Signaling dynamics of the KSR1 scaffold complex

Coordinating ERK/MAPK signalling through scaffolds and inhibitors

Kölch, W. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1743 · Cited by 1,070 · see citing works

Bmi-1 collaborates with c-Myc in tumorigenesis by inhibiting c-Myc-induced apoptosis via INK4a/ARFPreprint

Jacobs, J. J. L., Scheijen, B., Voncken, J. W., Kieboom, K., Berns, A. J. M., & van Lohuizen, M. (1999) · Genes & Development · doi:10.1101/gad.13.20.2678 · Cited by 1,060 · see citing works

The MEK/ERK cascade: From signaling specificity to diverse functions

Shaul, Y. D., & Seger, R. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.10.005 · Cited by 934 · see citing works

Regulation of MAP Kinase Signaling Modules by Scaffold Proteins in Mammals

Morrison, D. K., & Davis, R. J. (2003) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.19.111401.091942 · Cited by 787 · see citing works

Integrating signals from RTKs to ERK/MAPK

Mckay, M., & Morrison, D. K. (2007) · Oncogene · doi:10.1038/sj.onc.1210394 · Cited by 616 · see citing works

MP1: A MEK Binding Partner That Enhances Enzymatic Activation of the MAP Kinase Cascade

Schaeffer, H. J., Catling, A. D., Eblen, S. T., Collier, L. S., Krauss, A., & Weber, M. J. (1998) · Science · doi:10.1126/science.281.5383.1668 · Cited by 472 · see citing works

Multiple docking sites on substrate proteins form a modular system that mediates recognition by ERK MAP kinase

Jacobs, D., Glossip, D., Xing, H., Muslin, A. J., & Kornfeld, K. (1999) · Genes & Development · doi:10.1101/gad.13.2.163 · Cited by 439 · see citing works

Localization of the MP1-MAPK Scaffold Complex to Endosomes Is Mediated by p14 and Required for Signal Transduction

Teis, D., Wunderlich, W., & Huber, L. A. (2002) · Developmental Cell · doi:10.1016/s1534-5807(02)00364-7 · Cited by 371 · see citing works

Using Engineered Scaffold Interactions to Reshape MAP Kinase Pathway Signaling Dynamics

Bashor, C. J., Helman, N. C., Yan, S., & Lim, W. A. (2008) · Science · doi:10.1126/science.1151153 · Cited by 347 · see citing works

KSR, a novel protein kinase required for RAS signal transduction

Therrien, M., Chang, H. C., Solomon, N. M., Karim, F. D., Wassarman, D. A., & Rubin, G. M. (1995) · Cell · doi:10.1016/0092-8674(95)90204-x · Cited by 340 · see citing works

The C. elegans ksr-1 gene encodes a novel raf-related kinase involved in Ras-mediated signal transduction

Sundaram, M. V., & Han, M. (1995) · Cell · doi:10.1016/0092-8674(95)90205-8 · Cited by 308 · see citing works

The ksr-1 gene encodes a novel protein kinase involved in Ras-mediated signaling in C. elegans

Kornfeld, K., Hom, D. B., & Horvitz, H. R. (1995) · Cell · doi:10.1016/0092-8674(95)90206-6 · Cited by 299 · see citing works

Protein phosphatase 2A positively regulates Ras signaling by dephosphorylating KSR1 and Raf-1 on critical 14-3-3 binding sites

Ory, S., Zhou, M., Conrads, T. P., Veenstra, T. D., & Morrison, D. K. (2003) · Current Biology · doi:10.1016/s0960-9822(03)00535-9 · Cited by 296 · see citing works

Docking Motif Interactions in MAP Kinases Revealed by Hydrogen Exchange Mass Spectrometry

Lee, T., Hoofnagle, A. N., Kabuyama, Y., Stroud, J., Min, X., Goldsmith, E. J., Chen, L., Resing, K. A., & Ahn, N. G. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00161-3 · Cited by 282 · see citing works

C-TAK1 Regulates Ras Signaling by Phosphorylating the MAPK Scaffold, KSR1

Müller, J., Ory, S., Copeland, T., Piwnica-Worms, H. M., & Morrison, D. K. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00383-5 · Cited by 274 · see citing works

Kinase Suppressor of Ras (KSR) Is a Scaffold Which Facilitates Mitogen-Activated Protein Kinase Activation In Vivo

Nguyen, A., Burack, R., Stock, J. L., Kortum, R. L., Chaika, O. V., Afkarian, M., Muller, W. J., MURPHY, K. M. M., Morrison, D. K., Lewis, R. E., et al. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.9.3035-3045.2002 · Cited by 269 · see citing works

KSR is a scaffold required for activation of the ERK/MAPK module

Roy, F., Laberge, G., Douziech, M., Ferland-McCollough, D., & Therrien, M. (2002) · Genes & Development · doi:10.1101/gad.962902 · Cited by 217 · see citing works

Identification of Constitutive and Ras-Inducible Phosphorylation Sites of KSR: Implications for 14-3-3 Binding, Mitogen-Activated Protein Kinase Binding, and KSR Overexpression

Cacace, A. M., Michaud, N. R., Therrien, M., Mathes, K. D., Copeland, T., Rubin, G. M., & Morrison, D. K. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.1.229 · Cited by 209 · see citing works

Kinase Suppressor of Ras Forms a Multiprotein Signaling Complex and Modulates MEK Localization

Stewart, S., Sundaram, M. V., Zhang, Y., Lee, J., Han, M., & Guan, K. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.8.5523 · Cited by 209 · see citing works

Regulation of the MAP kinase pathway by mammalian Ksr through direct interaction with MEK and ERK

Yu, W., Fantl, W. J., Harrowe, G., & Williams, L. T. (1998) · Current Biology · doi:10.1016/s0960-9822(98)70020-x · Cited by 197 · see citing works

A Proline-Rich Sequence Unique to MEK1 and MEK2 Is Required for Raf Binding and Regulates MEK Function

Catling, A. D., Schaeffer, H. J., Reuter, C. W., Reddy, G. R., & Weber, M. J. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.10.5214 · Cited by 197 · see citing works

Murine Ksr interacts with MEK and inhibits Ras-induced transformation

Denouel-Galy, A., Douville, E. M. J., Warne, P. H., Papin, C., Laugier, D., Calothy, G., Downward, J., & Eychène, A. (1998) · Current Biology · doi:10.1016/s0960-9822(98)70019-3 · Cited by 150 · see citing works

Activation of c‐Raf‐1 by Ras and Src through different mechanisms: activation in vivo and in vitro

Stokoe, D., & McCormick, F. P. (1997) · The EMBO Journal · doi:10.1093/emboj/16.9.2384 · Cited by 146 · see citing works

The Molecular Scaffold KSR1 Regulates the Proliferative and Oncogenic Potential of Cells

Kortum, R. L., & Lewis, R. E. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.10.4407-4416.2004 · Cited by 145 · see citing works

Ras Subcellular Localization Defines Extracellular Signal-Regulated Kinase 1 and 2 Substrate Specificity through Distinct Utilization of Scaffold Proteins

Casar, B., Arozarena, I., Sanz-Moreno, V., Pinto, A., Agudo-Ibáñez, L., Marais, R., Lewis, R. E., Berciano, M., & Crespo, P. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01359-08 · Cited by 126 · see citing works

Identification of novel ERK-mediated feedback phosphorylation sites at the C-terminus of B-Raf

Brummer, T., Naegele, H., Reth, M. G., & Misawa, Y. (2003) · Oncogene · doi:10.1038/sj.onc.1207185 · Cited by 115 · see citing works

Proteomics Analysis of Protein Kinases by Target Class-selective Prefractionation and Tandem Mass Spectrometry

Wissing, J. B., Jänsch, L., Nimtz, M., Dieterich, G., Hornberger, R., Kéri, G., Wehland, J., & Daub, H. (2006) · Molecular & Cellular Proteomics · doi:10.1074/mcp.t600062-mcp200 · Cited by 112 · see citing works

CK2 Is a Component of the KSR1 Scaffold Complex that Contributes to Raf Kinase Activation

Ritt, D. A., Zhou, M., Conrads, T. P., Veenstra, T. D., Copeland, T. D., & Morrison, D. K. (2006) · Current Biology · doi:10.1016/j.cub.2006.11.061 · Cited by 100 · see citing works

Identification of B-KSR1, a Novel Brain-Specific Isoform of KSR1 That Functions in Neuronal Signaling

Müller, J., Cacace, A. M., Lyons, W. E., McGill, C. B., & Morrison, D. K. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.15.5529-5539.2000 · Cited by 89 · see citing works

The Molecular Scaffold Kinase Suppressor of Ras 1 (KSR1) Regulates Adipogenesis

Kortum, R. L., Costanzo, D. L., Haferbier, J. L., Schreiner, S. J., Razidlo, G. L., Wu, M.-H., Volle, D. J., Mori, T., Sakaue, H., Chaika, N. V., et al. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.17.7592-7604.2005 · Cited by 80 · see citing works

The MEK1 Scaffolding Protein MP1 Regulates Cell Spreading by Integrating PAK1 and Rho Signals

Pullikuth, A., McKinnon, E., Schaeffer, H. J., & Catling, A. D. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.12.5119-5133.2005 · Cited by 65 · see citing works

Compartmentalised MAPK Pathways

Brown, M. D., & Sacks, D. B. (2008) · Handbook of experimental pharmacology · doi:10.1007/978-3-540-72843-6_9 · Cited by 58 · see citing works

Phosphorylation of the Kinase Suppressor of Ras by Associated Kinases

Volle, D. J., Fulton, J. A., Chaika, O. V., McDermott, K., Huang, H., Steinke, L., & Lewis, R. E. (1999) · Biochemistry · doi:10.1021/bi983050d · Cited by 33 · see citing works

Caspase-dependent Cleavage Disrupts the ERK Cascade Scaffolding Function of KSR1

McKay, M., & Morrison, D. K. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702692200 · Cited by 19 · see citing works

Scaffold Proteins: Hubs for Controlling the Flow of Cellular Information

Good, M. C., Zalatan, J. G., & Lim, W. A. (2011) · Science · doi:10.1126/science.1198701 · Cited by 886 · see citing works

Regulation of RAF protein kinases in ERK signalling

Lavoie, H., & Therrien, M. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3979 · Cited by 683 · see citing works

Negative feedback regulation of the ERK1/2 MAPK pathway

Lake, D., Corrêa, S. A. L., & Müller, J. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2297-8 · Cited by 565 · see citing works

JNK Signaling: Regulation and Functions Based on Complex Protein-Protein Partnerships

Zeke, A., Misheva, M., Reményi, A., & Bogoyevitch, M. A. (2016) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00043-14 · Cited by 524 · see citing works

Raf Family Kinases: Old Dogs Have Learned New Tricks

Matallanas, D., Birtwistle, M. R., Romano, D., Zebisch, A., Rauch, J., von Kriegsheim, A., & Kölch, W. (2011) · Genes & Cancer · doi:10.1177/1947601911407323 · Cited by 383 · see citing works

Disruption of CRAF-Mediated MEK Activation Is Required for Effective MEK Inhibition in KRAS Mutant Tumors

Lito, P., Saborowski, A., Yue, J., Solomon, M., Joseph, E., Gadal, S., Saborowski, M., Kastenhuber, E., Fellmann, C., Ohara, K., et al. (2014) · Cancer Cell · doi:10.1016/j.ccr.2014.03.011 · Cited by 324 · see citing works

Molecular basis of MAP kinase regulation

Peti, W., & Page, R. (2013) · Protein Science · doi:10.1002/pro.2374 · Cited by 302 · see citing works

A Raf-induced allosteric transition of KSR stimulates phosphorylation of MEK

Brennan, D. F., Dar, A. C., Hertz, N. T., Chao, W. C. H., Burlingame, A. L., Shokat, K. M., & Barford, D. (2011) · Nature · doi:10.1038/nature09860 · Cited by 254 · see citing works

Structure of the BRAF-MEK Complex Reveals a Kinase Activity Independent Role for BRAF in MAPK Signaling

Haling, J. R., Sudhamsu, J., Yen, I., Sideris, S., Sandoval, W. N., Phung, W., Bravo, B. J., Giannetti, A. M., Peck, A., Masselot, A., et al. (2014) · Cancer Cell · doi:10.1016/j.ccr.2014.07.007 · Cited by 242 · see citing works

The MEK/ERK Network as a Therapeutic Target in Human Cancer

Barbosa, R. L., Acevedo, L. A., & Marmorstein, R. (2020) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-20-0687 · Cited by 212 · see citing works

Functional proteomics to dissect tyrosine kinase signalling pathways in cancer

Kölch, W., & Pitt, A. R. (2010) · Nature reviews. Cancer · doi:10.1038/nrc2900 · Cited by 200 · see citing works

Targeting oncogenic Raf protein-serine/threonine kinases in human cancers

Roskoski, R. J. (2018) · Pharmacological Research · doi:10.1016/j.phrs.2018.08.013 · Cited by 194 · see citing works

Ras-Mediated Activation of the Raf Family KinasesPreprint

Terrell, E. M., & Morrison, D. K. (2018) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a033746 · Cited by 189 · see citing works

MEK5/ERK5 Pathway: The first fifteen years

Drew, B. A., Burow, M., & Beckman, B. (2011) · Biochimica et Biophysica Acta · doi:10.1016/j.bbcan.2011.10.002 · Cited by 198 · see citing works

BSK s are partially redundant positive regulators of brassinosteroid signaling in A rabidopsis

Sreeramulu, S., Mostizky, Y., Sunitha, S., Shani, E., Nahum, H., Salomon, D., Hayun, L. B., Gruetter, C., Rauh, D., Ori, N., et al. (2013) · The Plant Journal · doi:10.1111/tpj.12175 · Cited by 183 · see citing works

A Ras Signaling Complex Controls the RasC-TORC2 Pathway and Directed Cell Migration

Charest, P. G., Shen, Z., Lakoduk, A. M., Sasaki, A. T., Briggs, S. P., & Firtel, R. (2010) · Developmental Cell · doi:10.1016/j.devcel.2010.03.017 · Cited by 152 · see citing works

Pseudokinases-remnants of evolution or key allosteric regulators?

Zeqiraj, E., & van Aalten, D. M. F. (2010) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2010.10.001 · Cited by 144 · see citing works

Mutation that blocks ATP binding creates a pseudokinase stabilizing the scaffolding function of kinase suppressor of Ras, CRAF and BRAF

Hu, J., Yu, H., Kornev, A. P., Zhao, J., Filbert, E. L., Taylor, S. S., & Shaw, A. S. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1102554108 · Cited by 133 · see citing works

Phosphorylation of BRAF by AMPK Impairs BRAF-KSR1 Association and Cell Proliferation

Shen, C., Yuan, P., Pérez‐Lorenzo, R., Zhang, Y., Lee, S. X., Ou, Y., Asara, J. M., Cantley, L. C., & Zheng, B. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.08.044 · Cited by 132 · see citing works

Navigating the ERK1/2 MAPK Cascade

Martín-Vega, A., & Cobb, M. H. (2023) · Biomolecules · doi:10.3390/biom13101555 · Cited by 124 · see citing works

A Novel Systems-Biology Algorithm for the Analysis of Coordinated Protein Responses Using Quantitative Proteomics

Garcia-Marques, F. J., Trevisán-Herraz, M., Martı́nez-Martı́nez, S., Camafeita, E., Jorge, I., López, J. A., Méndez‐Barbero, N., Méndez‐Ferrer, S., del Pozo, M. Á., Ibáñez, B., et al. (2016) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m115.055905 · Cited by 113 · see citing works

Sulfiredoxin–Peroxiredoxin IV axis promotes human lung cancer progression through modulation of specific phosphokinase signaling

Wei, Q., Jiang, H., Xiao, Z., Baker, A. R., Young, M. R., Veenstra, T. D., & Colburn, N. H. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1013012108 · Cited by 111 · see citing works

Mechanisms shaping the role of ERK1/2 in cellular sene scence (Review)

Zou, J., Lei, T., Guo, P., Yu, J., Xu, Q., Luo, Y., Ke, R., & Huang, D. (2018) · Molecular Medicine Reports · doi:10.3892/mmr.2018.9712 · Cited by 107 · see citing works

Self-signalling and self-fusion in filamentous fungi

Read, N. D., Lichius, A., Shoji, J., & Goryachev, A. B. (2009) · Current Opinion in Microbiology · doi:10.1016/j.mib.2009.09.008 · Cited by 105 · see citing works

There’s more to death than life: Noncatalytic functions in kinase and pseudokinase signaling

Mace, P. D., & Murphy, J. M. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100705 · Cited by 99 · see citing works

Small molecule stabilization of the KSR inactive state antagonizes oncogenic Ras signalling

Dhawan, N. S., Scopton, A. P., & Dar, A. C. (2016) · Nature · doi:10.1038/nature19327 · Cited by 94 · see citing works

How scaffolds shape MAPK signaling: what we know and opportunities for systems approaches

Witzel, F., Maddison, L. E., & Blüthgen, N. (2012) · Frontiers in Physiology · doi:10.3389/fphys.2012.00475 · Cited by 94 · see citing works

ERK and PDE4 cooperate to induce RAF isoform switching in melanoma

Marquette, A., André, J., Bagot, M., Bensussan, A., & Dumaz, N. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2022 · Cited by 89 · see citing works

RSK phosphorylates SOS1 creating 14-3-3-docking sites and negatively regulating MAPK activation

Saha, M., Carriere, A., Cheerathodi, M., Zhang, X., Lavoie, G., Rush, A. J., Roux, P. P., & Ballif, B. A. (2012) · Biochemical Journal · doi:10.1042/bj20120938 · Cited by 88 · see citing works

Modularity and functional plasticity of scaffold proteins as p(l)acemakers in cell signaling

Pan, C. Q., Sudol, M., Sheetz, M. P., & Low, B. C. (2012) · Cellular Signalling · doi:10.1016/j.cellsig.2012.06.002 · Cited by 84 · see citing works

Gene Deletions and Amplifications in Human Hepatocellular Carcinomas

Nalesnik, M. A., Tseng, G. C., Ding, Y., Xiang, G., Zheng, Z., Yu, Y., Marsh, J. W., Michalopoulos, G. K., & Luo, J. (2012) · American Journal Of Pathology · doi:10.1016/j.ajpath.2011.12.021 · Cited by 80 · see citing works

Pathogen-inducible OsMPKK10.2-OsMPK6 cascade phosphorylates the Raf-like kinase OsEDR1 and inhibits its scaffold function to promote rice disease resistance

Ma, H., Li, J., Ma, L., Wang, P., Xue, Y. C., Yin, P., Xiao, J., & Wang, S. (2021) · Molecular Plant · doi:10.1016/j.molp.2021.01.008 · Cited by 78 · see citing works

RAF Inhibitor-Induced KSR1/B-RAF Binding and Its Effects on ERK Cascade Signaling

McKay, M., Ritt, D. A., & Morrison, D. K. (2011) · Current Biology · doi:10.1016/j.cub.2011.02.033 · Cited by 77 · see citing works

Mechanistic principles of RAF kinase signaling

Udell, C. M., Rajakulendran, T., Sicheri, F., & Therrien, M. (2010) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-010-0520-6 · Cited by 74 · see citing works

Agent-based simulation of reactions in the crowded and structured intracellular environment: Influence of mobility and location of the reactants

Klann, M., Lapin, A., & Reuß, M. (2011) · BMC Systems Biology · doi:10.1186/1752-0509-5-71 · Cited by 73 · see citing works

Accessory proteins of the RAS-MAPK pathway: moving from the side line to the front line

Pudewell, S., Wittich, C., Jasemi, N. S. K., Bazgir, F., & Ahmadian, M. R. (2021) · Communications Biology · doi:10.1038/s42003-021-02149-3 · Cited by 72 · see citing works

Src inhibitors, PP2 and dasatinib, increase retinoic acid-induced association of Lyn and c-Raf (S259) and enhance MAPK-dependent differentiation of myeloid leukemia cells

Congleton, J., MacDonald, R., & Yen, A. (2011) · Leukemia · doi:10.1038/leu.2011.390 · Cited by 69 · see citing works

Vitamin D3-driven signals for myeloid cell differentiation—Implications for differentiation therapy

Hughes, P., Marcinkowska, E., Gocek, E., Studzinski, G. P., & Brown, G. (2009) · Leukemia Research · doi:10.1016/j.leukres.2009.09.010 · Cited by 66 · see citing works

Network rewiring is an important mechanism of gene essentiality change

Kim, J., Kim, I., Han, S. K., Bowie, J. U., & Kim, S. (2012) · Scientific Reports · doi:10.1038/srep00900 · Cited by 62 · see citing works

Phosphorylation of Rap1 by cAMP-dependent Protein Kinase (PKA) Creates a Binding Site for KSR to Sustain ERK Activation by cAMP

Takahashi, M., Li, Y., Dillon, T. J., & Stork, P. A. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.768986 · Cited by 59 · see citing works

Signalling dynamics in embryonic development

Sonnen, K. F., & Janda, C. Y. (2021) · Biochemical Journal · doi:10.1042/bcj20210043 · Cited by 56 · see citing works

Kinase Suppressor of Ras 2 (KSR2) Regulates Tumor Cell Transformation via AMPK

Fernandez, M. R., Henry, M. D., & Lewis, R. E. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.06754-11 · Cited by 56 · see citing works

Divergent effects of intrinsically active MEK variants on developmental Ras signaling

Goyal, Y., Jindal, G. A., Pelliccia, J. L., Yamaya, K., Yeung, E., Futran, A. S., Burdine, R. D., Schüpbach, T., & Shvartsman, S. Y. (2017) · Nature Genetics · doi:10.1038/ng.3780 · Cited by 55 · see citing works

Partner exchange: protein–protein interactions in the Raf pathway

Wimmer, R., & Baccarini, M. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.06.001 · Cited by 52 · see citing works

Elucidation of the binding preferences of peptide recognition modules: SH3 and PDZ domains

Teyra, J., Sidhu, S. S., & Kim, P. M. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.05.043 · Cited by 49 · see citing works

VRK2 anchors KSR1-MEK1 to endoplasmic reticulum forming a macromolecular complex that compartmentalizes MAPK signaling

Fernández, I. F., Perez‐Rivas, L. G., Blanco, S., Castillo-Dominguez, A. A., Lozano, J., & Lazo, P. A. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1056-8 · Cited by 47 · see citing works

Mechanistic model of MAPK signaling reveals how allostery and rewiring contribute to drug resistance

Fröhlich, F., Gerosa, L., Muhlich, J. L., & Sorger, P. K. (2023) · Molecular Systems Biology · doi:10.15252/msb.202210988 · Cited by 48 · see citing works

Nesprin-2-dependent ERK1/2 compartmentalisation regulates the DNA damage response in vascular smooth muscle cell ageing

Warren, D. T., Tajsic, T., Porter, L. J., Minaisah, R.-M., Cobb, A. M., Jacob, A., Rajgor, D., Zhang, Q., & Shanahan, C. M. (2015) · Cell Death and Differentiation · doi:10.1038/cdd.2015.12 · Cited by 43 · see citing works

Transcriptome-based analysis of mitogen-activated protein kinase cascades in the rice response to Xanthomonas oryzae infection

Yang, Z., Ma, H., Hong, H., Yao, W., Xie, W., Xiao, J., Li, X., & Wang, S. (2015) · Rice · doi:10.1186/s12284-014-0038-x · Cited by 45 · see citing works

Structural basis of autoregulatory scaffolding by apoptosis signal-regulating kinase 1

Weijman, J. F., Kumar, A., Jamieson, S. A., King, C., Caradoc-Davies, T. T., Ledgerwood, E. C., Murphy, J. M., & Mace, P. D. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1620813114 · Cited by 44 · see citing works

Therapeutic potential of MEK inhibition in acute myelogenous leukemia: rationale for “vertical” and “lateral” combination strategies

Ricciardi, M. R., Scerpa, M. C., Bergamo, P., Ciuffreda, L., Petrucci, M. T., Chiaretti, S., Tavolaro, S., Mascolo, M. G., Abrams, S. L., Steelman, L. S., et al. (2012) · Journal of Molecular Medicine · doi:10.1007/s00109-012-0886-z · Cited by 43 · see citing works

Discovery of Raf Family Is a Milestone in Deciphering the Ras-Mediated Intracellular Signaling Pathway

Zhao, J., & Luo, Z. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23095158 · Cited by 42 · see citing works

SEL-10/Fbw7-dependent negative feedback regulation of LIN-45/Braf signaling in C. elegans via a conserved phosphodegronPreprint

de la Cova, C., & Greenwald, I. (2012) · Genes & Development · doi:10.1101/gad.203703.112 · Cited by 41 · see citing works

The dual function of KSR1: a pseudokinase and beyond

Zhang, H., Koo, C.-Y., Stebbing, J., & Giamas, G. (2013) · Biochemical Society Transactions · doi:10.1042/bst20130042 · Cited by 40 · see citing works

Spatially Dependent Dynamic MAPK Modulation by the Nde1-Lis1-Brap Complex Patterns Mammalian CNS

Chomiak, A. A., Peng, C., Pawlisz, A. S., Joksimovic, M., & Feng, Y. (2013) · Developmental Cell · doi:10.1016/j.devcel.2013.04.006 · Cited by 40 · see citing works

praja2 regulates KSR1 stability and mitogenic signaling

Rinaldi, L., Donne, R. D., Sepe, M., Porpora, M., Garbi, C., Chiuso, F., Gallo, A., Parisi, S., Russo, L., Bachmann, V. A., et al. (2016) · Cell Death and Disease · doi:10.1038/cddis.2016.109 · Cited by 39 · see citing works

Regulators of the RAS-ERK pathway as therapeutic targets in thyroid cancer

Zaballos, M. A., Acuña-Ruíz, A., Morante, M., Crespo, P., & Santisteban, P. (2019) · Endocrine Related Cancer · doi:10.1530/erc-19-0098 · Cited by 39 · see citing works

Hierarchical scaffolding of an ERK1/2 activation pathway

Vetterkind, S., Poythress, R. H., Lin, Q., & Morgan, K. G. (2013) · Cell Communication and Signaling · doi:10.1186/1478-811x-11-65 · Cited by 38 · see citing works

A CC-SAM, for Coiled Coil–Sterile α Motif, Domain Targets the Scaffold KSR-1 to Specific Sites in the Plasma Membrane

Koveal, D., Schuh-Nuhfer, N., Ritt, D., Page, R., Morrison, D. K., & Peti, W. (2012) · Science Signaling · doi:10.1126/scisignal.2003289 · Cited by 36 · see citing works

Targeting RAS mutants in malignancies: successes, failures, and reasons for hope

Yang, H. S., Zhou, X., Fu, D., Le, C., Wang, J., Zhou, Q., Liu, X., Yuan, Y., Ding, K., & Xiao, Q. (2022) · 癌症：英文版 · doi:10.1002/cac2.12377 · Cited by 35 · see citing works

ERK Signals: Scaffolding Scaffolds?

Casar, B., & Crespo, P. (2016) · Front. Cell Dev. Biol. · doi:10.3389/fcell.2016.00049 · Cited by 34 · see citing works

Coordinating ERK signaling via the molecular scaffold Kinase Suppressor of Ras

Frodyma, D. E., Neilsen, B. K., Costanzo-Garvey, D. L., Fisher, K. W., & Lewis, R. E. (2017) · F1000Research · doi:10.12688/f1000research.11895.1 · Cited by 35 · see citing works

KSR induces RAS‐independent MAPK pathway activation and modulates the efficacy of KRAS inhibitors

Paniagua, G., Jacob, H. K. C., Brehey, O., García‐Alonso, S., Lechuga, C. G., Pons, T., Musteanu, M., Guerra, C., Drosten, M., & Barbacid, M. (2022) · Molecular Oncology · doi:10.1002/1878-0261.13213 · Cited by 34 · see citing works

KSR as a therapeutic target for Ras-dependent cancers

Neilsen, B. K., Frodyma, D. E., Lewis, R. E., & Fisher, K. W. (2017) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2017.1311325 · Cited by 33 · see citing works

KSR1 and EPHB4 Regulate Myc and PGC1β To Promote Survival of Human Colon Tumors

McCall, J. L., Gehring, D., Neilsen, B. K., Fisher, K. W., Das, B., Kelly, D. L., Kim, H.-S., White, M. A., & Lewis, R. E. (2016) · Molecular and Cellular Biology · doi:10.1128/mcb.00087-16 · Cited by 33 · see citing works

Anchorage-independent growth conditions reveal a differential SOS2 dependence for transformation and survival in RAS-mutant cancer cells

Sheffels, E., Sealover, N. E., Theard, P. L., & Kortum, R. L. (2019) · Small GTPases · doi:10.1080/21541248.2019.1611168 · Cited by 30 · see citing works

SOS1 and KSR1 modulate MEK inhibitor responsiveness to target resistant cell populations based on PI3K and KRAS mutation status

Daley, B. R., Vieira, H. M., Rao, C., Hughes, J. M., Beckley, Z., Huisman, D. H., Chatterjee, D., Sealover, N. E., Cox, K., Askew, J. W., et al. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2313137120 · Cited by 30 · see citing works

Treatment of cultured human astrocytes and vascular endothelial cells with protein kinase CK2 inhibitors induces early changes in cell shape and cytoskeleton

Kramerov, A. A., Golub, A. G., Bdzhola, V. G., Yarmoluk, S. M., Ahmed, K., Bretner, M., & Ljubimov, A. V. (2010) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-010-0667-3 · Cited by 31 · see citing works

The interplay of double phosphorylation and scaffolding in MAPK pathways

Kocieniewski, P., Faeder, J. R., & Lipniacki, T. (2011) · Journal of Theoretical Biology · doi:10.1016/j.jtbi.2011.11.014 · Cited by 30 · see citing works

Phospho-proteomic analyses of B-Raf protein complexes reveal new regulatory principles

Eisenhardt, A. E., Sprenger, A., Röring, M., Herr, R., Weinberg, F., Köhler, M., Braun, S. L., Orth, J. H. C., Diedrich, B., Lanner, U., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.8427 · Cited by 30 · see citing works

Leukocyte‐Specific Protein 1: A Novel Regulator of Hepatocellular Proliferation and Migration Deleted in Human Hepatocellular Carcinoma

Koral, K., Paranjpe, S., Bowen, W. C., Mars, W. M., Luo, J., & Michalopoulos, G. K. (2014) · Hepatology · doi:10.1002/hep.27444 · Cited by 29 · see citing works

B-Raf and CRHR1 Internalization Mediate Biphasic ERK1/2 Activation by CRH in Hippocampal HT22 Cells

Bonfiglio, J. J., Inda, C., Senin, S. A., Maccarrone, G., Refojo, D., Giacomini, D., Turck, C. W., Holsboer, F., ARZT, E. S., & Silberstein, S. (2013) · Molecular Endocrinology · doi:10.1210/me.2012-1359 · Cited by 27 · see citing works

Growth factor–dependent ErbB vesicular dynamics couple receptor signaling to spatially and functionally distinct Erk pools

Brüggemann, Y., Karajannis, L. S., Stanoev, A., Stallaert, W., & Bastiaens, P. I. H. (2021) · Science Signaling · doi:10.1126/scisignal.abd9943 · Cited by 27 · see citing works

Complexity in KSR function revealed by Raf inhibitor and KSR structure studies

McKay, M., Freeman, A. K., & Morrison, D. K. (2011) · Small GTPases · doi:10.4161/sgtp.2.5.17740 · Cited by 27 · see citing works

Caveolin-1 Is Required for Kinase Suppressor of Ras 1 (KSR1)-Mediated Extracellular Signal-Regulated Kinase 1/2 Activation, H-RasV12-Induced Senescence, and Transformation

Kortum, R. L., Fernandez, M. R., Costanzo-Garvey, D. L., Johnson, H. J., Fisher, K. W., Volle, D. J., & Lewis, R. E. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.01633-13 · Cited by 26 · see citing works

Scaffolds are ‘active’ regulators of signaling modules

Alexa, A., Varga, J. M., & Reményi, A. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07867.x · Cited by 24 · see citing works

Multiplexed imaging of intracellular protein networks

Grecco, H. E., Imtiaz, S., & Zamir, E. (2016) · Cytometry Part A · doi:10.1002/cyto.a.22876 · Cited by 23 · see citing works

Compartmentalization of the MAPK scaffold protein KSR1 modulates synaptic plasticity in hippocampal neurons

Canal, F., Palygin, O., Pankratov, Y., Corrêa, S. A. L., & Müller, J. (2011) · The FASEB Journal · doi:10.1096/fj.10-173153 · Cited by 24 · see citing works

The Potential of Vitamin D-Regulated Intracellular Signaling Pathways as Targets for Myeloid Leukemia Therapy

Gocek, E., & Studzinski, G. P. (2015) · Journal of Clinical Medicine · doi:10.3390/jcm4040504 · Cited by 22 · see citing works

JCPyV-Induced MAPK Signaling Activates Transcription Factors during Infection

DuShane, J. K., Mayberry, C. L., Wilczek, M. P., Nichols, S. L., & Maginnis, M. S. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20194779 · Cited by 21 · see citing works

Oncogenic RAS-Induced Perinuclear Signaling Complexes Requiring KSR1 Regulate Signal Transmission to Downstream Targets

Basu, S. K., Lee, S., Salotti, J., Basu, S., Sakchaisri, K., Xiao, Z., Walia, V., Westlake, C. J., Morrison, D. K., & Johnson, P. F. (2017) · Cancer Research · doi:10.1158/0008-5472.can-17-2353 · Cited by 21 · see citing works

KSR1- and ERK-dependent translational regulation of the epithelial-to-mesenchymal transition

Rao, C., Frodyma, D. E., Southekal, S., Svoboda, R. A., Black, A. R., Guda, C., Mizutani, T., Clevers, H. C., Johnson, K. R., Fisher, K. W., et al. (2021) · eLife · doi:10.7554/elife.66608 · Cited by 20 · see citing works

Ras Family Small GTPase-Mediated Neuroprotective Signaling in Stroke

Shi, G., Andres, D., & Cai, W. (2011) · Central Nervous System Agents in Medicinal Chemistry · doi:10.2174/187152411796011349 · Cited by 19 · see citing works

Ras Mitogen-activated Protein Kinase Signaling and Kinase Suppressor of Ras as Therapeutic Targets for Hepatocellular Carcinoma

Moon, H., & Ro, S. (2021) · Journal of Liver Cancer · doi:10.17998/jlc.21.1.1 · Cited by 17 · see citing works

Shoc2-tranduced ERK1/2 motility signals — Novel insights from functional genomics

Jeoung, M., Jang, E. R., Liu, J., Wang, C., Rouchka, E. C., Li, X., & Galperin, E. (2016) · Cellular Signalling · doi:10.1016/j.cellsig.2016.02.005 · Cited by 18 · see citing works

The scaffold protein KSR1, a novel therapeutic target for the treatment of Merlin-deficient tumors

Zhou, L., Rimmer, J. L., Ammoun, S., Müller, J., Lasonder, E., Sharma, V., Ercolano, E., Hilton, D. A., Taiwo, I., Barczyk, M., et al. (2015) · Oncogene · doi:10.1038/onc.2015.404 · Cited by 18 · see citing works

Bidirectional alteration of Cav-1 expression is associated with mitogenic conversion of its function in gastric tumor progression

Ryu, B., Lee, M.-G., Kim, N.-H., Lee, K. Y., Oh, S.-J., Moon, J.-R., Kim, H. J., & Chi, S.-G. (2017) · BMC Cancer · doi:10.1186/s12885-017-3770-y · Cited by 16 · see citing works

Shaping Brassinosteroid Signaling through Scaffold Proteins

Guo, B., Kim, E., Zhu, Y., Wang, K., & Russinova, E. (2024) · Plant and Cell Physiology · doi:10.1093/pcp/pcae040 · Cited by 16 · see citing works

Regulation of Glucose Homeostasis by KSR1 and MARK2

Klutho, P. J., Costanzo-Garvey, D. L., & Lewis, R. E. (2011) · PLoS ONE · doi:10.1371/journal.pone.0029304 · Cited by 15 · see citing works

BRAF activates and physically interacts with PAK to regulate cell motility

McCarty, S., Saji, M., Zhang, X., Knippler, C. M., Kirschner, L. S., Fernández, S., & Ringel, M. D. (2014) · Endocrine Related Cancer · doi:10.1530/erc-14-0424 · Cited by 15 · see citing works

Scaffold coupling: ERK activation by trans-phosphorylation across different scaffold protein species

Martín-Vega, A., Ruiz-Peinado, L., García‐Gómez, R., Herrero, A., de la Fuente‐Vivas, D., Parvathaneni, S., Caloto, R., Morante, M., von Kriegsheim, A., Bustelo, X. R., et al. (2023) · Science Advances · doi:10.1126/sciadv.add7969 · Cited by 14 · see citing works

Spatiotemporal Modulation of ERK Activation by GPCRs

Waturuocha, U. W., Jain, R., Asthana, S., & Saini, D. K. (2018) · International review of cytology · doi:10.1016/bs.ircmb.2018.02.004 · Cited by 13 · see citing works

ScaPD: a database for human scaffold proteins

Han, X., Wang, J., Wang, J., Liu, S., Hu, J., Zhu, H., & Qian, J. X. (2017) · BMC Bioinformatics · doi:10.1186/s12859-017-1806-6 · Cited by 13 · see citing works

Cytoplasmic Protein Serine/Threonine Kinases

Thiriet, M. (2012) · Biomathematical and biomechanical modeling of the circulatory and ventilatory systems · doi:10.1007/978-1-4614-4370-4_5 · Cited by 11 · see citing works

Dissection of MAPK signaling specificity through protein engineering in a developmental context

Wengier, D. L., Lampard, G. R., & Bergmann, D. C. (2018) · BMC Plant Biology · doi:10.1186/s12870-018-1274-9 · Cited by 12 · see citing works

Limited Proteolysis Combined with Stable Isotope Labeling Reveals Conformational Changes in Protein (Pseudo)kinases upon Binding Small Molecules

Michele, M. D., Stes, E., Vandermarliere, E., Arora, R., Astorga‐Wells, J., Vandenbussche, J., van Heerde, E., Zubarev, R. A., Bonnet, P., Linders, J. T. M., et al. (2015) · Journal of Proteome Research · doi:10.1021/acs.jproteome.5b00282 · Cited by 11 · see citing works

KSR Plays CRAF-ty

Shi, F., & Lemmon, M. A. (2011) · Science · doi:10.1126/science.1208063 · Cited by 11 · see citing works

Signaling Lipids

Thiriet, M. (2012) · Biomathematical and biomechanical modeling of the circulatory and ventilatory systems · doi:10.1007/978-1-4614-4370-4_2 · Cited by 9 · see citing works

KSR1 Mediates Small Cell Lung Carcinoma Tumor Initiation and Cisplatin Resistance

Chatterjee, D., Svoboda, R. A., Huisman, D. H., Drapkin, B. J., Vieira, H. M., Rao, C., Askew, J. W., Fisher, K. W., & Lewis, R. E. (2025) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-24-0652 · Cited by 10 · see citing works

Stabilization of C-RAF:KSR1 complex by DiRas3 reduces availability of C-RAF for dimerization with B-RAF

Baljuls, A., Dobrzyński, M., Rauch, J., Rauch, N., & Kölch, W. (2016) · Cellular Signalling · doi:10.1016/j.cellsig.2016.06.019 · Cited by 10 · see citing works

KSR is a scaffold required for activation of the ERK/MAPK module

Roy, F., Laberge, G., Douziech, M., Ferland-McCollough, D., & Therrien, M. (2002) · Genes & Development · doi:10.1101/gad.962902 · Cited by 217 · see citing works

KSR Regulation of the Raf‐MEK‐ERK Cascade

Ritt, D. A., Daar, I. O., & Morrison, D. K. (2006) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(05)07019-9 · Cited by 21 · see citing works

CK2 Is a Component of the KSR1 Scaffold Complex that Contributes to Raf Kinase Activation

Ritt, D. A., Zhou, M., Conrads, T. P., Veenstra, T. D., Copeland, T. D., & Morrison, D. K. (2006) · Current Biology · doi:10.1016/j.cub.2006.11.061 · Cited by 100 · see citing works

VRK2 anchors KSR1-MEK1 to endoplasmic reticulum forming a macromolecular complex that compartmentalizes MAPK signaling

Fernández, I. F., Perez‐Rivas, L. G., Blanco, S., Castillo-Dominguez, A. A., Lozano, J., & Lazo, P. A. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1056-8 · Cited by 47 · see citing works

Kinase Suppressor of Ras (KSR) Is a Scaffold Which Facilitates Mitogen-Activated Protein Kinase Activation In Vivo

Nguyen, A., Burack, R., Stock, J. L., Kortum, R. L., Chaika, O. V., Afkarian, M., Muller, W. J., MURPHY, K. M. M., Morrison, D. K., Lewis, R. E., et al. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.9.3035-3045.2002 · Cited by 269 · see citing works