Serine/threonine kinase receptors and ligands

Current Opinion in Genetics and Development

Volumn 7, Issue 3, 1997, Pages 371-377

  Josso, Nathalie ^a   Di Clemente, Nathalie ^a  

^a ECOLE NORMALE SUPÉRIEURE   (France)

Author keywords

[No Author keywords available]

Indexed keywords

BONE MORPHOGENETIC PROTEIN; CYTOKINE RECEPTOR; GLIAL CELL LINE DERIVED NEUROTROPHIC FACTOR; HORMONE RECEPTOR; IMMUNOPHILIN; LIGAND; PROTEIN SERINE THREONINE KINASE; TRANSFORMING GROWTH FACTOR BETA;

EMBRYO PATTERN FORMATION; GENE TARGETING; HUMAN; MUELLERIAN DUCT; NONHUMAN; PRIORITY JOURNAL; PROTEIN FAMILY; REVIEW; SIGNAL TRANSDUCTION;

EID: 0030749294     PISSN: 0959437X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-437X(97)80151-7     Document Type: Article

References (68)

1. Wrana JL, Attisano L, Wieser R, Ventura F, Massagué J: Mechanism of activation of the TGF-β receptor. Nature 1994, 370:341-347.
2. Yamashita H, Ten Dijke P, Heldin CH, Miyazono K: Bone morphogenetic protein receptors. Bone 1996, 19:569-574.
3. Weis-Garcia F, Massagué J: Complementation between kinase-defective and activation-defective TGF-β receptors reveals a novel form of receptor cooperativity essential for signaling. EMBO J 1996, 15:276-289. A new class of TβR-I mutants, which contain a functional kinase but have lost susceptibility to phosphorylation by TGF-β can be rescued by kinase-defective mutants, proving that at least two molecules of TβR-I are present in trie receptor complex.
4. Luo KX, Lodish HF: Signaling by chimeric erythropoietin-TGF-beta receptors: homodimerization of the cytoplasmic domain of the type I TGF-beta receptor and heterodimerization with the type II receptor are both required for intracellular signal transduction. EMBO J 1996, 15:4485-4496.
5. Ten Dijke P, Miyazono K, Heldin CH: Signaling via hetero-oligomeric complexes of type I and type II serine/threonine kinase receptors. Curr Opin Cell Biol 1996, 8:139-145. An excellent review of 1994 and 1995 literature by major players in the field.
6. Franzén P, Heldin CH, Miyazono K: The GS domain of the transforming growth factor-beta type I receptor is important in signal transduction. Biochem Biophys Res Commun 1995, 207:682-689.
7. Càrcamo J, Zentella A, Massagué J: Disruption of transforming growth factor-β signaling by a mutation that prevents transphosphorylation within the receptor complex. Mol Cell Biol 1995, 15:1573-1581.
8. Wieser R, Wrana JL, Massagué J: GS domain mutations that constitutively activate TβR-I, the downstream signaling component in the TGF-β receptor complex. EMBO J 1995, 14:2199-2208.
9. Brand T, Schneider MD: Transforming growth factor-beta signal transduction. Circ Res 1996, 78:173-179. A review focused upon signal transduction in cardiac myocyte and describing receptor mutations in detail.
10. Willis SA, Zimmerman CM, Li L, Mathews LS: Formation and activation by phosphorylation of activin receptor complexes. Mol Endocrinol 1996, 10:367-379. Introduction of an activin type I receptor into a TGF-β responsive cell line confers activin responsiveness on those cells. A constitutively active activin type I receptor is obtained by mutation of threonine 206 to serine, the signalling activity of this mutant is not affected by overexpression of a dominant negative type II receptor.
11. Attisano L, Wrana JL, Montalvo E, Massagué J: Activation of signalling by the activin receptor complex. Mol Cell Biol 1996, 16:1066-1073. See annotation [10•].
12. De Winter JP, De Vries CJM, Van Achterberg TAE, Ameerun RF, Feijen A, Sugino H, De Waele P, Huylebroeck D, Verschueren K, Van den Eijnden-van Raaij AJM: Truncated activin type II receptors inhibit activin bioactivity by the formation of heteromeric complexes with activin type I receptors. Exp Cell Res 1996, 224:323-334.
13. Massagué J, Weis-Garcia F: Serine/threonine kinase receptors: mediators of transforming growth factor beta family signals. In Cancer Surveys, vol 27. Cell Signalling. London: Imperial Cancer Research Fund; 1996:41-64. An excellent update by a leading group, focused upon the respective function of type I and type II receptors and suggesting a new nomenclature.
14. Vivien D, Wrana JL: Ligand-induced recruitment and phosphorylation of reduced TGF-beta type I receptor. Exp Cell Res 1995, 221:60-65.
15. Ten Dijke P, Yamashita H, Ichijo H, Franzen P, Laiho M, Miyazono K, Heldin CH: Characterization of type-I receptors for transforming growth factor-β and activin. Science 1994, 264:101-104.
16. Imbeaud S, Faure E, Lamarre I, Mattei MG, Di Clemente N, Tizard R, Carré-Eusèbe D, Belville C, Tragethon L, Tonkin C et al.: Insensitivity to anti-Müllerian hormone due to a spontaneous mutation in the human anti-Müllerian hormone receptor. Nat Genet 1995, 11:382-388. Cloning of the human type II receptor for AMH and demonstration of a splicing mutation in a clinically affected patient.
17. Johnson DW, Berg JN, Baldwin MA, Gallione CJ, Marondel I, Yoon SJ, Stenzel TT, Speer M, Pericakvance MA, Diamond A et al.: Mutations in the activin receptor-like kinase 1 gene in hereditary haemorrhagic telangiectasia type 2: Nat Genet 1996, 13:189-195. A mutation in a human type I receptor expressed predominantly in the endo-thelium leads to Osler-Rendu-Weber disease.
18. Lustig KD, Kroll K, Sun E, Ramos R, Elmendorf H, Kirschner MW: A Xenopus nodal-related gene that acts in synergy with NOGGIN to induce complete secondary axis and notochord formation. Development 1996, 122:3275-3282.
19. Jones CM, Dale L, Hogan BLM, Wright CVE, Smith JC: Bone morphogenetic protein-4 (BMP-4) acts during gastrula stages to cause ventralization of Xenopus embryos. Development 1996, 122:1545-1554.
20. Hawley SHB, Wunnenberg-Stapleton K, Hashimoto C, Laurent MN, Watabe T, Blumberg BW, Cho KWY: Disruption of BMP signals in embryonic Xenopus ectoderm leads to direct neural induction. Genes Dev 1995, 9:2923-2935. Direct neural induction in Xenopus obtained by blocking processing of BMP molecules by mutating cleavage sites. The phenotype is similar to the one previously obtained by ectopic expression of a truncated BMP receptor.
21. Green JBA: Roads to neuralness-embryonic neural induction as derepression of a default state. Cell 1994, 77:317-320.
22. Hemmati-Brivanlou A, Melton D: Vertebrate embryonic cells will become nerve cells unless told otherwise. Cell 1997, 88:13-17. A reappraisal of the theory of active neural induction by the Spemann organizer.
23. Zimmerman LB, De Jesús-Escobar JM, Harland RM: The Spemann organizer signal NOGGIN binds and inactivates bone morphogenetic protein 4. Cell 1996, 86:599-606.
24. Piccolo S, Sasai Y, Lu B, De Robertis EM: Dorsoventral patterning in Xenopus: inhibition of ventral signals by direct binding of chordin to BMP-4. Cell 1996, 86:589-598.
25. Holley SA, Neul JL, Attisano L, Wrana JL, Sasai Y, O'Connor MB, De Robertis EM, Ferguson EL: The Xenopus dorsalizing factor NOGGIN ventralizes Drosophila embryos by preventing DPP from activating its receptor. Cell 1996, 86:607-617. NOGGIN, a product of the Xenopus Spemann organizer, ventralizes the Drosophila embryo by blocking the opposite effects of Dpp upstream of the Dpp receptor. In keeping with this hypothesis, the dorsalizing activity of constitutively active forms of the Dpp receptor is not affected by NOGGIN. This paper also provides support for the conservation of dorso-ventral patterning mechanisms between arthropods and vertebrates, in spite of the apparent inversion of the expression patterns of early dorso-ventral patterning genes. Similar conclusions are reached in [23,24].
26. Renucci A, Lemarchandel V, Rosa F: An activated type of serine/threonine kinase receptor TARAM-A reveals a specific signalling pathway involved in fish head organiser formation. Development 1996, 122:3735-3743.
27. Mishina Y, Suzuki A, Ueno N, Behringer RR: Bmpr encodes a type I bone morphogenetic protein receptor that is essential for gastrulation during mouse embryogenesis. Genes Dev 1995, 9:3027-3037.
28. Collignon J, Varlet I, Robertson E: Relationship between asymmetric nodal expression and the direction of embryonic turning. Nature 1996, 381:155-158. Nodal is a member of the TGF-β family expressed asymmetrically during early mouse organogenesis and which could be involved, with two other genes, in the specification of the left→right axis.
29. Carré-Eusèbe D, Di Clemente N, Rey R, Pieau C, Vigier B, Josso N, Picard JY: Cloning and expression of the chick anti-Müllerian hormone gene. J Biol Chem 1996, 271:4798-4804.
30. Neeper M, Lowe R, Galuska S, Hoffmann KJ, Smith RG, Elbrecht A: Molecular cloning of an avian anti-Müllerian hormone homologue. Gene 1996, 176:203-209.
31. Nachtigal MW, Ingraham HA: Bioactivation of Müllerian inhibiting substance during gonadal development by a kex2/subtilisin-like endoprotease. Proc Natl Acad Sci USA 1996, 93:7711-7716. PC5, an endoprotease capable of processing AMH/MIS, is expressed in fetal testis and could be involved in the physiological activation of the hormone.
32. Faure E, Gouédard L, Imbeaud S, Cate RL, Picard JY, Josso N, Di Clemente N: Mutant isoforms of the anti-Müllerian hormone type II receptor are not expressed at the cell membrane. J Biol Chem 1996, 271:30571-30575. Proof that the mutant isoforms of the AMH type II receptor produced by the splicing mutation described in [16•] are retained intracellularly, explaining their lack of bioactivity.
33. Imbeaud S, Belville C, Messika-Zeitoun L, Rey R, Di Clemente N, Josso N, Picard JY: A 27 base-pair deletion of the anti-Müllerian type II receptor gene is the most common cause of the persistent Müllerian duct syndrome. Hum Mol Genet 1996, 5:1269-1279.
34. Mishina Y, Rey R, Finegold MJ, Matzuk MM, Josso N, Cate RL, Behringer RR: Genetic analysis of the Müllerian-inhibiting substance signal transduction pathway. Genes Dev 1996, 10:2577-2587. The phenotype of AMH/MIS ligand/AMH/MIS receptor double ligand mutant males is identical, providing additional in vivo evidence that AMH/MIS is the only ligand of the AMH/MIS type II receptor, in contrast to the complexity of the activin signalling pathway.
35. Behringer RR, Finegold MJ, Cate RL: Müllerian-inhibiting substance function during mammalian sexual development Cell 1994, 79:415-425.
36. Coerver KA, Woodruff TK, Finegold MJ, Mather J, Bradley A, Matzuk MM: Activin signaling through activin receptor type II causes the cachexia-like symptoms in inhibin-deficient mice. Mol Endocrinol 1996, 10:534-543.
37. Matzuk MM, Finegold MJ, Mishina Y, Bradley A, Behringer RR: Synergistic effects of inhibins and Mullerian-inhibiting substance on testicular tumorigenesis. Mol Endocrinol 1995, 9:1337-1345.
38. Kumar TR, Wang Y, Matzuk MM: Gonadotropins are essential modifier factors for gonadal tumor development in inhibin-deficient mice. Endocrinology 1996, 137:4210-4216.
39. Dong J, Albertini DF, Nishimori K, Kumar TR, Lu N, Matzuk MM: Growth differentiation factor-9 is required during early ovarian folliculogenesis. Nature 1996, 383:531-535. GDF-9 mRNA is synthesized only in the oocyte, nevertheless, inactivation of the gene in mice impairs folliculogenesis beyond the primary follicle stage.
40. Pichel JG, Shen L, Sheng HZ, Granholm AC, Drago J, Grinberg A, Lee EJ, Huang SP, Saarma M, Hoffer BJ et al.: Defects in enteric innervation and kidney development in mice lacking GDNF. Nature 1996, 382:73-76.
41. Sanchez MP, Silos-Santiago I, Frisen J, He B, Lira SA, Barbacid M: Renal agenesis and the absence of enteric neurons in mice lacking GDNF. Nature 1996, 382:70-73.
42. Moore MW, Klein RD, Farinas I, Sauer H, Armanini M, Phillips H, Reichardt LF, Ryan AM, Carver-Moore K, Rosenthal A: Renal and neuronal abnormalities in mice lacking GDNF. Nature 1996, 382:76-79.
43. Schuchardt A, D'Agati V, Larsson-Blomberg L, Costantini F, Pachnis V: Defects in the kidney and enteric nervous system of mice lacking the tyrosine kinase receptor ret Nature 1994, 367:380-383.
44. Ivanchuk SM, Myers SM, Eng C, Mulligan LM: De novo mutation of GDNF, ligand for the RET/GDNFR-alpha receptor complex, in Hirschsprung disease. Hum Mol Genet 1996, 5:2023-2026.
45. Trupp M, Arenas E, Fainzilber M, Nilsson AS, Sieber BA, Grigoriou M, Kilkenny C, Salazar-Grueso E, Pachnis V, Arumae U et al.: Functional receptor for GDNF encoded by the c-ret proto-oncogene. Nature 1996, 381:785-789. GDNF binds to and induces the phosphorylation of the c-ret proto-oncogene, an orphan receptor tyrosine kinase, in a GDNF-responsive cell line, indicating that ret is a signal-transducing receptor for GDNF.
46. Durbec P, Marcos-Gutierrez CV, Kilkenny C, Grigoriou M, Wartiowaara K, Suvanto P, Smith D, Ponder B, Costantini F, Saarma M et al.: GDNF signalling through the Ret receptor tyrosine kinase. Nature 1996, 381:789-793. Same conclusions as for [45•] but reached by a different method: co-expression of GDNF and Ret in Xenopus animal caps leads to mesoderm formation. Treatment by GDNF of Xenopus oocytes expressing Ret leads to Ret-specific tyrosine phosphorylation. As other members of the TGF-β family signal through serine/kinase receptors, this finding emphasizes the distant relationship of GDNF to other members of the family.
47. Jing SQ, Wen DZ, Yu YB, Holst PL, Luo Y, Fang M, Tamir R, Antonio L, Hu Z, Cupples R et al.: GDNF-induced activation of the Ret protein tyrosine kinase is mediated by GDNFR-alpha, a novel receptor for GDNF. Cell 1996, 85:1113-1124. Binding of GDNF to GDNFR-α activates phosphorylation of the protein tyrosine kinase RET, even if GDNFR-α is released from the plasma membrane.
48. Treanor JJS, Goodman L, De Sauvage F, Stone DM, Poulsen KT, Beck CD, Gray C, Armanini MP, Pollock RA, Hefti F et al.: Characterization of a multicomponent receptor for GDNF. Nature 1996, 382:80-83.
49. Chen RH, Miettinen RJ, Maruoka EM, Choy L, Derynck R: A WD domain protein that is associated with and phosphorylated by the type II TGF-β receptor. Nature 1995, 377:548-552.
50. RAS farnesyltransferase alpha unit in TGF-beta and activin signaling. Science 1996, 271:1120-1122.
51. Wang TW, Li BY, Danielson PD, Shah PC, Rockwell S, Lechleider RJ, Martin J, Manganaro T, Donahoe PK: The immunophilin FKBP12 functions as a common inhibitor of the TGF beta family type I receptors. Cell 1996, 86:435-444. Binding of the immunophilin FKBP12 to ligand-free TβR-I is released by ligand-induced phosphorylation of TβR-I by TβR-II. Non-functional derivatives of FKBP12 block the interaction of FKBP12 with TβR-I and enhance ligand activity.
52. Hoodless PA, Haerry T, Abdollah S, Stapleton M, O'Connor MB, Attisano L, Wrana JL: MADR1, a MAD-related protein that functions in BMP2 signaling pathways. Cell 1996, 85:489-500. Cloning of a human equivalent of Drosophila MAD, MADR1, which is phosphorylated by BMP2, but not TGF-β or activin. BMP2-dependent phosphorylation of MADR1 is abolished by the introduction of a Gly419Ser mutation which produces a null phenotype in MAD.
53. Savage C, Das P, Finelli AL, Townsend SR, Sun CY, Baird SE, Padgett RW: Caenorhabditis elegans genes sma2, sma-3, and sma-4 define a conserved family of transforming growth factor beta pathway components. Proc Natl Acad Sci USA 1996, 93:790-794.
54. Graff JM, Bansal A, Melton DA: Xenopus Mad proteins transduce distinct subsets of signals for the TGF beta superfamily. Cell 1996, 85:479-487.
55. Baker JC, Harland RM: A novel mesoderm inducer, Madr2 functions in the activin signal transduction pathway. Genes Dev 1996, 10:1880-1889.
56. Liu F, Hata A, Baker JC, Doody J, Carcamo J, Harland RM, Massagué J: A human Mad protein acting as a BMP-regulated transcriptional activator. Nature 1996, 381:620-623. Smad1, a human homologue of MAD, moves into the nucleus in response to BMP4 and has transcriptional activity when fused to a heterologous DNA-binding domain, this activity is enhanced by BMP4.
57. Zhang Y, Feng XH, Wu RY, Derynck R: Receptor-associated Mad homologues synergize as effectors of the TGF-beta response. Nature 1996, 383:168-172.
58. Eppert K, Scherer SW, Ozcelik H, Pirone R, Hoodless P, Kim H, Tsui LC, Bapat B, Gallinger S, Andrulis IL et al.: MADR2 maps to 18q21 and encodes a TGF beta-regulated MAD-related protein that is functionally mutated in colorectal carcinoma. Cell 1996, 86:543-552. Cloning of MADR2, a human equivalent of the Drosophila MAD, is specifically phosphorylated by TGF-β and not by BMPs. Three somatically acquired missense mutations of MADR2 have been detected in random screens of colorectal cancer patients. Expression of these mutations in epithelial cells and Xenopus embryos show that these mutations are inactivating.
59. Riggins GJ, Thiagalingam S, Rozenblum E, Weinstein CL, Kern SE, Hamilton SR, Willson JKV, Markowitz SD, Kinzler KW, Vogelstein B: Mad-related genes in the human. Nat Genet 1996, 13:347-349.
60. Hahn SA, Schutte M, Hoque ATMS, Moskaluk CA, Da Costa LT, Rozenblum E, Weinstein CL, Fischer A, Yeo CJ, Hruban RH, Kern SE: DPC4, a candidate tumor suppressor gene at human chromosome 18q21.1. Science 1996, 271:350-353.
61. Massagué J: TGF beta signaling: receptors, transducers, and Mad proteins. Cell 1996, 85:947-950. Joan Massagué, whose group was the first to analyze the mechanism of activation of the TGF-β receptor complex, now provides us with a creative review, integrating MADS in the downstream signalling cascade.
62. Thomsen GH: Xenopus mothers against decapentaplegic is an embryonic ventralizing agent that acts downstream of the BMP-2/4 receptor. Development 1996, 122:2359-2366.
63. Macias-Silva M, Abdollah S, Hoodless PA, Pirone R, Attisano L, Wrana JL: MADR2 is a substrate of the TGF-beta receptor and its phosphorylation is required for nuclear accumulation and signaling. Cell 1996, 87:1215-1224. Proof that a MAD protein transiently associates with the TGF-β receptor complex and is directly phosphorylated on carboxy-terminal serines. Mutation of phosphorylation sites produces a dominant negative molecule that cannot dissociate from the receptor complex and fails to translocate to the nucleus in response to TGF-β.
64. Lechleider RJ, Decaestecker MP, Dehejia A, Polymeropoulos MH, Roberts AB: Serine phosphorylation, chromosomal localization, and transforming growth factor-beta signal transduction by human bsp-1. J Biol Chem 1996, 271:17617-17620.
65. Wieser R, Attisano L, Wrana JL, Massagué J: Signaling activity of transforming growth factor β type II receptors lacking specific domains in the cytoplasmic region. Mol Cell Biol 1993, 13:7239-7247.
66. Brand T, Schneider MD: Inactive type II and type I receptors for TGF-β are dominant inhibitors of TGF-β-dependent transcription. J Biol Chem 1995, 270:8274-8284.
67. Brand T, Maclellan WR, Schneider MD: A dominant-negative receptor for type-beta transforming growth factors created by deletion of the kinase domain. J Biol Chem 1993, 268:11500-11503.
68. Wrana JL, Attisano L, Cárcamo J, Zentella A, Doody J, Laiho M, Wang XF, Massagué J: TGF-β signals through a heteromeric protein kinase receptor complex. Cell 1992, 71:1003-1014.