Protein kinase D1

Protein kinase D1
Identifiers
Symbols	PRKD1 ; PKC-MU; PKCM; PKD; PRKCM
External IDs	OMIM: 605435 MGI: 99879 HomoloGene: 55680 ChEMBL: 3863 GeneCards: PRKD1 Gene
EC number	2.7.11.13
Gene ontology Molecular function • protein serine/threonine kinase activity • protein kinase C activity • protein binding • ATP binding • identical protein binding • metal ion binding Cellular component • nucleus • cytoplasm • Golgi apparatus • trans-Golgi network • cytosol • plasma membrane • integral component of plasma membrane • cell-cell junction • cell cortex Biological process • angiogenesis • positive regulation of endothelial cell proliferation • sphingolipid metabolic process • apoptotic process • inflammatory response • Golgi organization • signal transduction • integrin-mediated signaling pathway • cell proliferation • positive regulation of endothelial cell migration • regulation of keratinocyte proliferation • positive regulation of neuron projection development • peptidyl-serine phosphorylation • sphingolipid biosynthetic process • positive regulation of CREB transcription factor activity • positive regulation of peptidyl-serine phosphorylation • cellular response to oxidative stress • intracellular signal transduction • cellular response to vascular endothelial growth factor stimulus • positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway • positive regulation of I-kappaB kinase/NF-kappaB signaling • positive regulation of blood vessel endothelial cell migration • small molecule metabolic process • innate immune response • positive regulation of osteoblast differentiation • positive regulation of angiogenesis • negative regulation of endocytosis • positive regulation of transcription from RNA polymerase II promoter • protein autophosphorylation • vascular endothelial growth factor receptor signaling pathway • Golgi vesicle transport • positive regulation of NF-kappaB transcription factor activity • regulation of release of sequestered calcium ion into cytosol • negative regulation of cell death • protein kinase D signaling • positive regulation of histone deacetylase activity • positive regulation of endothelial cell chemotaxis • regulation of integrin-mediated signaling pathway Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	5587	18760
Ensembl	ENSG00000184304	ENSMUSG00000002688
UniProt	Q15139	Q62101
RefSeq (mRNA)	NM_002742	NM_008858
RefSeq (protein)	NP_002733	NP_032884
Location (UCSC)	Chr 14: 29.58 – 30.19 Mb	Chr 12: 50.34 – 50.65 Mb
PubMed search

Serine/threonine-protein kinase D1 is an enzyme that in humans is encoded by the PRKD1 gene.^[1][2][3]

Function

Members of the protein kinase D (PKD) family function in many extracellular receptor-mediated signal transduction pathways. 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]^[3]

Interactions

Protein kinase D1 has been shown to interact with:

• Bruton's tyrosine kinase,^[4]
• C1QBP,^[5]
• Centaurin, alpha 1,^[6]
• Metallothionein 2A,^[7] and
• YWHAQ.^[5][8]

References

1. Johannes FJ, Prestle J, Eis S, Oberhagemann P, Pfizenmaier K (April 1994). "PKCu is a novel, atypical member of the protein kinase C family". J Biol Chem 269 (8): 6140–8. PMID 8119958.
2. Owczarek CM, Portbury KJ, Kola I, Hertzog PJ (September 2000). "Assignment of protein kinase C mu (PRKCM) to human chromosome band 14q11 with somatic cell hybrids and radiation hybrids". Cytogenet Cell Genet 89 (3–4): 240–1. doi:10.1159/000015624. PMID 10965134.
3. "Entrez Gene: PRKD1 protein kinase D1".
4. Johannes FJ, Hausser A, Storz P, Truckenmüller L, Link G, Kawakami T, Pfizenmaier K (November 1999). "Bruton's tyrosine kinase (Btk) associates with protein kinase C mu". FEBS Lett. 461 (1-2): 68–72. doi:10.1016/s0014-5793(99)01424-6. PMID 10561498.
5. Storz P, Hausser A, Link G, Dedio J, Ghebrehiwet B, Pfizenmaier K, Johannes FJ (August 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.
6. Zemlickova E, Dubois T, Kerai P, Clokie S, Cronshaw AD, Wakefield RI, Johannes FJ, Aitken A (August 2003). "Centaurin-alpha(1) associates with and is phosphorylated by isoforms of protein kinase C". Biochem. Biophys. Res. Commun. 307 (3): 459–65. doi:10.1016/s0006-291x(03)01187-2. PMID 12893243.
7. Rao PS, Jaggi M, Smith DJ, Hemstreet GP, Balaji KC (October 2003). "Metallothionein 2A interacts with the kinase domain of PKCmu in prostate cancer". Biochem. Biophys. Res. Commun. 310 (3): 1032–8. doi:10.1016/j.bbrc.2003.09.118. PMID 14550308.
8. Hausser A, Storz P, Link G, Stoll H, Liu YC, Altman A, Pfizenmaier K, Johannes FJ (April 1999). "Protein kinase C mu is negatively regulated by 14-3-3 signal transduction proteins". J. Biol. Chem. 274 (14): 9258–64. doi:10.1074/jbc.274.14.9258. PMID 10092600.

Further reading

• Van Lint J, Rykx A, Maeda Y, Vantus T, Sturany S, Malhotra V, Vandenheede JR, Seufferlein T (2002). "Protein kinase D: an intracellular traffic regulator on the move". Trends Cell Biol. 12 (4): 193–200. doi:10.1016/S0962-8924(02)02262-6. 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. PMC 551792. 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. doi:10.1073/pnas.82.7.1974. PMC 397463. 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. doi:10.1073/pnas.82.12.4080. PMC 397938. PMID 2987962.
• 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. PMC 189957. PMID 8627654.
• Sidorenko SP, Law CL, Klaus SJ, Chandran KA, Takata M, Kurosaki T, Clark EA (1996). "Protein kinase C mu (PKC mu) associates with the B cell antigen receptor complex and regulates lymphocyte signaling". Immunity 5 (4): 353–63. doi:10.1016/S1074-7613(00)80261-7. 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. doi:10.1006/bbrc.1997.7877. PMID 9446795.
• Zidovetzki R, Wang JL, Chen P, Jeyaseelan R, Hofman F (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. doi:10.1089/aid.1998.14.825. 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. doi:10.1074/jbc.274.14.9224. PMID 10092595.
• Hausser A, Storz P, Link G, Stoll H, Liu YC, Altman A, Pfizenmaier K, Johannes FJ (1999). "Protein kinase C mu is negatively regulated by 14-3-3 signal transduction proteins". J. Biol. Chem. 274 (14): 9258–64. doi:10.1074/jbc.274.14.9258. PMID 10092600.
• Jamora C, Yamanouye N, Van Lint J, Laudenslager J, Vandenheede JR, Faulkner DJ, Malhotra V (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. PMC 1171625. PMID 10523301.
• Johannes FJ, Hausser A, Storz P, Truckenmüller L, Link G, Kawakami T, Pfizenmaier K (1999). "Bruton's tyrosine kinase (Btk) associates with protein kinase C mu". FEBS Lett. 461 (1–2): 68–72. doi:10.1016/S0014-5793(99)01424-6. PMID 10561498.
• Storz P, Hausser A, Link G, Dedio J, Ghebrehiwet B, Pfizenmaier K, Johannes FJ (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. doi:10.4049/jimmunol.164.12.6538. 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. PMC 203351. PMID 10856238.
• Vertommen D, Rider M, Ni Y, Waelkens E, Merlevede W, Vandenheede JR, Van Lint J (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.