Protein kinase D1

Protein kinase D1

Protein kinase D1, also known as PRKD1, is a human gene.cite web | title = Entrez Gene: PRKD1 protein kinase D1| url =| accessdate = ]

section_title =
summary_text = Members of the protein kinase C (PKC) family function in many extracellular receptor-mediated signal transduction pathways. See PRKCA (MIM 176960) for further background information. The PRKCM gene encodes a cytosolic serine-threonine kinase that binds to the trans-Golgi network and regulates the fission of transport carriers specifically destined to the cell surface. [supplied by OMIM] cite web | title = Entrez Gene: PRKD1 protein kinase D1| url =| accessdate = ]


Further reading

citations =
*cite journal | author=Van Lint J, Rykx A, Maeda Y, "et al." |title=Protein kinase D: an intracellular traffic regulator on the move. |journal=Trends Cell Biol. |volume=12 |issue= 4 |pages= 193–200 |year= 2002 |pmid= 11978539 |doi=
*cite journal | author=Busch H, Eisenhart-Rothe BV |title= [Old and new dangers of blood transfusion (author's transl)] |journal=MMW, Münchener medizinische Wochenschrift |volume=118 |issue= 22 |pages= 713–8 |year= 1976 |pmid= 5668 |doi=
*cite journal | author=Jakobovits A, Rosenthal A, Capon DJ |title=Trans-activation of HIV-1 LTR-directed gene expression by tat requires protein kinase C. |journal=EMBO J. |volume=9 |issue= 4 |pages= 1165–70 |year= 1990 |pmid= 2182321 |doi=
*cite journal | author=Davis RJ, Czech MP |title=Tumor-promoting phorbol diesters cause the phosphorylation of epidermal growth factor receptors in normal human fibroblasts at threonine-654. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=82 |issue= 7 |pages= 1974–8 |year= 1985 |pmid= 2984676 |doi=
*cite journal | author=Davis RJ, Czech MP |title=Platelet-derived growth factor mimics phorbol diester action on epidermal growth factor receptor phosphorylation at threonine-654. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=82 |issue= 12 |pages= 4080–4 |year= 1985 |pmid= 2987962 |doi=
*cite journal | author=Johannes FJ, Prestle J, Eis S, "et al." |title=PKCu is a novel, atypical member of the protein kinase C family. |journal=J. Biol. Chem. |volume=269 |issue= 8 |pages= 6140–8 |year= 1994 |pmid= 8119958 |doi=
*cite journal | author=Conant K, Ma M, Nath A, Major EO |title=Extracellular human immunodeficiency virus type 1 Tat protein is associated with an increase in both NF-kappa B binding and protein kinase C activity in primary human astrocytes. |journal=J. Virol. |volume=70 |issue= 3 |pages= 1384–9 |year= 1996 |pmid= 8627654 |doi=
*cite journal | author=Sidorenko SP, Law CL, Klaus SJ, "et al." |title=Protein kinase C mu (PKC mu) associates with the B cell antigen receptor complex and regulates lymphocyte signaling. |journal=Immunity |volume=5 |issue= 4 |pages= 353–63 |year= 1996 |pmid= 8885868 |doi=
*cite journal | author=Holmes AM |title=In vitro phosphorylation of human immunodeficiency virus type 1 Tat protein by protein kinase C: evidence for the phosphorylation of amino acid residue serine-46. |journal=Arch. Biochem. Biophys. |volume=335 |issue= 1 |pages= 8–12 |year= 1996 |pmid= 8914829 |doi= 10.1006/abbi.1996.0476
*cite journal | author=Borgatti P, Zauli G, Cantley LC, Capitani S |title=Extracellular HIV-1 Tat protein induces a rapid and selective activation of protein kinase C (PKC)-alpha, and -epsilon and -zeta isoforms in PC12 cells. |journal=Biochem. Biophys. Res. Commun. |volume=242 |issue= 2 |pages= 332–7 |year= 1998 |pmid= 9446795 |doi=
*cite journal | author=Zidovetzki R, Wang JL, Chen P, "et al." |title=Human immunodeficiency virus Tat protein induces interleukin 6 mRNA expression in human brain endothelial cells via protein kinase C- and cAMP-dependent protein kinase pathways. |journal=AIDS Res. Hum. Retroviruses |volume=14 |issue= 10 |pages= 825–33 |year= 1998 |pmid= 9671211 |doi=
*cite journal | author=Waldron RT, Iglesias T, Rozengurt E |title=The pleckstrin homology domain of protein kinase D interacts preferentially with the eta isoform of protein kinase C. |journal=J. Biol. Chem. |volume=274 |issue= 14 |pages= 9224–30 |year= 1999 |pmid= 10092595 |doi=
*cite journal | author=Hausser A, Storz P, Link G, "et al." |title=Protein kinase C mu is negatively regulated by 14-3-3 signal transduction proteins. |journal=J. Biol. Chem. |volume=274 |issue= 14 |pages= 9258–64 |year= 1999 |pmid= 10092600 |doi=
*cite journal | author=Jamora C, Yamanouye N, Van Lint J, "et al." |title=Gbetagamma-mediated regulation of Golgi organization is through the direct activation of protein kinase D. |journal=Cell |volume=98 |issue= 1 |pages= 59–68 |year= 1999 |pmid= 10412981 |doi= 10.1016/S0092-8674(00)80606-6
*cite journal | author=Bagowski CP, Stein-Gerlach M, Choidas A, Ullrich A |title=Cell-type specific phosphorylation of threonines T654 and T669 by PKD defines the signal capacity of the EGF receptor. |journal=EMBO J. |volume=18 |issue= 20 |pages= 5567–76 |year= 1999 |pmid= 10523301 |doi= 10.1093/emboj/18.20.5567
*cite journal | author=Johannes FJ, Hausser A, Storz P, "et al." |title=Bruton's tyrosine kinase (Btk) associates with protein kinase C mu. |journal=FEBS Lett. |volume=461 |issue= 1-2 |pages= 68–72 |year= 1999 |pmid= 10561498 |doi=
*cite journal | author=Storz P, Hausser A, Link G, "et al." |title=Protein kinase C [micro] is regulated by the multifunctional chaperon protein p32. |journal=J. Biol. Chem. |volume=275 |issue= 32 |pages= 24601–7 |year= 2000 |pmid= 10831594 |doi= 10.1074/jbc.M002964200
*cite journal | author=Mayne M, Holden CP, Nath A, Geiger JD |title=Release of calcium from inositol 1,4,5-trisphosphate receptor-regulated stores by HIV-1 Tat regulates TNF-alpha production in human macrophages. |journal=J. Immunol. |volume=164 |issue= 12 |pages= 6538–42 |year= 2000 |pmid= 10843712 |doi=
*cite journal | author=Matthews SA, Iglesias T, Rozengurt E, Cantrell D |title=Spatial and temporal regulation of protein kinase D (PKD). |journal=EMBO J. |volume=19 |issue= 12 |pages= 2935–45 |year= 2000 |pmid= 10856238 |doi= 10.1093/emboj/19.12.2935
*cite journal | author=Vertommen D, Rider M, Ni Y, "et al." |title=Regulation of protein kinase D by multisite phosphorylation. Identification of phosphorylation sites by mass spectrometry and characterization by site-directed mutagenesis. |journal=J. Biol. Chem. |volume=275 |issue= 26 |pages= 19567–76 |year= 2000 |pmid= 10867018 |doi= 10.1074/jbc.M001357200

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