Protein kinase D1

From Wikipedia, the free encyclopedia

Protein kinase D1

Identifiers

PRKD1; PKC-MU; PKCM; PKD; PRKCM

External IDs

OMIM: 605435 MGI: 99879 HomoloGene: 55680

Gene ontology
Molecular Function:	• nucleotide binding • protein serine/threonine kinase activity • atypical protein kinase C activity • protein binding • ATP binding • zinc ion binding • transferase activity • diacylglycerol binding • metal ion binding
Cellular Component:	• Golgi apparatus • cytosol • plasma membrane • integral to plasma membrane
Biological Process:	• protein amino acid phosphorylation • intracellular signaling cascade • cell proliferation

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_002742 (mRNA)
NP_002733 (protein)

NM_008858 (mRNA)
NP_032884 (protein)

Location

Chr 14: 29.12 - 29.47 Mb

Chr 12: 51.22 - 51.57 Mb

Pubmed search

[1]

[2]

Protein kinase D1, also known as PRKD1, is a human gene.^[1]

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]^[1]

[edit] References

^ ^a ^b Entrez Gene: PRKD1 protein kinase D1.

[edit] Further reading

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