mus musculus 73-77 10197446-8 1999 These results provide direct evidence that PKD becomes activated in vivo as a consequence of PKC-mediated phosphorylation of serines 744 and 748. Serine 125-132 protein kinase D1 Mus musculus 43-46 33381112-1 2020 Rationale: Protein kinase D (PKD) is a serine/threonine kinase family that is involved in a wide array of signaling pathways. Serine 39-45 protein kinase D1 Mus musculus 11-27 33381112-1 2020 Rationale: Protein kinase D (PKD) is a serine/threonine kinase family that is involved in a wide array of signaling pathways. Serine 39-45 protein kinase D1 Mus musculus 29-32 11514571-5 2001 Concomitantly, these stimuli induced PKD phosphorylation at Ser(744), Ser(748), and Ser(916). Serine 60-63 protein kinase D1 Mus musculus 37-40 10197446-2 1999 Structural comparison of the PKD catalytic domain with other kinases reveals a close similarity with MEK family kinases, which are activated upon phosphorylation of key serine and threonine residues in a region termed the activation loop. Serine 169-175 protein kinase D1 Mus musculus 29-32 10197446-3 1999 To study the regulation of PKD, we transfected mutant PKD cDNAs in which putative activation loop serine residues 744 and 748 were mutated to either alanine or glutamic acid into COS-7 cells. Serine 98-104 protein kinase D1 Mus musculus 54-57 10197446-4 1999 Replacement of serines 744 and 748 with alanine prevented activation of the overexpressed PKD form upon phorbol ester treatment of cells, whereas replacement with glutamic acid results in full constitutive activation. Serine 15-22 protein kinase D1 Mus musculus 90-93 10197446-6 1999 In vivo 32P-labeling and two-dimensional phosphopeptide mapping of PKD and catalytically inactive PKD mutants at serine 744, 748 or at both residues revealed that phorbol ester-sensitive phosphopeptides could be selectively eliminated from patterns observed as a result of these mutations. Serine 113-119 protein kinase D1 Mus musculus 67-70 10197446-6 1999 In vivo 32P-labeling and two-dimensional phosphopeptide mapping of PKD and catalytically inactive PKD mutants at serine 744, 748 or at both residues revealed that phorbol ester-sensitive phosphopeptides could be selectively eliminated from patterns observed as a result of these mutations. Serine 113-119 protein kinase D1 Mus musculus 98-101 33675805-6 2021 Further studies revealed that blockade of PKD1 significantly increased phosphorylation of SREBP1c at serine 372 site. Serine 101-107 protein kinase D1 Mus musculus 42-46 22636676-4 2012 Using immunoprecipitation, we showed that, in contracting cardiomyocytes, PKD binds to cMyBP-C and phosphorylates it at Ser(315). Serine 120-123 protein kinase D1 Mus musculus 74-77 29669813-4 2018 Here we report that protein kinase D (PKD) phosphorylates only one serine of cTnI Ser-23/24. Serine 67-73 protein kinase D1 Mus musculus 20-36 29669813-4 2018 Here we report that protein kinase D (PKD) phosphorylates only one serine of cTnI Ser-23/24. Serine 67-73 protein kinase D1 Mus musculus 38-41 29669813-4 2018 Here we report that protein kinase D (PKD) phosphorylates only one serine of cTnI Ser-23/24. Serine 82-85 protein kinase D1 Mus musculus 20-36 29669813-4 2018 Here we report that protein kinase D (PKD) phosphorylates only one serine of cTnI Ser-23/24. Serine 82-85 protein kinase D1 Mus musculus 38-41 22820510-10 2012 Oleate induces PKD phosphorylation at residues Ser-744/748 and Ser-916 in WT but not Gpr40 (-/-) islets. Serine 47-50 protein kinase D1 Mus musculus 15-18 29669813-6 2018 Phos-tag gels, Western blotting, and high-resolution MS revealed that PKD produced >90% monophosphorylation of cTnI, primarily at Ser-24, whereas PKA led to cTnI bisphosphorylation exclusively. Serine 133-136 protein kinase D1 Mus musculus 70-73 23253477-5 2012 The VEGF-induced translocation of Syx from EC junctions was caused by PKD1 (protein kinase D1)-mediated phosphorylation of Syx at Ser(806), which reduced Syx association to its junctional anchors. Serine 130-133 protein kinase D1 Mus musculus 70-74 23253477-5 2012 The VEGF-induced translocation of Syx from EC junctions was caused by PKD1 (protein kinase D1)-mediated phosphorylation of Syx at Ser(806), which reduced Syx association to its junctional anchors. Serine 130-133 protein kinase D1 Mus musculus 76-93 22636676-9 2012 Furthermore, the phosphorylation of both PKD-Ser(916) and cMyBP-C-Ser(315) was contraction frequency-dependent, suggesting that PKD-mediated cMyBP-C phosphorylation is operational primarily during periods of increased contractile activity. Serine 45-48 protein kinase D1 Mus musculus 41-44 20018870-1 2010 Protein kinase D (PKD), a serine/threonine kinase with emerging cardiovascular functions, phosphorylates cardiac troponin I (cTnI) at Ser(22)/Ser(23), reduces myofilament Ca(2+) sensitivity, and accelerates cross-bridge cycle kinetics. Serine 134-137 protein kinase D1 Mus musculus 0-16 21051537-5 2011 Transgenic PKD1 exhibited constitutive catalytic activity and phosphorylation at the activation loop residues Ser(744) and Ser(748) and on the autophosphorylation site, Ser(916). Serine 110-113 protein kinase D1 Mus musculus 11-15 21051537-5 2011 Transgenic PKD1 exhibited constitutive catalytic activity and phosphorylation at the activation loop residues Ser(744) and Ser(748) and on the autophosphorylation site, Ser(916). Serine 123-126 protein kinase D1 Mus musculus 11-15 21051537-5 2011 Transgenic PKD1 exhibited constitutive catalytic activity and phosphorylation at the activation loop residues Ser(744) and Ser(748) and on the autophosphorylation site, Ser(916). Serine 123-126 protein kinase D1 Mus musculus 11-15 20018870-4 2010 In skinned myocardium from wild-type (WT) mice, PKD increased cTnI phosphorylation at Ser(22)/Ser(23) and decreased the Ca(2+) sensitivity of force. Serine 86-89 protein kinase D1 Mus musculus 48-51 20018870-4 2010 In skinned myocardium from wild-type (WT) mice, PKD increased cTnI phosphorylation at Ser(22)/Ser(23) and decreased the Ca(2+) sensitivity of force. Serine 94-97 protein kinase D1 Mus musculus 48-51 20018870-9 2010 Furthermore, PKD phosphorylated Ser(302) selectively and to a similar extent in native cMyBP-C of skinned myocardium from WT and cTnI-Ala(2) mice, and this phosphorylation occurred throughout the C-zones of sarcomeric A-bands. Serine 32-35 protein kinase D1 Mus musculus 13-16 20018870-10 2010 In conclusion, PKD reduces myofilament Ca(2+) sensitivity through cTnI phosphorylation at Ser(22)/Ser(23) but accelerates cross-bridge cycle kinetics by a distinct mechanism. Serine 90-93 protein kinase D1 Mus musculus 15-18 20018870-10 2010 In conclusion, PKD reduces myofilament Ca(2+) sensitivity through cTnI phosphorylation at Ser(22)/Ser(23) but accelerates cross-bridge cycle kinetics by a distinct mechanism. Serine 98-101 protein kinase D1 Mus musculus 15-18 20018870-11 2010 PKD phosphorylates cMyBP-C at Ser(302), which may mediate the latter effect. Serine 30-33 protein kinase D1 Mus musculus 0-3 20018870-1 2010 Protein kinase D (PKD), a serine/threonine kinase with emerging cardiovascular functions, phosphorylates cardiac troponin I (cTnI) at Ser(22)/Ser(23), reduces myofilament Ca(2+) sensitivity, and accelerates cross-bridge cycle kinetics. Serine 134-137 protein kinase D1 Mus musculus 18-21 20018870-1 2010 Protein kinase D (PKD), a serine/threonine kinase with emerging cardiovascular functions, phosphorylates cardiac troponin I (cTnI) at Ser(22)/Ser(23), reduces myofilament Ca(2+) sensitivity, and accelerates cross-bridge cycle kinetics. Serine 142-145 protein kinase D1 Mus musculus 0-16 20018870-1 2010 Protein kinase D (PKD), a serine/threonine kinase with emerging cardiovascular functions, phosphorylates cardiac troponin I (cTnI) at Ser(22)/Ser(23), reduces myofilament Ca(2+) sensitivity, and accelerates cross-bridge cycle kinetics. Serine 142-145 protein kinase D1 Mus musculus 18-21 20018870-2 2010 Whether PKD regulates cardiac myofilament function entirely through cTnI phosphorylation at Ser(22)/Ser(23) remains to be established. Serine 92-95 protein kinase D1 Mus musculus 8-11 18378685-7 2008 Pasteuralla multocida toxin (PMT), a direct Galpha(q) agonist that induces robust cardiomyocyte hypertrophy, also activates the PKD-CREB-Ser(133) phosphorylation pathway, leading to the accumulation of active PKD and Ser(133)-phosphorylated CREB in the nucleus, activation of a CRE-responsive promoter, and increased Bcl-2 (CREB target gene) expression in cardiomyocyte cultures. Serine 217-220 protein kinase D1 Mus musculus 128-131 18378685-9 2008 Collectively, these studies identify a novel Galpha(q)-PKCdelta-PKD-CREB-Ser(133) phosphorylation pathway that is predicted to contribute to cardiac remodeling and could be targeted for therapeutic advantage in the setting of heart failure phenotypes. Serine 73-76 protein kinase D1 Mus musculus 64-67 19183835-6 2009 Furthermore, the disruption of actin cytoskeleton induced phosphorylation of 744/748 serine within the activation loop of PKD in a dose-dependent manner. Serine 85-91 protein kinase D1 Mus musculus 122-125 18845612-9 2008 Utilizing bioinformatics we predicted that extracellular regulated protein-serine kinase (ERK1/2), inhibitor of nuclear factor (NF)-kappaB protein-serine kinase beta (IKKbeta) and protein kinase D (PKD) may phosphorylate ACC2 at Ser-221 but during in vitro phosphorylation assays only AMPK phosphorylated ACC2. Serine 229-232 protein kinase D1 Mus musculus 198-201 18378685-3 2008 We show that thrombin activates a PKCdelta-PKD pathway leading to CREB-Ser(133) phosphorylation in cardiomyocytes and cardiac fibroblasts. Serine 71-74 protein kinase D1 Mus musculus 43-46 18378685-4 2008 alpha(1)-Adrenergic receptors also activate a PKCdelta-PKD-CREB-Ser(133) phosphorylation pathway in cardiomyocytes. Serine 64-67 protein kinase D1 Mus musculus 55-58 18378685-7 2008 Pasteuralla multocida toxin (PMT), a direct Galpha(q) agonist that induces robust cardiomyocyte hypertrophy, also activates the PKD-CREB-Ser(133) phosphorylation pathway, leading to the accumulation of active PKD and Ser(133)-phosphorylated CREB in the nucleus, activation of a CRE-responsive promoter, and increased Bcl-2 (CREB target gene) expression in cardiomyocyte cultures. Serine 137-140 protein kinase D1 Mus musculus 128-131 18378685-7 2008 Pasteuralla multocida toxin (PMT), a direct Galpha(q) agonist that induces robust cardiomyocyte hypertrophy, also activates the PKD-CREB-Ser(133) phosphorylation pathway, leading to the accumulation of active PKD and Ser(133)-phosphorylated CREB in the nucleus, activation of a CRE-responsive promoter, and increased Bcl-2 (CREB target gene) expression in cardiomyocyte cultures. Serine 137-140 protein kinase D1 Mus musculus 209-212