Receptor serine/threonine kinase (RSTK) family | Catalytic receptors

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{ //window.open(ui.item.value); self.location.href = ui.item.value; return false; } }); </script> </div> </div> </div>  <div class="container_16">  <div class="breadcrumbscont"> <ul class="crumbtext"> <li><a href="/index.jsp">Home</a></li> <li><a href="/targets.jsp">Targets</a></li> <li><a href="FamilyDisplayForward?familyId=862">Catalytic receptors</a></li> <li><a href="FamilyDisplayForward?familyId=699">Receptor kinases</a></li> <li><a href="FamilyDisplayForward?familyId=687">TKL: Tyrosine kinase-like</a></li> <li>Receptor serine/threonine kinase (RSTK) family</li> </ul> </div>   <div class="grid_12">  <div class="grid_16 alpha"> <a name="top"></a> <div class="contentboxfull"> <h2 style="margin-top: 0px;">Receptor serine/threonine kinase (RSTK) family<span class='cgtp'> C</span></h2> <div class="textright"> </div> </div> </div>   <div class="grid_16 alpha list"> <h4>Contents</h4> <ul style="list-style:none;"> <li><a href="#overview">Overview</a></li> <li><a href="#subfamilies">Subfamilies</a></li> <li><a href="#comments">Comments</a></li> <li><a href="#reading">Further reading</a></li> <li><a href="#references">References</a></li> <li><a href="#citing">How to cite this family page</a></li> </ul> </div>   <div class="grid_16 alpha"> <a name="overview"></a> <h4>Overview</h4> <div class="contentboxfullhelp"> <div class="imageleft"> <a style="color:white;" href="JavaScript:callRef('helpPagePopup.jsp#overview', 800, 400)" title="Click here for help"><img style="vertical-align:baseline;" src="images/help_blue_small.png" alt="Click here for help"/></a> </div> <div class="textright"> <p class="split_para"> <a id="show_overview" style="display:none;" href="javascript:toggleLayerAndLink('overview_text', 'show_overview', 'hide_overview');"><small>Show</small> »</a><a id="hide_overview" href="javascript:toggleLayerAndLink('overview_text', 'show_overview', 'hide_overview');">« <small>Hide</small></a> </p> <div id="overview_text"> <p class="grac_text"> Receptor serine/threonine kinases (RSTK), <a href="http://www.genome.jp/kegg-bin/search_brite?option=-a&search_string=2.7.11.30">EC 2.7.11.30</a>, respond to particular cytokines, the transforming growth factor β (TGFβ) and bone morphogenetic protein (BMP) families, and may be divided into two subfamilies on the basis of structural similarities. Agonist binding initiates formation of a cell-surface complex of type I and type II RSTK, possibly heterotetrameric, where both subunits express serine/threonine kinase activity. The type I receptor serine/threonine kinases are also known as activin receptors or activin receptor-like kinases, ALKs, for which a systematic nomenclature has been proposed (ALK1-7). The type II protein phosphorylates the kinase domain of the type I partner (sometimes referred to as the signal propagating subunit), causing displacement of the protein partners, such as the FKBP12 FK506-binding protein <a href="https://www.genenames.org/data/gene-symbol-report/#!/hgnc_id/HGNC:3711"><i>FKBP1A</i></a> (<a href="http://www.uniprot.org/uniprot/P62942">P62942</a>) and allowing the binding and phosphorylation of particular members of the Smad family. These migrate to the nucleus and act as complexes to regulate gene transcription. Type III receptors, sometimes called co-receptors or accessory proteins, regulate the signalling of the receptor complex, in either enhancing (for example, presenting the ligand to the receptor) or inhibitory manners. TGFβ family ligand signalling may be inhibited by endogenous proteins, such as <a href="LigandDisplayForward?ligandId=4933">follistatin</a> (<a href="https://www.genenames.org/data/gene-symbol-report/#!/hgnc_id/HGNC:3971" target="_blank" title="HUGO Gene Nomenclature Committee (HGNC) database"><i>FST</i></a>, <a href="http://www.uniprot.org/uniprot/P19883" target="_blank" title="Universal Protein Resource catalog of information on proteins">P19883</a>), which binds and neutralizes activins to prevent activation of the target receptors.<br><br>Endogenous agonists, approximately 30 in man, are often described as paracrine messengers acting close to the source of production. They are characterized by six conserved cysteine residues and are divided into two subfamilies on the basis of sequence comparison and signalling pathways activated, the TGFβ/activin/nodal subfamily and the BMP/GDF (growth/differentiation factor)/MIS (Müllerian inhibiting substance) subfamily. Ligands active at RSTKs appear to be generated as large precursors which undergo complex maturation processes [<a href='javascript:callRef("ReferenceDisplayForward?referenceId=16946&displayId=2", 960, 600)' title="2. Li MO, Flavell RA. (2008) Cell. 134 (3): 392-404">2</a>]. Some are known to form disulphide-linked homo- and/or heterodimeric complexes. Thus, inhibins are α subunits linked to a variety of β chains, while activins are combinations of β subunits. </p> </div> </div> </div> </div>   <div class="grid_16 alpha"> <a name="subfamilies"></a> <h4>Subfamilies</h4> <div class="contentboxfullhelp"> <div class="textright"> <div style="text-align:right;"> <button class="button_gtoimmupdb_off" onClick='window.location.href="http://www.guidetoimmunopharmacology.org/GRAC/FamilyDisplayForward?familyId=303"; return false;'>GtoImmuPdb View OFF</button> </div> <table> <tr> <td width="400px"> <ul class="mktree" id ="family_tree"><li class="liOpen"><a id="link318" href="FamilyDisplayForward?familyId=318">Type I receptor serine/threonine kinases</a><span class="cgtp"> C</span></li><li class="liOpen"><a id="link319" href="FamilyDisplayForward?familyId=319">Type II receptor serine/threonine kinases</a><span class="cgtp"> C</span></li><li class="liOpen"><a id="link798" href="FamilyDisplayForward?familyId=798">Type III receptor serine/threonine kinases</a><span class="cgtp"> C</span></li><li class="liOpen"><a id="link797" href="FamilyDisplayForward?familyId=797">RSTK functional heteromers</a><span class="cgtp"> C</span></li> </td> <td width="400px" valign="top" text-align="right" style="padding:25px 0px 0px 25px"> <img id="myImg" src="images/approved_Ki_targets_kinome.jpg" alt="The Kinome image shown here was obtained from Chartier et al. (2013, <a href='https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3740139/figure/fig-4/' target='_blank'>Figure 4</a>) <a href='https://www.ncbi.nlm.nih.gov/pubmed/23940838' target='_blank'>https://www.ncbi.nlm.nih.gov/pubmed/23940838</a> and has been annotated to show the kinases that are targeted by currently approved kinase inhibitor drugs (last updated in April 2018)." width="377px" height="357px"> </td> </tr> </table> </div> </div> </div>   <div class="grid_16 alpha"> <a name="comments"></a> <h4>Comments</h4> <div class="contentboxfullhelp"> <div class="imageleft"> <a style="color:white;" href="JavaScript:callRef('helpPagePopup.jsp#comments', 800, 400)" title="Click here for help"><img style="vertical-align:baseline;" src="images/help_blue_small.png" alt="Click here for help"/></a> </div> <div class="textright"> <p> <a id="show_comments" style="display:none;" href="javascript:toggleLayerAndLink('comments_text', 'show_comments', 'hide_comments');"><small>Show</small> »</a><a id="hide_comments" href="javascript:toggleLayerAndLink('comments_text', 'show_comments', 'hide_comments');">« <small>Hide</small></a> </p> <div id="comments_text"> <p class="grac_text"> A number of endogenous inhibitory ligands have been identified for RSTKs, including <a href="LigandDisplayForward?ligandId=4882">BMP-3</a> (<a href="https://www.genenames.org/data/gene-symbol-report/#!/hgnc_id/HGNC:1070" target="_blank" title="HUGO Gene Nomenclature Committee (HGNC) database"><i>BMP3</i></a>, <a href="http://www.uniprot.org/uniprot/P12645" target="_blank" title="Universal Protein Resource catalog of information on proteins">P12645</a>), <a href="LigandDisplayForward?ligandId=5005">inhibin α</a> (<a href="https://www.genenames.org/data/gene-symbol-report/#!/hgnc_id/HGNC:6065" target="_blank" title="HUGO Gene Nomenclature Committee (HGNC) database"><i>INHA</i></a>, <a href="http://www.uniprot.org/uniprot/P05111" target="_blank" title="Universal Protein Resource catalog of information on proteins">P05111</a>), <a href="LigandDisplayForward?ligandId=5008">inhibin βC</a> (<a href="https://www.genenames.org/data/gene-symbol-report/#!/hgnc_id/HGNC:6068" target="_blank" title="HUGO Gene Nomenclature Committee (HGNC) database"><i>INHBC</i></a>, <a href="http://www.uniprot.org/uniprot/P55103" target="_blank" title="Universal Protein Resource catalog of information on proteins">P55103</a>) and <a href="LigandDisplayForward?ligandId=5009">inhibin βE</a> (<a href="https://www.genenames.org/data/gene-symbol-report/#!/hgnc_id/HGNC:24029" target="_blank" title="HUGO Gene Nomenclature Committee (HGNC) database"><i>INHBE</i></a>, <a href="http://www.uniprot.org/uniprot/P58166" target="_blank" title="Universal Protein Resource catalog of information on proteins">P58166</a>).<br><br> An appraisal of small molecule inhibitors of TGFβ and BMP signalling concluded that TGFβ pathway inhibitors were more selective than BMP signalling inhibitors [<a href='javascript:callRef("ReferenceDisplayForward?referenceId=17369&displayId=3", 960, 600)' title="3. Vogt J, Traynor R, Sapkota GP. (2011) Cell Signal. 23 (11): 1831-42">3</a>]. The authors confirmed the selectivity of <a href="LigandDisplayForward?ligandId=6049">TGF-beta RI inhibitor III</a> to inhibit TGFβ signalling through ALK4, ALK5, ALK7 [<a href='javascript:callRef("ReferenceDisplayForward?referenceId=17368&displayId=1", 960, 600)' title="1. DaCosta Byfield S, Major C, Laping NJ, Roberts AB. (2004) Mol Pharmacol. 65 (3): 744-52">1</a>]. <a href="LigandDisplayForward?ligandId=4907">Dorsomorphin</a> inhibits BMP signalling through ALK2 and ALK3, it also inhibits AMP kinase [<a href='javascript:callRef("ReferenceDisplayForward?referenceId=17367&displayId=4", 960, 600)' title="4. Zhou G, Myers R, Li Y, Chen Y, Shen X, Fenyk-Melody J, Wu M, Ventre J, Doebber T, Fujii N et al.. (2001) J Clin Invest. 108 (8): 1167-74">4</a>]. <br><br><b>Smads</b> were identified as mammalian orthologues of Drosophila genes termed “mothers against decapentaplegic” and may be divided into Receptor-regulated Smads (R-Smads, including Smad1, Smad2, Smad3, Smad5 and Smad8), Co-mediated Smad (Co-Smad, Smad4) and Inhibitory Smads (I-Smad, Smad6 and Smad7). R-Smads form heteromeric complexes with Co-Smad. I-Smads compete for binding of R-Smad with both receptors and Co-Smad.<br><br><table class="comment_table_no_border"><tr><td><b><u>Nomenclature</u></b></td><td><b><u>HGNC gene symbol</u></b></td><td><b><u>Uniprot ID</u></b></td><td><b><u>Other names</u></b></td></tr><tr><td>Smad1</td><td><a href="https://www.genenames.org/data/gene-symbol-report/#!/hgnc_id/HGNC:6767"><i>SMAD1</i></a></td><td><a href=" http://www.uniprot.org/uniprot/Q15797">Q15797</a></td><td>JV4-1, MADH1, MADR1</td></tr><tr><td>Smad2</td><td><a href="https://www.genenames.org/data/gene-symbol-report/#!/hgnc_id/HGNC:6768"><i>SMAD2</i></a></td><td><a href=" http://www.uniprot.org/uniprot/Q15796">Q15796</a></td><td>JV18-1, MADH2, MADR2</td></tr><tr><td>Smad3</td><td><a href="https://www.genenames.org/data/gene-symbol-report/#!/hgnc_id/HGNC:6769"><i>SMAD3</i></a></td><td><a href=" http://www.uniprot.org/uniprot/P84022">P84022</a></td><td>HsT17436, JV15-2, MADH3</td></tr><tr><td>Smad4</td><td><a href="https://www.genenames.org/data/gene-symbol-report/#!/hgnc_id/HGNC:6770"><i>SMAD4</i></a></td><td><a href=" http://www.uniprot.org/uniprot/Q13485">Q13485</a></td><td>DPC4, MADH4</td></tr><tr><td>Smad5</td><td><a href="https://www.genenames.org/data/gene-symbol-report/#!/hgnc_id/HGNC:6771"><i>SMAD5</i></a></td><td><a href=" http://www.uniprot.org/uniprot/Q99717">Q99717</a></td><td>Dwfc, JV5-1, MADH5</td></tr><tr><td>Smad6</td><td><a href="https://www.genenames.org/data/gene-symbol-report/#!/hgnc_id/HGNC:6772"><i>SMAD6</i></a></td><td><a href=" http://www.uniprot.org/uniprot/O43541">O43541</a></td><td>HsT17432, MADH6, MADH7</td></tr><tr><td>Smad7</td><td><a href="https://www.genenames.org/data/gene-symbol-report/#!/hgnc_id/HGNC:6773"><i>SMAD7</i></a></td><td><a href=" http://www.uniprot.org/uniprot/O15105">O15105</a></td><td>MADH7, MADH8</td></tr><tr><td>Smad8</td><td><a href="https://www.genenames.org/data/gene-symbol-report/#!/hgnc_id/HGNC:6774"><i>SMAD9</i></a></td><td><a href=" http://www.uniprot.org/uniprot/O15198">O15198</a></td><td>MADH6, MADH9</td></tr></table><br> </p> </div> </div> </div> </div>   <div class="grid_16 alpha"> <a name="reading"></a> <h4>Further reading</h4> <div class="contentboxfullhelp"> <div class="imageleft"> <a style="color:white;" href="JavaScript:callRef('helpPagePopup.jsp#furtherReading', 800, 400)" title="Click here for help"><img style="vertical-align:baseline;" src="images/help_blue_small.png" alt="Click here for help"/></a> </div> <div class="textright"> <p> <a id="show_fr" href="javascript:toggleLayerAndLink('fr', 'show_fr', 'hide_fr');"><small>Show</small> »</a><a id="hide_fr" style="display:none;" href="javascript:toggleLayerAndLink('fr', 'show_fr', 'hide_fr');">« <small>Hide</small></a> </p> <div id="fr" style="display: none;"> <p>* Key recommended reading is highlighted with an asterisk</p> <p class="grac_text"> Bragdon B, Moseychuk O, Saldanha S, King D, Julian J, Nohe A. (2011) Bone morphogenetic proteins: a critical review. <i>Cell Signal</i>, <b>23</b> (4): 609-20. [PMID:<a href="javascript:newWindow('http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=AbstractPlus&list_uids=20959140', 800, 500)">20959140</a>] </p> <p class="grac_text"> * Budi EH, Duan D, Derynck R. (2017) Transforming Growth Factor-β Receptors and Smads: Regulatory Complexity and Functional Versatility. <i>Trends Cell Biol</i>, <b>27</b> (9): 658-672. [PMID:<a href="javascript:newWindow('http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=AbstractPlus&list_uids=28552280', 800, 500)">28552280</a>] </p> <p class="grac_text"> * Chen W, Ten Dijke P. (2016) Immunoregulation by members of the TGFβ superfamily. <i>Nat Rev Immunol</i>, <b>16</b> (12): 723-740. [PMID:<a href="javascript:newWindow('http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=AbstractPlus&list_uids=27885276', 800, 500)">27885276</a>] </p> <p class="grac_text"> Clarke DC, Liu X. (2008) Decoding the quantitative nature of TGF-beta/Smad signaling. <i>Trends Cell Biol</i>, <b>18</b> (9): 430-42. [PMID:<a href="javascript:newWindow('http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=AbstractPlus&list_uids=18706811', 800, 500)">18706811</a>] </p> <p class="grac_text"> Ehrlich M, Horbelt D, Marom B, Knaus P, Henis YI. (2011) Homomeric and heteromeric complexes among TGF-β and BMP receptors and their roles in signaling. <i>Cell Signal</i>, <b>23</b> (9): 1424-32. [PMID:<a href="javascript:newWindow('http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=AbstractPlus&list_uids=21515362', 800, 500)">21515362</a>] </p> <p class="grac_text"> Gatza CE, Oh SY, Blobe GC. (2010) Roles for the type III TGF-beta receptor in human cancer. <i>Cell Signal</i>, <b>22</b> (8): 1163-74. [PMID:<a href="javascript:newWindow('http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=AbstractPlus&list_uids=20153821', 800, 500)">20153821</a>] </p> <p class="grac_text"> * Heger J, Schulz R, Euler G. (2016) Molecular switches under TGFβ signalling during progression from cardiac hypertrophy to heart failure. <i>Br J Pharmacol</i>, <b>173</b> (1): 3-14. [PMID:<a href="javascript:newWindow('http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=AbstractPlus&list_uids=26431212', 800, 500)">26431212</a>] </p> <p class="grac_text"> Hinck AP. (2012) Structural studies of the TGF-βs and their receptors - insights into evolution of the TGF-β superfamily. <i>FEBS Lett</i>, <b>586</b> (14): 1860-70. [PMID:<a href="javascript:newWindow('http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=AbstractPlus&list_uids=22651914', 800, 500)">22651914</a>] </p> <p class="grac_text"> Kang JS, Liu C, Derynck R. (2009) New regulatory mechanisms of TGF-beta receptor function. <i>Trends Cell Biol</i>, <b>19</b> (8): 385-94. 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DaCosta Byfield S, Major C, Laping NJ, Roberts AB. (2004) SB-505124 is a selective inhibitor of transforming growth factor-beta type I receptors ALK4, ALK5, and ALK7. <i>Mol Pharmacol</i>, <b>65</b> (3): 744-52. [PMID:<a href="javascript:newWindow('http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=AbstractPlus&list_uids=14978253', 800, 500)">14978253</a>] </p> <p class="grac_text"> 2. Li MO, Flavell RA. (2008) TGF-beta: a master of all T cell trades. <i>Cell</i>, <b>134</b> (3): 392-404. [PMID:<a href="javascript:newWindow('http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=AbstractPlus&list_uids=18692464', 800, 500)">18692464</a>] </p> <p class="grac_text"> 3. Vogt J, Traynor R, Sapkota GP. (2011) The specificities of small molecule inhibitors of the TGFß and BMP pathways. <i>Cell Signal</i>, <b>23</b> (11): 1831-42. 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IUPHAR/BPS Guide to PHARMACOLOGY, <a href="http://www.guidetopharmacology.org/GRAC/FamilyDisplayForward?familyId=303">http://www.guidetopharmacology.org/GRAC/FamilyDisplayForward?familyId=303</a>. </p>  <p style="font-style:italic;">Concise Guide to PHARMACOLOGY citation:</p> <p> Alexander SPH, Fabbro D, Kelly E, Mathie A, Peters JA, Veale EL, Armstrong JF, Faccenda E, Harding SD, Pawson AJ, Sharman JL, Southan C, Davies JA; CGTP Collaborators. 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Receptor serine/threonine kinase (RSTK) family | Catalytic receptors | IUPHAR/BPS Guide to PHARMACOLOGY