Biology:Protein kinase D1
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Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
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
- ↑ "PKCu is a novel, atypical member of the protein kinase C family". J Biol Chem 269 (8): 6140–8. April 1994. doi:10.1016/S0021-9258(17)37580-4. PMID 8119958.
- ↑ "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. September 2000. doi:10.1159/000015624. PMID 10965134.
- ↑ 3.0 3.1 "Entrez Gene: PRKD1 protein kinase D1". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5587.
- ↑ "Bruton's tyrosine kinase (Btk) associates with protein kinase C mu". FEBS Lett. 461 (1–2): 68–72. November 1999. doi:10.1016/s0014-5793(99)01424-6. PMID 10561498.
- ↑ 5.0 5.1 "Protein kinase C [micro] is regulated by the multifunctional chaperon protein p32". J. Biol. Chem. 275 (32): 24601–7. August 2000. doi:10.1074/jbc.M002964200. PMID 10831594.
- ↑ "Centaurin-alpha(1) associates with and is phosphorylated by isoforms of protein kinase C". Biochem. Biophys. Res. Commun. 307 (3): 459–65. August 2003. doi:10.1016/s0006-291x(03)01187-2. PMID 12893243.
- ↑ "Metallothionein 2A interacts with the kinase domain of PKCmu in prostate cancer". Biochem. Biophys. Res. Commun. 310 (3): 1032–8. October 2003. doi:10.1016/j.bbrc.2003.09.118. PMID 14550308.
- ↑ "Protein kinase C mu is negatively regulated by 14-3-3 signal transduction proteins". J. Biol. Chem. 274 (14): 9258–64. April 1999. doi:10.1074/jbc.274.14.9258. PMID 10092600.
Further reading
- "Protein kinase D: an intracellular traffic regulator on the move". Trends Cell Biol. 12 (4): 193–200. 2002. doi:10.1016/S0962-8924(02)02262-6. PMID 11978539.
- "[Old and new dangers of blood transfusion (author's transl)]". Münchener medizinische Wochenschrift 118 (22): 713–8. 1976. PMID 5668.
- "Trans-activation of HIV-1 LTR-directed gene expression by tat requires protein kinase C". EMBO J. 9 (4): 1165–70. 1990. doi:10.1002/j.1460-2075.1990.tb08223.x. PMID 2182321.
- "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. 1985. doi:10.1073/pnas.82.7.1974. PMID 2984676. Bibcode: 1985PNAS...82.1974D.
- "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. 1985. doi:10.1073/pnas.82.12.4080. PMID 2987962. Bibcode: 1985PNAS...82.4080D.
- "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. 1996. doi:10.1128/JVI.70.3.1384-1389.1996. PMID 8627654.
- "Protein kinase C mu (PKC mu) associates with the B cell antigen receptor complex and regulates lymphocyte signaling". Immunity 5 (4): 353–63. 1996. doi:10.1016/S1074-7613(00)80261-7. PMID 8885868.
- "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. 1996. doi:10.1006/abbi.1996.0476. PMID 8914829.
- "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. 1998. doi:10.1006/bbrc.1997.7877. PMID 9446795.
- "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. 1998. doi:10.1089/aid.1998.14.825. PMID 9671211.
- "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. 1999. doi:10.1074/jbc.274.14.9224. PMID 10092595.
- "Protein kinase C mu is negatively regulated by 14-3-3 signal transduction proteins". J. Biol. Chem. 274 (14): 9258–64. 1999. doi:10.1074/jbc.274.14.9258. PMID 10092600.
- "Gbetagamma-mediated regulation of Golgi organization is through the direct activation of protein kinase D". Cell 98 (1): 59–68. 1999. doi:10.1016/S0092-8674(00)80606-6. PMID 10412981.
- "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. 1999. doi:10.1093/emboj/18.20.5567. PMID 10523301.
- "Bruton's tyrosine kinase (Btk) associates with protein kinase C mu". FEBS Lett. 461 (1–2): 68–72. 1999. doi:10.1016/S0014-5793(99)01424-6. PMID 10561498.
- "Protein kinase C [micro] is regulated by the multifunctional chaperon protein p32". J. Biol. Chem. 275 (32): 24601–7. 2000. doi:10.1074/jbc.M002964200. PMID 10831594.
- "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. 2000. doi:10.4049/jimmunol.164.12.6538. PMID 10843712.
- "Spatial and temporal regulation of protein kinase D (PKD)". EMBO J. 19 (12): 2935–45. 2000. doi:10.1093/emboj/19.12.2935. PMID 10856238.
- "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. 2000. doi:10.1074/jbc.M001357200. PMID 10867018.
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