Regular ArticleProtein Kinase D Is a Downstream Target of Protein Kinase Cθ☆
References (35)
J Biol. Chem.
(1995)- et al.
Trends Biochem. Sci.
(1994) - et al.
Semin. Immunol.
(2001) - et al.
J. Biol. Chem.
(1997) - et al.
Metabolism
(2001) - et al.
J. Biol. Chem.
(1994) - et al.
J. Biol. Chem.
(1997) - et al.
FEBS Lett.
(1998) - et al.
J. Biol. Chem.
(2000) - et al.
J. Biol. Chem.
(2001)
J. Biol. Chem.
Journal of Biol. Chem.
J. Biol. Chem.
J. Biol. Chem.
J. Biol. Chem.
Immunity
J. Biol. Chem.
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Protein kinase D1 — A targetable mediator of pancreatic cancer development
2024, Biochimica et Biophysica Acta - Molecular Cell ResearchEvaluating the current status of protein kinase C (PKC)-protein kinase D (PKD) signalling axis as a novel therapeutic target in ovarian cancer
2021, Biochimica et Biophysica Acta - Reviews on CancerCitation Excerpt :Earlier studies using intact cells such as human lymphocytes, HeK293 and HeLa showed that treating the cells with different external stimuli such as phorbol esters and DAG induced PKD activation as assessed by in vitro kinase assay and that PKD phosphorylation could be selectively inhibited by treating the cells with PKC inhibitors including GFI and Ro31-8220 [85,86]. Moreover, constitutively active PKC isoforms (PKCs δ, ε and ε) strongly activated PKD in an extracellular stimulus-independent manner [87,88]. Furthermore, PKC-dependent activation of PKD by various stimuli such as bombesin, endothelin and growth factors have been observed in many cells such as fibroblasts [89], platelets [90] and several tumors such as carcinomas of the lung [91] and pancreas [92].
VLDL-activated cell signaling pathways that stimulate adrenal cell aldosterone production
2016, Molecular and Cellular EndocrinologyCitation Excerpt :PKD possesses two cysteine-rich domains that allow its direct activation by DAG and additionally the enzyme can be transphosphorylated and activated by novel PKC isoenzymes (Wang, 2006). Therefore, given the parallels between the signaling pathways activated by VLDL and AngII, as well as the fact that PKD is a downstream mediator of PKC action (Romero et al., 2006; Matthews et al., 2000; Yuan et al., 2002), it seems possible that VLDL might also activate PKD. Experiments are in progress to investigate this possibility.
Protein kinase C and Src family kinases mediate angiotensin II-induced protein kinase D activation and acute aldosterone production
2014, Molecular and Cellular EndocrinologyPKCθ activation in pancreatic acinar cells by gastrointestinal hormones/neurotransmitters and growth factors is needed for stimulation of numerous important cellular signaling cascades
2011, Biochimica et Biophysica Acta - Molecular Cell ResearchCitation Excerpt :These results demonstrate that not only do the CCKA receptor states differ in their coupling to pancreatic cellular kinase cascades, but even with different novel PKCs in the same cell, the CCKAR receptor activation states show differential coupling. In other cells activated by various stimulants, PKCθ activation is known to be important in the stimulation of a number of important cellular signaling proteins [5], including Src, [41], PKD [42], Raf [42,68], CARMA and IKK/NFκβ [43], Cbl [44,47], 14-3-3 [45], Blc-10 [46], MALT-1 [47], PI3K [19], ERK [13], IRS-1 [12], p125FAK [69] and Akt [12]. In pancreatic acinar cells, stimulation by growth factors and GPCRs causes activation of a number of these cellular signaling proteins, including Src kinases [64], PKD [18,49], Raf [70], IKKα/β/NFκβ [49], PI3K [19,71], p44/42 MAPKs [72], p125FAK, PYK2 and paxillin and Akt [19], which have been shown to be important in mediating cell activation, enzyme secretion [73,74], proliferation and apoptosis [19], cell survival [75] and protein synthesis [76].
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This work was supported by National Health Institute Grants DK 55003, DK56930, DK 17294, and NCI Grant P50 CA 90388-01.
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Supported by NIH National Research Service Award F32 CA84658-01A1.
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Supported by the U.S. Public Health Service Grant RO-1 AG14992.
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To whom all correspondence should be addressed at Department of Medicine, Warren Hall, Room 11-124, UCLA School of Medicine, 900 Veteran Avenue, Los Angeles, CA 90095-1786. Fax: 310-267-2399. E-mail: [email protected].