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A protein kinase is a kinase which selectively modifies other proteins by covalently adding phosphates to them (phosphorylation) as opposed to kinases which modify lipids, carbohydrates, or other molecules. Phosphorylation usually results in a functional change of the target protein (substrate) by changing enzyme activity, cellular location, or association with other proteins. The human genome contains about 500 protein kinase genes and they constitute about 2% of all human genes. There are two main types of protein kinase. The great majority are serine/threonine kinases, which phosphorylate the hydroxyl groups of serines and threonines in their targets. Most of the others are tyrosine kinases, although additional types exist. Protein kinases are also found in bacteria and plants. Up to 30% of all human proteins may be modified by kinase activity, and kinases are known to regulate the majority of cellular pathways, especially those involved in signal transduction.
In biochemistry, a kinase is an enzyme that catalyzes the transfer of phosphate groups from high-energy, phosphate-donating molecules to specific substrates. This process is known as phosphorylation, where the high-energy ATP molecule donates a phosphate group to the substrate molecule. As a result, kinase produces a phosphorylated substrate and ADP. Conversely, it is referred to as dephosphorylation when the phosphorylated substrate donates a phosphate group and ADP gains a phosphate group. These two processes, phosphorylation and dephosphorylation, occur four times during glycolysis.
Protein kinase B (PKB), also known as Akt, is the collective name of a set of three serine/threonine-specific protein kinases that play key roles in multiple cellular processes such as glucose metabolism, apoptosis, cell proliferation, transcription, and cell migration.
Bone morphogenetic protein 4 is a protein that in humans is encoded by BMP4 gene. BMP4 is found on chromosome 14q22-q23.
Bone morphogenetic protein receptor type II or BMPR2 is a serine/threonine receptor kinase encoded by the BMPR2 gene. It binds bone morphogenetic proteins, members of the TGF beta superfamily of ligands, which are involved in paracrine signaling. BMPs are involved in a host of cellular functions including osteogenesis, cell growth and cell differentiation. Signaling in the BMP pathway begins with the binding of a BMP to the type II receptor. This causes the recruitment of a BMP type I receptor, which the type II receptor phosphorylates. The type I receptor phosphorylates an R-SMAD, a transcriptional regulator.
The bone morphogenetic protein receptor, type IA also known as BMPR1A is a protein which in humans is encoded by the BMPR1A gene. BMPR1A has also been designated as CD292.
A serine/threonine protein kinase is a kinase enzyme, in particular a protein kinase, that phosphorylates the OH group of the amino-acid residues serine or threonine, which have similar side chains. At least 350 of the 500+ human protein kinases are serine/threonine kinases (STK).
In molecular biology, ribosomal s6 kinase (rsk) is a family of protein kinases involved in signal transduction. There are two subfamilies of rsk, p90rsk, also known as MAPK-activated protein kinase-1 (MAPKAP-K1), and p70rsk, also known as S6-H1 Kinase or simply S6 Kinase. There are three variants of p90rsk in humans, rsk 1-3. Rsks are serine/threonine kinases and are activated by the MAPK/ERK pathway. There are two known mammalian homologues of S6 Kinase: S6K1 and S6K2.
The PHLPP isoforms are a pair of protein phosphatases, PHLPP1 and PHLPP2, that are important regulators of Akt serine-threonine kinases and conventional/novel protein kinase C (PKC) isoforms. PHLPP may act as a tumor suppressor in several types of cancer due to its ability to block growth factor-induced signaling in cancer cells.
The enzyme phosphatidate phosphatase (PAP, EC 3.1.3.4) is a key regulatory enzyme in lipid metabolism, catalyzing the conversion of phosphatidate to diacylglycerol:
Protein phosphatase 1A is an enzyme that in humans is encoded by the PPM1A gene.
Lipid phosphate phosphohydrolase 1 also known as phosphatidic acid phosphatase 2a is an enzyme that in humans is encoded by the PPAP2A gene.
Serine/threonine-protein phosphatase 4 catalytic subunit is an enzyme that in humans is encoded by the PPP4C gene.
Protein phosphorylation is a reversible post-translational modification of proteins in which an amino acid residue is phosphorylated by a protein kinase by the addition of a covalently bound phosphate group. Phosphorylation alters the structural conformation of a protein, causing it to become activated, deactivated, or otherwise modifying its function. Approximately 13,000 human proteins have sites that are phosphorylated.
Lipid phosphate phosphohydrolase 3 (LPP3), also known as phospholipid phosphatase 3 (PLPP3) and phosphatidic acid phosphatase type 2B, is an enzyme that in humans is encoded by the PPAP2B gene on chromosome 1. It is ubiquitously expressed in many tissues and cell types. LPP3 is a cell-surface glycoprotein that hydrolyzes extracellular lysophosphatidic acid (LPA) and short-chain phosphatidic acid. Its function allows it to regulate vascular and embryonic development by inhibiting LPA signaling, which is associated with a wide range of human diseases, including cardiovascular disease and cancer, as well as developmental defects. The PPAP2B gene also contains one of 27 loci associated with increased risk of coronary artery disease.
The Akt signaling pathway or PI3K-Akt signaling pathway is a signal transduction pathway that promotes survival and growth in response to extracellular signals. Key proteins involved are PI3K and Akt.
Dishevelled (Dsh) is a family of proteins involved in canonical and non-canonical Wnt signalling pathways. Dsh is a cytoplasmic phosphoprotein that acts directly downstream of frizzled receptors. It takes its name from its initial discovery in flies, where a mutation in the dishevelled gene was observed to cause improper orientation of body and wing hairs. There are vertebrate homologs in zebrafish, Xenopus (Xdsh), mice and humans. Dsh relays complex Wnt signals in tissues and cells, in normal and abnormal contexts. It is thought to interact with the SPATS1 protein when regulating the Wnt Signalling pathway.
The Nodal signaling pathway is a signal transduction pathway important in regional and cellular differentiation during embryonic development.
In cell biology, CTDNEP1 is a protein coding gene involved in neural development. It is a member of DXDX(T/V) phosphatase family and is a potential regulator of neural tube development in Xenopus. The gene promotes neural development by inhibiting Bone Morphogenetic Proteins (BMPs). The encoded protein is relatively small and only contains 244 amino acids.
Ceramide-activated protein phosphatases (CAPPs) are a group of enzymes that are activated by the lipid second messenger ceramide. Known CAPPs include members of the protein phosphatase 1 (PP1) and protein phosphatase 2A (PP2A) families. CAPPs are a subset of intracellular serine/threonine phosphatases. Each CAPP consists of a catalytic subunit which confers phosphatase activity and a regulatory subunit which confers substrate specificity. CAPP involvement has been implicated in glycogen metabolism, apoptotic pathways related to cancer and other cellular pathways related to Alzheimer’s disease.
References
- 1 2 Kim, Y.; Gentry, M. S.; Harris, T. E.; Wiley, S. E.; Lawrence, J. C.; Dixon, J. E. (2007). "A conserved phosphatase cascade that regulates nuclear membrane biogenesis". Proceedings of the National Academy of Sciences. 104 (16): 6596–6601. Bibcode:2007PNAS..104.6596K. doi: 10.1073/pnas.0702099104 . PMC 1871831 . PMID 17420445.
- ↑ "CTDNEP1 Gene". genecards.org. Retrieved 2016-11-06.
- 1 2 Wu, Rui; Garland, Megan; Dunaway-Mariano, Debra; Allen, Karen N. (2011-04-19). "Homo sapiens Dullard Protein Phosphatase Shows a Preference for the Insulin-Dependent Phosphorylation Site of Lipin1". Biochemistry. 50 (15): 3045–3047. doi:10.1021/bi200336b. ISSN 0006-2960. PMC 3338355 . PMID 21413788.
- 1 2 Reiko, Satow; Te-chuan, Chan (2002). "Molecular cloning and characterization of dullard: a novel gene required for neural development". Biochemical and Biophysical Research Communications. 295 (1): 85–91. doi:10.1016/s0006-291x(02)00641-1. PMID 12083771.
- ↑ R. Harland (2000). "Neural induction". Curr. Opin. Genet. Dev. 10 (4): 357–362. doi:10.1016/s0959-437x(00)00096-4. PMID 10889069.
- ↑ Tanaka, Satomi S.; Nakane, Akihiro; Yamaguchi, Yasuka L.; Terabayashi, Takeshi; Abe, Takaya; Nakao, Kazuki; Asashima, Makoto; Steiner, Kirsten A.; Tam, Patrick P. L. (2013-03-04). "Dullard/Ctdnep1 Modulates WNT Signalling Activity for the Formation of Primordial Germ Cells in the Mouse Embryo". PLOS ONE. 8 (3): e57428. Bibcode:2013PLoSO...857428T. doi: 10.1371/journal.pone.0057428 . ISSN 1932-6203. PMC 3587611 . PMID 23469192.
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