Protein kinase D1

Serine/threonine-protein kinase D1 is an enzyme that in humans is encoded by the PRKD1 gene.^[5][6][7]

PRKD1
Identifiers
Aliases	PRKD1, PKC-MU, PKCM, PKD, PRKCM, Protein kinase D1, CHDED
External IDs	OMIM: 605435; MGI: 99879; HomoloGene: 55680; GeneCards: PRKD1; OMA:PRKD1 - orthologs
Gene location (Human) Chr. Chromosome 14 (human)[1] Band 14q12 Start 29,576,479 bp[1] End 30,191,898 bp[1]
Gene location (Mouse) Chr. Chromosome 12 (mouse)[2] Band 12|12 B3 Start 50,341,231 bp[2] End 50,649,098 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in ventricular zone seminal vesicula thoracic aorta ascending aorta testicle saphenous vein Descending thoracic aorta right coronary artery popliteal artery tibial arteries Top expressed in primitive streak substantia nigra external carotid artery internal carotid artery fossa primary oocyte condyle renal corpuscle epithelium of lens vas deferens More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transferase activity nucleotide binding protein kinase activity protein kinase C activity metal ion binding kinase activity protein binding identical protein binding ATP binding protein serine/threonine kinase activity Cellular component Golgi apparatus membrane plasma membrane integral component of plasma membrane autophagosome membrane cytoplasm trans-Golgi network cytosol Biological process negative regulation of endocytosis cell differentiation intracellular signal transduction positive regulation of endothelial cell proliferation regulation of protein stability Golgi organization phosphorylation immune system process positive regulation of endothelial cell chemotaxis protein kinase D signaling sphingolipid biosynthetic process negative regulation of cell death nervous system development positive regulation of peptidyl-serine phosphorylation positive regulation of angiogenesis positive regulation of endothelial cell migration protein phosphorylation positive regulation of histone deacetylase activity positive regulation of CREB transcription factor activity vascular endothelial growth factor receptor signaling pathway regulation of integrin-mediated signaling pathway positive regulation of NF-kappaB transcription factor activity angiogenesis positive regulation of blood vessel endothelial cell migration positive regulation of neuron projection development 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 integrin-mediated signaling pathway protein autophosphorylation cellular response to oxidative stress cellular response to vascular endothelial growth factor stimulus Ras protein signal transduction cell population proliferation inflammatory response innate immune response signal transduction positive regulation of transcription by RNA polymerase II apoptotic process positive regulation of autophagy cellular response to amino acid starvation positive regulation of phosphatidylinositol 3-kinase activity cellular response to hydroperoxide regulation of keratinocyte proliferation positive regulation of osteoblast differentiation Golgi vesicle transport peptidyl-serine phosphorylation peptidyl-threonine phosphorylation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 5587 18760 Ensembl ENSG00000184304 ENSMUSG00000002688 UniProt Q15139 Q62101 RefSeq (mRNA) NM_002742 NM_001330069 NM_001348390 NM_008858 RefSeq (protein) NP_001316998 NP_002733 NP_001335319 NP_032884 NP_001369743 NP_001369744 NP_001369745 Location (UCSC) Chr 14: 29.58 – 30.19 Mb Chr 12: 50.34 – 50.65 Mb PubMed search [3] [4]
Wikidata
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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]^[7]

Interactions

Protein kinase D1 has been shown to interact with:

• Bruton's tyrosine kinase,^[8]
• C1QBP,^[9]
• Centaurin, alpha 1,^[10]
• Metallothionein 2A,^[11] and
• YWHAQ.^[9][12]

References

1. GRCh38: Ensembl release 89: ENSG00000184304 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000002688 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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. doi:10.1016/S0021-9258(17)37580-4. PMID 8119958.
6. 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. S2CID 26620985.
7. "Entrez Gene: PRKD1 protein kinase D1".
8. 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.
9. 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.
10. 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.
11. 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.
12. 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)]". 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. doi:10.1002/j.1460-2075.1990.tb08223.x. 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. Bibcode:1985PNAS...82.1974D. 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. Bibcode:1985PNAS...82.4080D. 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. doi:10.1128/JVI.70.3.1384-1389.1996. 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.