(1)
Project-team INRIA-UPMC-CNRS REO Laboratoire Jacques-Louis Lions, CNRS UMR 7598, Université Pierre et Marie Curie, Place Jussieu 4, Paris Cedex 05, France
Abstract
Dual-specificity kinases (DSK; or Ser/Thr/Tyr kinases) phosphorylate their substrates on serine, threonine, and/or tyrosine residues. Dual-specificity kinases intervene in the regulation of cell growth, differentiation, and apoptosis. Dual-specificity kinases include, at least, members of the superfamily of mitogen-activated protein kinases as well as those of the family of glycogen synthase kinases.
Dual-specificity kinases (DSK; or Ser/Thr/Tyr kinases) phosphorylate their substrates on serine, threonine, and/or tyrosine residues. Dual-specificity kinases intervene in the regulation of cell growth, differentiation, and apoptosis. Dual-specificity kinases include, at least, members of the superfamily of mitogen-activated protein kinases as well as those of the family of glycogen synthase kinases.
Certain dual-specificity kinases can target Tyr residues for their own activation (autophosphorylation), but not on their substrates, on which they act as protein Ser/Thr kinases. Therefore, DSKs can be kinases that phosphorylate substrates at Tyr and Thr residues or kinases that exhibit dual specificity only via autophosphorylation [536].
7.1 Mitogen-Activated Protein Kinase Kinase
Dual-specificity MAPK kinase corresponds to middle tier of mitogen-activated protein kinase module that also comprises upstream and downstream Ser/Thr kinases (Chap. 6).
7.2 Glycogen Synthase Kinase
Glycogen synthase kinase-3 (GSK3) is involved in the control of several regulatory proteins. It mainly phosphorylates serine and threonine residues of its substrates. It is one among several kinases that phosphorylate glycogen synthase, the rate-limiting enzyme of glycogen formation. Moreover, it targets transcription factor cJun to prevent DNA binding [623]. It also activates MgATP-dependent form of protein Ser/Thr phosphatase PP1.
In mammals, isozymes GSK3α and GSK3β are encoded by 2 distinct genes (Gsk3A and Gsk3B). Kinase GSK3 intervenes in protein synthesis, controls cellular response to damaged DNA, and participates in Wnt signaling.
Enzyme GSK3 can autophosphorylate Ser, Thr, and Tyr residues. Autophosphorylations at Ser and Thr residues induce inactivation, whereas Tyr autophosphorylation causes activation [624]. In particular, autophosphorylation of GSK3α (Tyr279) and GSK3β (Tyr216) activates GSK3 kinase.
Phosphorylation of GSK3α (Ser21) and GSK3β (Ser9) by several types of protein kinases occurs in response to signals that activate the cAMP, PI3K, or MAPK cascade to inhibit GSK3 enzyme. Furthermore, FAK2 and Fyn kinases can phosphorylate GSK3 at Tyr residues. Protein GSK3 is also inhibited by secreted Wnt glycoproteins (Vol. 3 – Chap. 10. Morphogen Receptors).
Phosphorylation by glycogen synthase kinase-3 usually requires a priming kinase, as efficient phosphorylation only occurs if another SerP or ThrP residue already exists in GSK3 substrate. The priming kinase phosphorylates a substrate that is afterward additionally phosphorylated by GSK3. Phosphorylation by GSK3 usually precludes the activity of target protein (e.g., glycogen synthase and nuclear factor of activated T cells).
Glycogen synthase kinase-3 is phosphorylated (inhibited) by PKB during insulin signaling. Protein kinase-B stimulates many signaling axes blocked by GSK3 protein. Protein kinase-C phosphorylates GSK3 upon stimulation by cytokines, such as interleukins IL3 and IL4 as well as granulocyte–macrophage colony-stimulating factor (CSF2) [625].
In addition, lithium that inhibits GSK3 is used to stabilize mood in bipolar disorder with alternating mania and depression. Lithium induces a delay in Per2 transcription and corrects circadian disturbances of bipolar disorder [626]. Kinase GSK3 thus intervenes in circadian rhythm.
7.3 Dual-Specificity Tyrosine Phosphorylation-Regulated Kinases
Dual-specificity Tyr (Y) phosphorylation-regulated kinases (DYRK1a–DYRK1b and DYRK2–DYRK4) are Ser/Thr kinases that autophosphorylate on Tyr residues. They possess a nuclear localization signal. They can shuttle between the nucleoplasm and cytoplasm. Inside the nucleus, they can localize to the splicing-factor compartment (nuclear speckles).
Among GSK3 substrates, ε subunit of eukaryotic protein-synthesis initiation factor eIF2bε is phosphorylated (inhibited) by GSK3. Priming kinases are isoforms DYRK1a and DYRK2 [627]. The DYRK isoforms also phosphorylate microtubule-associated protein Tau, or MAPT,1 (Thr212) for phosphorylation by GSK3 (Ser208). In addition, some members of the DYRK family are involved in gene expression, as they phosphorylate certain transcription factors.
Members of the DYRK family either abound in the testis or have a testis-restricted expression pattern.
7.3.1 DYRK1a
Ubiquitous DYRK1a is encoded by the Dyrk1A gene on human chromosome 21. It autophosphorylates (Tyr321) to prime its activation. It phosphorylates or interacts with many proteins, such as transcription factors (CREB1, FoxO1, Gli1, NFAT, and STAT3), chromatin-remodeling factor ARIP4, protein-synthesis initiation factor eIF2bε, splicing factors (cyclin-L2, SF2, and SF3b1), inhibitor of receptor Tyr kinase Sprouty homolog Spry2, proteins involved in synapse functioning (amphiphysin-1, dynamin-1, synaptojanin-1, α-synuclein, and huntingtin-interacting protein-1), 14-3-3 proteins, in addition to GSK3 and Tau [628, 629].
Phytanoyl CoAαhydroxylase-associated protein PAHxAP1 is a DYRK1a-interacting protein that can control the subcellular DYRK1a location. Two splice variants of DYRK1a are expressed at comparable level without functional differences [629].
7.3.2 DYRK1b
Isoform DYRK1b is strongly expressed in skeletal muscles and testis [630]. In muscles, it regulates MEF2-dependent transcription, as it phosphorylates class-2 histone deacetylases. It reinforces G0 arrest of myoblasts, as it phosphorylates cell cycle regulators cyclin-D1 and -D3 and CKI1b inhibitor. Splice variants include ubiquitous, predominant P69DYRK1b and P75DYRK1b, which is restricted to skeletal muscle, as well as catalytically inactive P65DYRK1b and P66DYRK1b.
Small RhoA GTPase activates transcription factor MyoD and elicits DYRK1b synthesis. Kinases MAP2K3 and MAP2K6 phosphorylate (activate) DYRK1b. Pterin-4 α-carbinolamine dehydratase/dimerization cofactor PCBD2 of HNF11α2 that stabilizes HNF1α and enhances its transcriptional activity is a DYRK1b-binding protein [630]. In addition, P38MAPKα and P38MAPKβ (but neither P38MAPKγ nor P38MAPKδ) inhibit DYRK1b enzyme.
7.3.3 DYRK2
Dual-specificity Tyrosine (Y)-phosphorylation-regulated kinase DYRK2 is able to autophosphorylate on Tyr residues. It also phosphorylates histones H2B and H3 as well as transcription factor P53 (Ser46) to induce apoptosis in response to DNA damage [631]. Two isoforms of DYRK2 exist.
7.3.4 DYRK3
Isoform DYRK3 is restricted to erythroid progenitor cells and testes. It inhibits nuclear factor of activated T cells. It attenuates erythropoiesis selectively during anemia [632].
7.3.5 DYRK4
Subtype DYRK4 is a testis-specific kinase that localizes in the cytoplasm [633]. It is dispensable for male fertility, as a functional redundancy exist among DYRK isoforms during spermiogenesis.
7.4 Cell Division Cycle-like Kinases
Cell division cycle (CDC)-like Kinase-1 (CLK1) has a catalytic domain similar to that of cyclin-dependent- and mitogen-activated protein kinases [634].3 It autophosphorylates on Ser, Thr, and Tyr residues. It phosphorylates substrates essentially on Ser residues.
In humans, ubiquitous isoforms (CLK1–CLK4) phosphorylate in the nucleus Ser–Arg-rich proteins involved in pre-mRNA processing such as the spliceosome. In humans, CLK1 to CLK3 isoforms have splice variant transcripts [634]. Both CLK1 and CLK2 activate PTPn1 protein Tyr phosphatase.
7.4.1 CLK1
Isoform CLK1 can interact with Ser–Arg-rich RNA-binding proteins, such as heterogeneous nuclear RNA ribonucleoprotein hnRNPG, RNA-binding protein RNPS1, alternative splicing factor, and splicing factors SFRS3 and SFRS4 [634]. Subtype CLK1 phosphorylates cyclophilins. It also activates PRP4 pre-mRNA processing factor PRPF4 of small nuclear ribonucleoprotein complexes of spliceosomes and targets histone H1.
7.4.2 CLK2
Isoform CLK2 phosphorylates scaffold attachment factor SAFb and alternative splicing factor. It also binds to splicing factor TRA2β1. Alternative splicing factor (ASF; a.k.a. splicing factor SF2) that is encoded by the SFRS1 gene participates not only in splicing reactions, but also in post-splicing activities, such as mRNA nuclear export and translation. It is phosphorylated by SFRS protein kinase-1 as well as CDC-like kinases CLK1 and CLK2, and, specifically, CLK3 subtype.
7.4.3 CLK3
This nuclear dual-specificity kinase regulates the intranuclear distribution of the Ser/Arg-rich (SR) family of splicing factors, as it phosphorylates SR proteins of the spliceosomal complex.
Two transcript variants encode different isoforms; the long (CLK3) and short isoform (CLK3152) that result from alternative splicing coexist in different tissue types. Isoform CLK3152, like CLK2139 splice variant, lacks the kinase domain [635].
7.4.4 CLK4
Human CLK4 interacts with an Ser–Arg-rich-like protein CLASP that is a post-transcriptional regulator of CLK1. The long isoform CLASP L induces the inclusion of an exon containing a premature termination codon in CLK1 messenger RNA [634].
7.5 Wee1 Kinase
Dual-specificity protein kinase Wee14 hampers entry into mitosis. The Wee1 family includes several members. Ubiquitous Wee1 is expressed in somatic cells, but Wee1b is synthesized only in embryonic cells.
7.6 Membrane-Associated Tyr/Thr Protein Kinase
Membrane-associated dual-specificity protein Tyr/Thr kinase-1 (PKMYT1) that is encoded by the Pkmyt1 gene is also a member of the protein Ser/Thr kinase class.5 Enzyme PKMYT1 is a member of the Wee kinase family. It is produced in both somatic and embryonic cells. Alternatively spliced transcript variants encode distinct isoforms.
Kinase PKMYT1 preferentially phosphorylates (inactivates) CDK1, hence impeding the G2–M transition during the cell division cycle. It causes an inhibitory phosphorylation of cyclin–CDK complexes by targeting adjacent Thr14 and Tyr15 (hence its name PKMYT) located near the ATP-binding pocket of the CDK subunit [636]. However, PKMYT1 shows preferential Thr14 phosphorylation. This kinase is anchored to the membrane throughout the cell cycle [636].
Activity of PKMYT1 is regulated through the cell cycle, at least partly, via phosphorylation. During mitosis, PKMYT1 activity decays 2-fold to 5-fold [636]. Hyperphosphorylated PKMYT1 loses its ability to bind to cyclin-B1. Protein kinase-B, Polo-like kinase, P90 ribosomal S6-kinase RSK, Raf of the MAPK module, and cyclin-B–CDK complex phosphorylate PKMYT1, in addition to PKMYT1 autophosphorylation.
The primary PKMYT1 partner is the cyclin–CDK1 complex that serves both as a substrate of PKMYT1 and kinase for PKMYT1. Yet, the cyclin-B–CDK complex is not the main repressor of PKMYT1 during M phase.
7.7 Raf Kinase Inhibitory Protein
Raf kinase inhibitory protein (RKIP)6 is a member of the phosphatidyl ethanolamine binder (PEBP) family. Protein RKIP was characterized as a phospholipid-binding protein. However, it is also able to bind nucleotides and opioids [637].
Protein RKIP can inhibit serine peptidases (e.g., thrombin, neuropsin, and chymotrypsin). It promotes differentiation of keratinocytes, dendritic cells, and macrophages. It modulates signaling cascades by impeding the MAPK, GRK, and NFκB pathways. Protein RKIP indeed acts as a sensor and integrator of several pathways. In its non-phosphorylated form, it downregulates the MAPK cascade, but potentiates GPCR signaling. In its phosphorylated state, RKIP P dissociates from cRaf and inhibits GRK2, an inhibitor of G-protein-coupled receptors.
In humans, the RKIP family includes RKIP1 and PEBP4 [638]. Protein RKIP can be the precursor of hippocampal cholinergic neurostimulatory peptide (HCNP) that participates in acetylcholine synthesis and secretion in the brain. Endocrine factors PEBP and HCNP are secreted with catecholamines into the blood circulation. In heart, HCNP has a negative inotropic effect [639].
Activated RKIP interacts with cRaf kinase [640], but RKIP does not directly inhibit cRaf. Protein RKIP blocks activation of cRaf in cells by preventing access to kinases and phosphorylation [637]. Furthermore, RKIP binds to locostatin and is then unable to inhibit cRaf, hindering cell migration. In tumors, RKIP is thus able to hinder angiogenesis and vascular invasion. In addition, RKIP phosphorylation by protein kinase-C prevents RKIP interaction with cRaf.
Raf kinase inhibitor protein impedes the interaction between cRaf or bRaf and MAP2K. In particular, it disrupts the cRaf–ERK1/2 pathways. However, RKIP operates as a modulator rather than an off switch for MAPK signaling, as RKIP decreases signaling output amplitude in response to stimuli. RKIP may indirectly affect bRaf signaling via the cRaf–bRaf dimer. Nevertheless, RKIP can regulate bRaf independently of cRaf kinase.
Stimulated G-protein-coupled receptor dissociates RKIP from cRaf kinase. RKIP phosphorylation by protein kinase-C enhances its ability to bind G-protein-coupled receptor kinase-2. Protein RKIP phosphorylated (activated) by PKC then inhibits G-protein-coupled receptor kinase-2 that phosphorylates and impedes the activity of many G protein-coupled receptors. Protein Ser/Thr kinase GRK2 indeed downregulates various G-protein-coupled receptors, particularly those hampering cell locomotion.
Activated Raf kinase inhibitor disturbs the nuclear factor-κB pathways, as it interacts with associated kinases. Agent RKIP in fact binds to several proteins that activate NFκB, such as transforming growth factor-β-activated kinase-1, IκB kinase IKKα and IKKβ, and NFκB-inducing kinase (MAP3K14). After degradation of IκB, NFκB translocates to the nucleus and can then bind to target gene promoters.
Phosphorylated RKIP localizes to centrosomes and kinetochores during the cell division cycle [637]. It participates in the regulation of the cell spindle checkpoint. It promotes the activity of Aurora-B kinase that ensures proper chromosome segregation during anaphase. However, Aurora-B contributes to a negative feedback loop by phosphorylating RKIP that then dissociates from cRaf and relieves its inhibition on MAPK enzyme.
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