The B55α Regulatory Subunit of Protein Phosphatase 2A Mediates Fibroblast Growth Factor-Induced p107 Dephosphorylation and Growth Arrest in Chondrocytes
Open accessAbstract
Fibroblast growth factor (FGF)-induced growth arrest of chondrocytes is a unique cell type-specific response which contrasts with the proliferative response of most cell types and underlies several genetic skeletal disorders caused by activating FGF receptor (FGFR) mutations. We have shown that one of the earliest key events in FGF-induced growth arrest is dephosphorylation of the retinoblastoma protein (Rb) family member p107 by protein phosphatase 2A (PP2A), a ubiquitously expressed multisubunit phosphatase. In this report, we show that the PP2A-B55α holoenzyme (PP2A containing the B55α subunit) is responsible for this phenomenon. Only the B55α (55-kDa regulatory subunit, alpha isoform) regulatory subunit of PP2A was able to bind p107, and this interaction was induced by FGF in chondrocytes but not in other cell types. Small interfering RNA (siRNA)-mediated knockdown of B55α prevented p107 dephosphorylation and FGF-induced growth arrest of RCS (rat chondrosarcoma) chondrocytes. Importantly, the B55α subunit bound with higher affinity to dephosphorylated p107. Since the p107 region interacting with B55α is also the site of cyclin-dependent kinase (CDK) binding, B55α association may also prevent p107 phosphorylation by CDKs. FGF treatment induces dephosphorylation of the B55α subunit itself on several serine residues that drastically increases the affinity of B55α for the PP2A A/C dimer and p107. Together these observations suggest a novel mechanism of p107 dephosphorylation mediated by activation of PP2A through B55α dephosphorylation. This mechanism might be a general signal transduction pathway used by PP2A to initiate cell cycle arrest when required by external signals.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
PP2A/B55α helps mediate chondrocyte maturation in response to FGF1.
“PP2A/B55α helps mediate chondrocyte maturation in response to fibroblast growth factor (FGF1) (Kolupaeva et al., 2013; Kurimchak et al., 2013).”
From PP2A holoenzymes, substrate specificity driving cellular functions and deregulation in cancer (2019) · cites this paper as Kolupaeva et al., 2013
FGF1 rapidly dephosphorylates p107 in RCS cells, followed by p130 and pRB, leading to chondrocyte maturation and cell cycle exit.
“Upon FGF1 treatment, p107 is rapidly dephosphorylated in rat chondrosarcoma (RCS) cells, followed by dephosphorylation of p130 and pRB, leading to chondrocyte maturation and cell cycle exit.”
From PP2A holoenzymes, substrate specificity driving cellular functions and deregulation in cancer (2019) · cites this paper as Kolupaeva et al., 2013
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Sequence and structure-based prediction of eukaryotic protein phosphorylation sites
Blom, N., Gammeltoft, S., & Brunak, S. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3310 · Cited by 3,197 · see citing works
The regulation of E2F by pRB-family proteins.
Dyson, N. (1998) · Genes & Development · doi:10.1101/gad.12.15.2245 · Cited by 2,317 · see citing works
Serine/threonine phosphatases: mechanism through structure
Shi, Y. (2009) · Cell · doi:10.1016/j.cell.2009.10.006 · Cited by 1,488 · see citing works
CIP2A inhibits PP2A in human malignancies
Junttila, M. R., Puustinen, P., Niemelä, M., Ahola, R., Arnold, H., Böttzauw, T., Ala-aho, R., Nielsen, C., Ivaska, J., Taya, Y., et al. (2007) · Cell · doi:10.1016/j.cell.2007.04.044 · Cited by 677 · see citing works
Structure and function of WD40 domain proteins
Xu, C., & Min, J. (2011) · Protein & Cell · doi:10.1007/s13238-011-1018-1 · Cited by 644 · see citing works
Regulation of peptide‐chain elongation in mammalian cells
Browne, G. J., & Proud, C. G. (2002) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2002.03290.x · Cited by 469 · see citing works
Shared role of the pRB-related p130 and p107 proteins in limb development.Preprint
Cobrinik, D. E., Lee, M. H., Hannon, G. J., Mulligan, G., Bronson, R. T., Dyson, N. J., Harlow, E. E., Beach, D., Weinberg, R. A., & Jacks, T. (1996) · Genes & Development · doi:10.1101/gad.10.13.1633 · Cited by 426 · see citing works
The Substrate of Greatwall Kinase, Arpp19, Controls Mitosis by Inhibiting Protein Phosphatase 2A
Gharbi-Ayachi, A., Labbé, J., Burgess, A., Vigneron, S., Strub, J., Brioudes, E., DORSSELAER, A. V., Castro, A., & Lorca, T. (2010) · Science · doi:10.1126/science.1197048 · Cited by 415 · see citing works
PP2A holoenzyme assembly: In cauda venenum (the sting is in the tail)
Janssens, V., Longin, S., & Goris, J. (2008) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2007.12.004 · Cited by 390 · see citing works
Kuo, Y.-C., Huang, K.-Y., Yang, C.-H., Yang, Y.-S., Lee, W.-Y., & Chiang, C.-W. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m709585200 · Cited by 367 · see citing works
Multiple pathways regulated by the tumor suppressor PP2A in transformation
Westermarck, J., & Hahn, W. C. (2008) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2008.02.001 · Cited by 344 · see citing works
Schmitz, M. H. A., Held, M., Janssens, V., Hutchins, J. R. A., Hudecz, O., Ivanova, E., Goris, J., Trinkle‐Mulcahy, L., Lamond, A. I., Poser, I., et al. (2010) · Nature Cell Biology · doi:10.1038/ncb2092 · Cited by 316 · see citing works
Mansukhani, A., Bellosta, P., Sahni, M., & Basilico, C. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.149.6.1297 · Cited by 295 · see citing works
Self-citationPhosphatases: providing safe passage through mitotic exit
Wurzenberger, C., & Gerlich, D. W. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3149 · Cited by 293 · see citing works
Structure of a Protein Phosphatase 2A Holoenzyme: Insights into B55-Mediated Tau Dephosphorylation
Xu, Y., Chen, Y., Zhang, P., Jeffrey, P. D., & Shi, Y. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.08.006 · Cited by 285 · see citing works
Denker, A. E., Haas, A. R., Nicoll, S. B., & Tuan, R. S. (1999) · Differentiation · doi:10.1046/j.1432-0436.1999.6420067.x · Cited by 252 · see citing works
Eukaryotic elongation factor‐2 (eEF2): its regulation and peptide chain elongation
Kaul, G., Pattan, G., & Rafeequi, T. (2011) · Cell Biochemistry and Function · doi:10.1002/cbf.1740 · Cited by 216 · see citing works
Longin, S., Zwaenepoel, K., Louis, J. V., Dilworth, S., Goris, J., & Janssens, V. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704059200 · Cited by 184 · see citing works
Dailey, L., Laplantine, E., Priore, R., & Basilico, C. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200302075 · Cited by 156 · see citing works
Self-citationThe B55α Subunit of PP2A Drives a p53-Dependent Metabolic Adaptation to Glutamine Deprivation
Reid, M. A., Wang, W.-I., Rosales, K. R., Welliver, M. X., Pan, M., & Kong, M. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.02.008 · Cited by 154 · see citing works
Elongation factor‐2 kinase and its newly discovered relatives
Ryazanov, A. G. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)02299-8 · Cited by 152 · see citing works
Kalev, P., Šimíček, M., Vázquez, I., Munck, S., Chen, L., Soin, T., Danda, N., Chen, W. L., & Sablina, A. A. (2012) · Cancer Research · doi:10.1158/0008-5472.can-12-1667 · Cited by 127 · see citing works
Association of PI-3 Kinase with PAK1 Leads to Actin Phosphorylation and Cytoskeletal Reorganization
Papakonstanti, E. A., & Stournaras, C. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.02-01-0599 · Cited by 125 · see citing works
Junttila, M. R., Saarinen, S., Schmidt, T. G. M., Kast, J., & Westermarck, J. K. (2005) · PROTEOMICS · doi:10.1002/pmic.200400991 · Cited by 122 · see citing works
Raucci, A., Laplantine, E., Mansukhani, A., & Basilico, C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310384200 · Cited by 121 · see citing works
Self-citationPhosphoprotein Phosphatase 2A: A Novel Druggable Target for Alzheimer’s Disease
Voronkov, M. V., Braithwaite, S. P., & Stock, J. B. (2011) · Future Medicinal Chemistry · doi:10.4155/fmc.11.47 · Cited by 121 · see citing works
p130 and p107 Use a Conserved Domain To Inhibit Cellular Cyclin-Dependent Kinase Activity†
Woo, M. S., Sánchez, I., & Dynlacht, B. D. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.7.3566 · Cited by 114 · see citing works
Zhang, W., Yang, J., Liu, Y., Chen, X., Yu, T., Jia, J., & Liu, C. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.013698 · Cited by 110 · see citing works
PP1 and PP2A phosphatases – cooperating partners in modulating retinoblastoma protein activation
KOLUPAEVA, V. G., & Janssens, V. (2012) · FEBS Journal · doi:10.1111/j.1742-4658.2012.08511.x · Cited by 107 · see citing works
Self-citationAn overlapping kinase and phosphatase docking site regulates activity of the retinoblastoma protein
Hirschi, A., Cecchini, M. J., Steinhardt, R. C., Schamber, M. R., Dick, F. A., & Rubin, S. M. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1868 · Cited by 103 · see citing works
Aikawa, T., Segre, G. V., & Lee, K. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101859200 · Cited by 101 · see citing works
Voorhoeve, P. M., Hijmans, E. M., & Bernards, R. (1999) · Oncogene · doi:10.1038/sj.onc.1202316 · Cited by 101 · see citing works
Culture and Phenotyping of Chondrocytes in Primary Culture
Thirion, S., & Berenbaum, F. (2004) · Humana Press eBooks · doi:10.1385/1-59259-810-2:001 · Cited by 99 · see citing works
SV40 small T antigen and PP2A phosphatase in cell transformation
Sablina, A. A., & Hahn, W. C. (2008) · Cancer and Metastasis Reviews · doi:10.1007/s10555-008-9116-0 · Cited by 95 · see citing works
Janssens, V., & Rebollo, A. (2012) · Current Molecular Medicine · doi:10.2174/156652412799218930 · Cited by 93 · see citing works
Determinants for Substrate Specificity of Protein Phosphatase 2A
Slupe, A. M., Merrill, R. A., & Strack, S. (2011) · Enzyme Research · doi:10.4061/2011/398751 · Cited by 91 · see citing works
Decreased Protein Phosphatase 2A Activity in Hippocampal Long‐Term Potentiation
Fukunaga, K., Müller, D., Ohmitsu, M., Bakó, É., DePaoli-Roach, A. A., & Miyamoto, E. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.740807.x · Cited by 90 · see citing works
Sontag, J., Nunbhakdi‐Craig, V., White, C. L., Halpain, S., & Sontag, E. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.338681 · Cited by 75 · see citing works
Induction of chondrocyte growth arrest by FGF: transcriptional and cytoskeletal alterations
Rozenblatt–Rosen, O., Ornan, E. M., Sadot, E., Madar-Shapiro, L., Sheinin, Y. M., Ginsberg, D., & Yayon, A. (2002) · Journal of Cell Science · doi:10.1242/jcs.115.3.553 · Cited by 70 · see citing works
Dual Cyclin-Binding Domains Are Required for p107 To Function as a Kinase Inhibitor
Castaño, E., Kleyner, Y., & Dynlacht, B. D. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.9.5380 · Cited by 67 · see citing works
Aviezer, D., Golembo, M., & Yayon, A. (2003) · Current Drug Targets · doi:10.2174/1389450033490993 · Cited by 62 · see citing works
Phosphorylation of eEF1A1 at Ser300 by TβR-I results in inhibition of mRNA translation.
Lin, K., Yakymovych, I., Jia, M., Yakymovych, M., & Souchelnytskyi, S. (2010) · Current Biology · doi:10.1016/j.cub.2010.08.017 · Cited by 59 · see citing works
FGF signaling targets the pRb-related p107 and p130 proteins to induce chondrocyte growth arrest
Laplantine, E., Rossi, F., Sahni, M., Basilico, C., & Cobrinik, D. E. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200205025 · Cited by 57 · see citing works
Self-citationProtein Phosphatase 2A as a Potential Target for Anticancer Therapy
Kalev, P., & Sablina, A. A. (2011) · Anti-Cancer Agents in Medicinal Chemistry · doi:10.2174/187152011794941172 · Cited by 57 · see citing works
A Dynamic Equilibrium between CDKs and PP2A Modulates Phosphorylation of pRB, p107 and p130
Garriga, J., Jayaraman, A. L., Limón, A., Jayadeva, G., Sotillo, E., Truongcao, M. M., Patsialou, A., Wadzinski, B. E., & Graña, X. (2004) · Cell Cycle · doi:10.4161/cc.3.10.1183 · Cited by 55 · see citing works
KOLUPAEVA, V. G., Laplantine, E., & Basilico, C. (2008) · PLoS ONE · doi:10.1371/journal.pone.0003447 · Cited by 39 · see citing works
Self-citationJayadeva, G., Kurimchak, A., Garriga, J., Sotillo, E., Davis, A. J., Haines, D. S., Mumby, M., & Graña, X. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.162354 · Cited by 37 · see citing works
The B55α-containing PP2A holoenzyme dephosphorylates FOXO1 in islet β-cells under oxidative stress
Yan, L., Guo, S., Brault, M. A., Harmon, J. S., Robertson, R. P., Hamid, R., Stein, R. W., & Yang, E. (2012) · Biochemical Journal · doi:10.1042/bj20111606 · Cited by 31 · see citing works
Álvarez‐Fernández, M., Halim, V. A., Aprelia, M., Mohammed, S., & Medema, R. H. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.253724 · Cited by 30 · see citing works
5′-AMP-activated protein kinase is inactivated by adrenergic signalling in adult cardiac myocytes
Tsuchiya, Y., Denison, F. C., Heath, R. B., Carling, D., & Saggerson, D. (2011) · Bioscience Reports · doi:10.1042/bsr20110076 · Cited by 11 · see citing works
p27kip1 Protein Levels Reflect a Nexus of Oncogenic Signaling during Cell Transformation
Miller, J. P., Yeh, N., Hofstetter, C. P., Keskin, D., Goldstein, A. S., & Koff, A. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.361972 · Cited by 9 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Fibroblast growth factor signaling in skeletal development and diseasePreprint
Ornitz, D. M., & Marie, P. J. (2015) · Genes & Development · doi:10.1101/gad.266551.115 · Cited by 419 · see citing works
PP2A as a master regulator of the cell cycle
Wlodarchak, N., & Xing, Y. (2016) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2016.1143913 · Cited by 366 · see citing works
Achondroplasia: Development, pathogenesis, and therapy
Ornitz, D. M., & Legeai‐Mallet, L. (2016) · Developmental Dynamics · doi:10.1002/dvdy.24479 · Cited by 264 · see citing works
Meeusen, B., & Janssens, V. (2018) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2017.10.002 · Cited by 96 · see citing works
PP2A holoenzymes, substrate specificity driving cellular functions and deregulation in cancer
(2019) · Advances in Cancer Research · doi:10.1016/bs.acr.2019.03.009 · Cited by 93 · see citing works
Developmental Regulation of the Growth Plate and Cranial Synchondrosis
Wei, X., Hu, M., Mishina, Y. M., & Liu, F. (2016) · Journal of Dental Research · doi:10.1177/0022034516651823 · Cited by 84 · see citing works
The chondrocytic journey in endochondral bone growth and skeletal dysplasia
Tsang, K. Y., Tsang, S. W., Chan, D. T.-M., & Cheah, K. S. E. (2014) · Birth Defects Research Part C Embryo Today Reviews · doi:10.1002/bdrc.21060 · Cited by 73 · see citing works
Karuppaiah, K., Yu, K., Lim, J., Chen, J., Smith, C., Long, F., & Ornitz, D. M. (2016) · Development · doi:10.1242/dev.131722 · Cited by 70 · see citing works
Fibroblast growth factors in skeletal development
Ornitz, D. M., & Marie, P. J. (2019) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/bs.ctdb.2018.11.020 · Cited by 65 · see citing works
Elgenaidi, I. S., & Spiers, P. (2019) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2019.02.011 · Cited by 65 · see citing works
Raman, D., & Pervaiz, S. (2019) · Redox Biology · doi:10.1016/j.redox.2019.101105 · Cited by 55 · see citing works
Zhang, X., Du, W., Zhang, J., Zou, Z., & Ruan, C. (2020) · BMC Genomics · doi:10.1186/s12864-020-07285-4 · Cited by 40 · see citing works
Javadpour, P., Dargahi, L., Ahmadiani, A., & Ghasemi, R. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03063-y · Cited by 35 · see citing works
Kurimchak, A., & Graña, X. (2014) · Cell Cycle · doi:10.4161/15384101.2014.985069 · Cited by 33 · see citing works
Shuhaibar, L. C., Robinson, J. W., Vigone, G., Shuhaibar, N., Egbert, J. R., Baena, V., Uliasz, T. F., Kaback, D., Yee, S., Feil, R., et al. (2017) · eLife · doi:10.7554/elife.31343 · Cited by 34 · see citing works
PP2A/B55α substrate recruitment as defined by the retinoblastoma-related protein p107
Fowle, H. A., Zhao, Z., Xu, Q., Wasserman, J. S., Wang, X., Adeyemi, M., Feiser, F., Kurimchak, A., Atar, D., McEwan, B. C., et al. (2021) · eLife · doi:10.7554/elife.63181 · Cited by 34 · see citing works
Ser/Thr-phosphoprotein phosphatases in chondrogenesis: neglected components of a two-player game
Matta, C., Mobasheri, A., Gergely, P., & Zákány, R. (2014) · Cellular Signalling · doi:10.1016/j.cellsig.2014.06.013 · Cited by 21 · see citing works
Mui, M. Z., Kucharski, M., Miron, M.-J., Hur, W. S., Berghuis, A. M., Blanchette, P., & Branton, P. E. (2013) · PLoS Pathogens · doi:10.1371/journal.ppat.1003742 · Cited by 21 · see citing works
Bálek, L., Gudernová, I., Veselá, I., Hampl, M., Oralová, V., Bosakova, M. K., Vařecha, M., Němec, P., Hall, T. G., Abbadessa, G., et al. (2017) · Bone · doi:10.1016/j.bone.2017.08.016 · Cited by 19 · see citing works
Chapman, J. R., Katsara, O., Ruoff, R., Morgenstern, D., Nayak, S., Basilico, C., Ueberheide, B. M., & KOLUPAEVA, V. G. (2017) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m116.064980 · Cited by 18 · see citing works
Self-citationDoi, K., Takeuchi, H., & Sakurai, H. (2022) · FEBS Journal · doi:10.1111/febs.16612 · Cited by 16 · see citing works
Krzyścik, M., Karl, K., Dudeja, P., Krejci, P., & Hristova, K. (2024) · Cytokine & growth factor reviews · doi:10.1016/j.cytogfr.2024.07.002 · Cited by 14 · see citing works
Zhang, H., Ge, G., Zhang, W., Sun, H., Liang, X., Xia, Y., Du, J., Wu, Z., Bai, J., Yang, H., et al. (2024) · Advanced Science · doi:10.1002/advs.202404080 · Cited by 13 · see citing works
RBL1/p107 Expression Levels Are Modulated by Multiple Signaling Pathways
Ventura, E., Iannuzzi, C. A., Pentimalli, F., Giordano, A., & Morrione, A. (2021) · Cancers · doi:10.3390/cancers13195025 · Cited by 12 · see citing works
Wasserman, J. S., Faezov, B., Patel, K. R., Kurimchak, A., Palacio, S. M., Glass, D. J., Fowle, H. A., McEwan, B. C., Xu, Q., Zhao, Z., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-50015-7 · Cited by 11 · see citing works
Ligand bias underlies differential signaling of multiple FGFs via FGFR1
Karl, K., Piccolo, N. D., Light, T. P., Roy, T., Dudeja, P., Ursachi, V.-C., Fafílek, B., Krejčı́, P., & Hristova, K. A. (2024) · eLife · doi:10.7554/elife.88144.4 · Cited by 9 · see citing works
Ábrahám, E., Yu, P., Farkas, I., Darula, Z., Varga, E., Lukács, N., Ayaydin, F., Medzihradszky, K. F., Dombrádi, V., Dudits, D., et al. (2014) · Plant Molecular Biology · doi:10.1007/s11103-014-0265-y · Cited by 7 · see citing works
Ligand bias underlies differential signaling of multiple FGFs via FGFR1
Karl, K., Piccolo, N. D., Light, T. P., Roy, T., Dudeja, P., Ursachi, V.-C., Fafílek, B., Krejčı́, P., & Hristova, K. A. (2023) · eLife · doi:10.7554/elife.88144 · Cited by 5 · see citing works
Fibroblast growth factor (FGF) and FGF receptor families in bone
Marie, P. J., Hurley, M. M., & Ornitz, D. M. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-814841-9.00045-2 · Cited by 3 · see citing works
Wasserman, J. S., Faezov, B., Patel, K. R., Kurimchak, A., Palacio, S. M., Fowle, H. A., McEwan, B. C., Xu, Q., Zhao, Z., Cressey, L. E., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.03.06.531310 · Cited by 3 · see citing works
Ligand bias underlies differential signaling of multiple FGFs via FGFR1Preprint
Karl, K., Piccolo, N. D., Light, T. P., Roy, T., Dudeja, P., Ursachi, V.-C., Fafílek, B., Krejčı́, P., & Hristova, K. A. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.01.06.475273 · Cited by 2 · see citing works
Molecular Control of Cartilage Differentiation
Wuelling, M., & Vortkamp, A. (2016) · Springer eBooks · doi:10.1007/978-3-319-29568-8_8 · Cited by 1 · see citing works
Ligand bias underlies differential signaling of multiple FGFs via FGFR1Preprint
Karl, K., Piccolo, N. D., Light, T. P., Roy, T., Dudeja, P., Ursachi, V.-C., Fafílek, B., Krejčı́, P., & Hristova, K. A. (2023) · eLife · doi:10.7554/elife.88144.3 · Cited by 1 · see citing works
Serine/Threonine-Protein Phosphatase 2A
Janssens, V. (2016) · Springer eBooks · doi:10.1007/978-1-4614-6438-9_101865-1
Serine/Threonine-Protein Phosphatase 2A
Janssens, V. (2017) · Springer eBooks · doi:10.1007/978-3-319-67199-4_101865
Ligand bias underlies differential signaling of multiple FGFs via FGFR1Preprint
Karl, K., Piccolo, N. D., Light, T. P., Roy, T., Dudeja, P., Ursachi, V.-C., Fafílek, B., Krejčı́, P., & Hristova, K. A. (2023) · eLife · doi:10.7554/elife.88144.2
Zhang, X., Du, W., Zhang, J., Zou, Z., & ChangChun, R. (2020) · Figshare · doi:10.6084/m9.figshare.13336489
- Authors
- Kolupaeva, V., Daempfling, L., & Basilico, C.
- Affiliations
- New York University (US)
- ORCID
- Kolupaeva, Victoria
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 2013-08-01
- Volume
- 33
- Issue
- 15
- Pages
- 2865-2878
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- PMC
- PMC3719682
- OpenAlex
- W2096035361
- Cited by
- 37
- References
- 51
- Citations by year
- 2024: 4 · 2023: 4 · 2022: 2 · 2021: 2 · 2020: 2 · 2019: 6 · 2017: 5 · 2016: 6 · 2015: 1 · 2014: 4 · 2013: 1
- FWCI
- 1.79
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Molecular and Cellular Biology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Cancer Institute (T32CA009161)
- National Institute of Dental and Craniofacial Research (DE013745, R01DE013745)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fibroblast Growth Factor Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- protein phosphatase 2A, FGF signaling, retinoblastoma protein family, cell cycle arrest, signal transduction, bone disease
- MeSH terms
- Amino Acid Sequence, Animals, Bone Neoplasms, Chondrosarcoma, Molecular Sequence Data, Phosphorylation, Fibroblast Growth Factor 1, Chondrocytes, Protein Subunits, Cell Line, Tumor, Cell Proliferation, Retinoblastoma-Like Protein p107, Rats, Protein Phosphatase 2, Protein Interaction Maps
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
