Mechanism for the activation of the anaplastic lymphoma kinase receptor

Reshetnyak, Andrey V.; Rossi, Paolo; Myasnikov, Alexander G.; Sowaileh, Munia; Mohanty, Jyotidarsini; Nourse, Amanda; Miller, Darcie J.; Lax, Irit; Schlessinger, Joseph; Kalodimos, Charalampos G.

doi:10.1038/s41586-021-04140-8

Mechanism for the activation of the anaplastic lymphoma kinase receptor

Journal Article · 01 November 2021 · Nature

DOI:https://doi.org/10.1038/s41586-021-04140-8· OSTI ID:1841226

Reshetnyak, Andrey V.; Rossi, Paolo; Myasnikov, Alexander G.; Sowaileh, Munia; Mohanty, Jyotidarsini; Nourse, Amanda; Miller, Darcie J.; Lax, Irit; Schlessinger, Joseph; Kalodimos, Charalampos G.

Research Organization:: Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS)

Sponsoring Organization:: DOE - Office Of Science; National Institutes of Health (NIH); OTHER

OSTI ID:: 1841226

Journal Information:: Nature, Vol. 600

Country of Publication:: United States

Language:: ENGLISH

References (55)

Fusion of a Kinase Gene, ALK , to a Nucleolar Protein Gene, NPM , in Non-Hodgkin's Lymphoma Morris, Stephan W.; Kirstein, Mark N.; Valentine, Marcus B. Science, Vol. 263, Issue 5151 https://doi.org/10.1126/science.8122112	journal	March 1994
Identification of ALK in Thinness Orthofer, Michael; Valsesia, Armand; Mägi, Reedik Cell, Vol. 181, Issue 6 https://doi.org/10.1016/j.cell.2020.04.034	journal	June 2020
Mechanistic insight into ALK receptor tyrosine kinase in human cancer biology Hallberg, Bengt; Palmer, Ruth H. Nature Reviews Cancer, Vol. 13, Issue 10 https://doi.org/10.1038/nrc3580	journal	September 2013
Oncogenic mutations of ALK kinase in neuroblastoma Chen, Yuyan; Takita, Junko; Choi, Young Lim Nature, Vol. 455, Issue 7215 https://doi.org/10.1038/nature07399	journal	October 2008
Activating mutations in ALK provide a therapeutic target in neuroblastoma George, Rani E.; Sanda, Takaomi; Hanna, Megan Nature, Vol. 455, Issue 7215 https://doi.org/10.1038/nature07397	journal	October 2008
Somatic and germline activating mutations of the ALK kinase receptor in neuroblastoma Janoueix-Lerosey, Isabelle; Lequin, Delphine; Brugières, Laurence Nature, Vol. 455, Issue 7215 https://doi.org/10.1038/nature07398	journal	October 2008
Identification of ALK as a major familial neuroblastoma predisposition gene Mossé, Yaël P.; Laudenslager, Marci; Longo, Luca Nature, Vol. 455, Issue 7215 https://doi.org/10.1038/nature07261	journal	August 2008
ALK, the chromosome 2 gene locus altered by the t(2;5) in non-Hodgkin's lymphoma, encodes a novel neural receptor tyrosine kinase that is highly related to leukocyte tyrosine kinase (LTK) Morris, Stephan W.; Naeve, Clayton; Mathew, Prasad Oncogene, Vol. 14, Issue 18 https://doi.org/10.1038/sj.onc.1201062	journal	May 1997
Cell Signaling by Receptor Tyrosine Kinases Lemmon, Mark A.; Schlessinger, Joseph Cell, Vol. 141, Issue 7 https://doi.org/10.1016/j.cell.2010.06.011	journal	June 2010
Deorphanization of the human leukocyte tyrosine kinase (LTK) receptor by a signaling screen of the extracellular proteome Zhang, H.; Pao, L. I.; Zhou, A. Proceedings of the National Academy of Sciences, Vol. 111, Issue 44 https://doi.org/10.1073/pnas.1412009111	journal	October 2014
FAM150A and FAM150B are activating ligands for anaplastic lymphoma kinase Guan, Jikui; Umapathy, Ganesh; Yamazaki, Yasuo eLife, Vol. 4 https://doi.org/10.7554/eLife.09811	journal	September 2015
Augmentor α and β (FAM150) are ligands of the receptor tyrosine kinases ALK and LTK: Hierarchy and specificity of ligand–receptor interactions Reshetnyak, Andrey V.; Murray, Phillip B.; Shi, Xiarong Proceedings of the National Academy of Sciences, Vol. 112, Issue 52 https://doi.org/10.1073/pnas.1520099112	journal	November 2015
Alk and Ltk ligands are essential for iridophore development in zebrafish mediated by the receptor tyrosine kinase Ltk Mo, Elizabeth S.; Cheng, Qianni; Reshetnyak, Andrey V. Proceedings of the National Academy of Sciences, Vol. 114, Issue 45 https://doi.org/10.1073/pnas.1710254114	journal	October 2017
ALKALs are in vivo ligands for ALK family receptor tyrosine kinases in the neural crest and derived cells Fadeev, Andrey; Mendoza-Garcia, Patricia; Irion, Uwe Proceedings of the National Academy of Sciences, Vol. 115, Issue 4 https://doi.org/10.1073/pnas.1719137115	journal	January 2018
Identification of a biologically active fragment of ALK and LTK-Ligand 2 (augmentor-α) Reshetnyak, Andrey V.; Mohanty, Jyotidarsini; Tomé, Francisco Proceedings of the National Academy of Sciences, Vol. 115, Issue 33 https://doi.org/10.1073/pnas.1807881115	journal	July 2018
Structure of Polyglycine II Crick, F. H. C.; Rich, Alexander Nature, Vol. 176, Issue 4486 https://doi.org/10.1038/176780a0	journal	October 1955
A rare polyglycine type II-like helix motif in naturally occurring proteins Warkentin, Eberhard; Weidenweber, Sina; Schühle, Karola Proteins: Structure, Function, and Bioinformatics, Vol. 85, Issue 11 https://doi.org/10.1002/prot.25355	journal	August 2017
A crucial role for the Anaplastic lymphoma kinase receptor tyrosine kinase in gut development in Drosophila melanogaster Lorén, Christina E.; Englund, Camilla; Grabbe, Caroline EMBO reports, Vol. 4, Issue 8 https://doi.org/10.1038/sj.embor.embor897	journal	July 2003
Highly accurate protein structure prediction with AlphaFold Jumper, John; Evans, Richard; Pritzel, Alexander Nature https://doi.org/10.1038/s41586-021-03819-2	journal	July 2021
Conformational Coupling across the Plasma Membrane in Activation of the EGF Receptor Endres, Nicholas F.; Das, Rahul; Smith, Adam W. Cell, Vol. 152, Issue 3 https://doi.org/10.1016/j.cell.2012.12.032	journal	January 2013
Targeting Tyro3, Axl and MerTK (TAM receptors): implications for macrophages in the tumor microenvironment Myers, Kayla V.; Amend, Sarah R.; Pienta, Kenneth J. Molecular Cancer, Vol. 18, Issue 1 https://doi.org/10.1186/s12943-019-1022-2	journal	May 2019
Interaction between proteins localized in membranes. Grasberger, B.; Minton, A. P.; DeLisi, C. Proceedings of the National Academy of Sciences, Vol. 83, Issue 17 https://doi.org/10.1073/pnas.83.17.6258	journal	September 1986
A structure-based model for ligand binding and dimerization of EGF receptors Klein, P.; Mattoon, D.; Lemmon, M. A. Proceedings of the National Academy of Sciences, Vol. 101, Issue 4 https://doi.org/10.1073/pnas.0307285101	journal	January 2004
The origin of protein interactions and allostery in colocalization Kuriyan, John; Eisenberg, David Nature, Vol. 450, Issue 7172 https://doi.org/10.1038/nature06524	journal	December 2007
More than the sum of the parts: Toward full‐length receptor tyrosine kinase structures Diwanji, Devan; Thaker, Tarjani; Jura, Natalia IUBMB Life, Vol. 71, Issue 6 https://doi.org/10.1002/iub.2060	journal	May 2019
Heparin is an activating ligand of the orphan receptor tyrosine kinase ALK Murray, Phillip B.; Lax, Irit; Reshetnyak, Andrey Science Signaling, Vol. 8, Issue 360 https://doi.org/10.1126/scisignal.2005916	journal	January 2015
Structural basis for ligand reception by anaplastic lymphoma kinase Li, Tongqing; Stayrook, Steven E.; Tsutsui, Yuko Nature, Vol. 600, Issue 7887 https://doi.org/10.1038/s41586-021-04141-7	journal	November 2021
Atomic Structures of the Human Immunophilin FKBP-12 Complexes with FK506 and Rapamycin Van Duyne, Gregory D.; Standaert, Robert F.; Karplus, P. Andrew Journal of Molecular Biology, Vol. 229, Issue 1 https://doi.org/10.1006/jmbi.1993.1012	journal	January 1993
Exploiting E. coli auxotrophs for leucine, valine, and threonine specific methyl labeling of large proteins for NMR applications Monneau, Yoan R.; Ishida, Yojiro; Rossi, Paolo Journal of Biomolecular NMR, Vol. 65, Issue 2 https://doi.org/10.1007/s10858-016-0041-1	journal	June 2016
[20] Processing of X-ray diffraction data collected in oscillation mode Otwinowski, Zbyszek; Minor, Wladek Macromolecular Crystallography Part A, 307-326 https://doi.org/10.1016/S0076-6879(97)76066-X	book	January 1997
Decision-making in structure solution using Bayesian estimates of map quality: the PHENIX AutoSol wizard Terwilliger, Thomas C.; Adams, Paul D.; Read, Randy J. Acta Crystallographica Section D Biological Crystallography, Vol. 65, Issue 6 https://doi.org/10.1107/S0907444909012098	journal	May 2009
Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix Liebschner, Dorothee; Afonine, Pavel V.; Baker, Matthew L. Acta Crystallographica Section D Structural Biology, Vol. 75, Issue 10 https://doi.org/10.1107/S2059798319011471	journal	October 2019
Features and development of Coot Emsley, P.; Lohkamp, B.; Scott, W. G. Acta Crystallographica Section D Biological Crystallography, Vol. 66, Issue 4 https://doi.org/10.1107/S0907444910007493	journal	March 2010
NMRPipe: A multidimensional spectral processing system based on UNIX pipes Delaglio, Frank; Grzesiek, Stephan; Vuister, GeertenW. Journal of Biomolecular NMR, Vol. 6, Issue 3 https://doi.org/10.1007/BF00197809	journal	November 1995
NMRFAM-SPARKY: enhanced software for biomolecular NMR spectroscopy Lee, Woonghee; Tonelli, Marco; Markley, John L. Bioinformatics, Vol. 31, Issue 8 https://doi.org/10.1093/bioinformatics/btu830	journal	December 2014
Determination of solution structures of proteins up to 40 kDa using CS-Rosetta with sparse NMR data from deuterated samples Lange, O. F.; Rossi, P.; Sgourakis, N. G. Proceedings of the National Academy of Sciences, Vol. 109, Issue 27 https://doi.org/10.1073/pnas.1203013109	journal	June 2012
Protein backbone and sidechain torsion angles predicted from NMR chemical shifts using artificial neural networks Shen, Yang; Bax, Ad Journal of Biomolecular NMR, Vol. 56, Issue 3 https://doi.org/10.1007/s10858-013-9741-y	journal	June 2013
15N and 13C- SOFAST-HMQC editing enhances 3D-NOESY sensitivity in highly deuterated, selectively [1H,13C]-labeled proteins Rossi, Paolo; Xia, Youlin; Khanra, Nandish Journal of Biomolecular NMR, Vol. 66, Issue 4 https://doi.org/10.1007/s10858-016-0074-5	journal	November 2016
Automatic methyl assignment in large proteins by the MAGIC algorithm Monneau, Yoan R.; Rossi, Paolo; Bhaumik, Anusarka Journal of Biomolecular NMR, Vol. 69, Issue 4 https://doi.org/10.1007/s10858-017-0149-y	journal	November 2017
Refinement of protein structures in explicit solvent Linge, Jens P.; Williams, Mark A.; Spronk, Christian A. E. M. Proteins: Structure, Function, and Bioinformatics, Vol. 50, Issue 3 https://doi.org/10.1002/prot.10299	journal	January 2003
Version 1.2 of the Crystallography and NMR system Brunger, Axel T. Nature Protocols, Vol. 2, Issue 11 https://doi.org/10.1038/nprot.2007.406	journal	October 2007
Evaluating protein structures determined by structural genomics consortia Bhattacharya, Aneerban; Tejero, Roberto; Montelione, Gaetano T. Proteins: Structure, Function, and Bioinformatics, Vol. 66, Issue 4 https://doi.org/10.1002/prot.21165	journal	December 2006
PDBStat: a universal restraint converter and restraint analysis software package for protein NMR Tejero, Roberto; Snyder, David; Mao, Binchen Journal of Biomolecular NMR, Vol. 56, Issue 4 https://doi.org/10.1007/s10858-013-9753-7	journal	July 2013
Automated electron microscope tomography using robust prediction of specimen movements Mastronarde, David N. Journal of Structural Biology, Vol. 152, Issue 1 https://doi.org/10.1016/j.jsb.2005.07.007	journal	October 2005
MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy Zheng, Shawn Q.; Palovcak, Eugene; Armache, Jean-Paul Nature Methods, Vol. 14, Issue 4 https://doi.org/10.1038/nmeth.4193	journal	February 2017
New tools for automated high-resolution cryo-EM structure determination in RELION-3 Zivanov, Jasenko; Nakane, Takanori; Forsberg, Björn O. eLife, Vol. 7 https://doi.org/10.7554/eLife.42166	journal	November 2018
cisTEM, user-friendly software for single-particle image processing Grant, Timothy; Rohou, Alexis; Grigorieff, Nikolaus eLife, Vol. 7 https://doi.org/10.7554/eLife.35383	journal	March 2018
cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination Punjani, Ali; Rubinstein, John L.; Fleet, David J. Nature Methods, Vol. 14, Issue 3 https://doi.org/10.1038/nmeth.4169	journal	February 2017
UCSF Chimera?A visualization system for exploratory research and analysis Pettersen, Eric F.; Goddard, Thomas D.; Huang, Conrad C. Journal of Computational Chemistry, Vol. 25, Issue 13 https://doi.org/10.1002/jcc.20084	journal	January 2004
Real-space refinement in PHENIX for cryo-EM and crystallography Afonine, Pavel V.; Poon, Billy K.; Read, Randy J. Acta Crystallographica Section D Structural Biology, Vol. 74, Issue 6 https://doi.org/10.1107/S2059798318006551	journal	May 2018
MolProbity: More and better reference data for improved all-atom structure validation: PROTEIN SCIENCE.ORG Williams, Christopher J.; Headd, Jeffrey J.; Moriarty, Nigel W. Protein Science, Vol. 27, Issue 1 https://doi.org/10.1002/pro.3330	journal	November 2017
Analysis of the Binding of the Fab Fragment of Monoclonal Antibody NC10 to Influenza Virus N9 Neuraminidase from Tern and Whale Using the BIAcore Biosensor: Effect of Immobilization Level and Flow Rate on Kinetic Analysis Kortt, Alexander A.; Nice, Edouard; Gruen, L. Clem Analytical Biochemistry, Vol. 273, Issue 1 https://doi.org/10.1006/abio.1999.4183	journal	August 1999
Overview of Current Methods in Sedimentation Velocity and Sedimentation Equilibrium Analytical Ultracentrifugation Zhao, Huaying; Brautigam, Chad A.; Ghirlando, Rodolfo Current Protocols in Protein Science, Vol. 71, Issue 1 https://doi.org/10.1002/0471140864.ps2012s71	journal	February 2013
Size-Distribution Analysis of Macromolecules by Sedimentation Velocity Ultracentrifugation and Lamm Equation Modeling Schuck, Peter Biophysical Journal, Vol. 78, Issue 3 https://doi.org/10.1016/S0006-3495(00)76713-0	journal	March 2000
Calculations and Publication-Quality Illustrations for Analytical Ultracentrifugation Data Brautigam, Chad A. Methods in Enzymology https://doi.org/10.1016/bs.mie.2015.05.001	book	January 2015

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