Publications

 

• 2023

  Titze S., Kümmel D. (2023)
  The difference is in the details: structural and mechanistic variations in the LAMTOR-Gtr/Rag module.
  Structure, accepted

  Füsser F.T, Wollenhaupt J., Weiss M.S., Kümmel D., Koch O. (2023)
  Novell starting points for fragment-based drug design in Mycobacterial Thioredoxin reductase using crystallographic fragment screening.
  Acta Crystallogr D Struct Biol, accepted

  Borchers A.C., Janz M., Schäfer J.H., Moeller A., Kümmel D., Paululat A., Ungermann C. Langemeyer L. (2023)
  Regulatory sites in the Mon1-Ccz1 complex control Rab5 to Rab7 transition and endosome maturation.
  Proc Natl Acad Sci USA, 120: e2303750120  doi: 10.1073/pnas.2303750120

  Mhaindarkar V.P., Rasche R., Kümmel D., Rudolph M.G., Klostermeier D. (2023)
  Structure of reverse gyrase with a minimal latch that supports ATP-dependent positive supercoiling without specific interactions with the topoisomerase domain.
  Acta Crystallogr D Struct Biol, 79: 498-507 doi: 10.1107/S2059798323002565

  Wilmes S., Kümmel D. (2023)
  Insights into the role of the membranes in Rab GTPase regulation.
  Curr Opin Cell Biol, 83: 10277 doi: 10.1016/j.ceb.2023.102177
  
  Pasch T., Schröder A., Kattelmann S., Eisenstein M., Pietrokovski S., Kümmel D., Mootz H.D. (2023)
  Structural and biochemical analysis of a novel atypically split intein reveals a conserved histidine specific to cysteine-less inteins.
  Chem Sci, ePub, doi: 10.1039/D3SC01200J
  
  Herrmann E., Schäfer J.H., Wilmes S., Ungermann C., Moeller A., Kümmel D. (2023)
  Structure of the metazoan Rab7 GEF complex Mon1-Ccz1-Bulli.
  Proc Natl Acad Sci USA, 120: e2301908120, doi: 10.1073/pnas.2301908120
  
  Herrmann E., Langemeyer L., Auffarth K. Ungermann C., Kümmel D. (2023)
  Targeting of the Mon1-Ccz1 Rab GEF to distinct organelles by a synergistic protein and lipid code.
  J Biol Chem 299:102915, doi: 10.1016/j.jbc.2023.102915

   

• 2022

  Kümmel D., Herrmann E., Langemeyer L., Ungermann C. (2022)
  Molecular insights into endolysosomal microcompartment formation and maintenance.
  Biol Chem, 404:441-454 doi: 10.1515/hsz-2022-0294

  Shvarev D., Schoppe J., König C., Perz A., Fuellbrunn N, Kiontke S., Langemeyer L., Januliene D., Schnelle K., Kümmel D., Fröhlich F., Möller A., Ungermann C. (2022)
  Structure of the lysosomal membrane fusion machinery.
  Elife 11,  doi: 10.7554/eLife.80901
  
  Gollwitzer P., Grützmacher N., Wilhelm S., Kümmel D., Demetriades C. (2022)
  A Rag GTPase Dimer Code Defines the Regulation of mTORC1 by Amino Acids.
  Nat Cell Biol, 24:1394-1406, doi: 10.1038/s41556-022-00976-y

  Marchetti G.M., Füsser F., Singh R.K., Brummel M., Koch O., Kümmel D., §Hippler M. (2022)
  Structural analysis revealed a novel conformation of the NTRC reductase domain from Chlamydomonas reinhardtii.
  J Struct Biol, 214, doi: 10.1016/j.jsb.2021.107829

  Peters A., Herrmann E., Cornelissen N.V., Klöcker N., Kümmel D., Rentmeister A. (2022)
  Visible-light Removable Photocaging Groups Accepted by MjMAT Variant: Structural Basis and Compatibility with DNA and RNA Methyltransferases.
  Chembiochem, 23, doi: 10.1002/cbic.202100437

  Klink B.U., Herrmann E., Antoni C., Langemeyer L., Kiontke S., Gatsogiannis C., Ungermann C., Raunser S., Kümmel D. (2022)
  Structure of the Mon1-Ccz1 complex reveals molecular basis of membrane binding for Rab7 activation.
  Proc Natl Acad Sci USA, 119, doi: 10.1073/pnas.2121494119

• 2021

  Fitzian K., Brückner, A., Brohée, L., Zech, R., Antoni, C., Kiontke, S., Gasper, R., Linard Matos, A.L., Beel S., Wilhelm S., Gerke V., Ungermann C., Nellist M., Raunser S., Demetriades C., Oeckinghaus A., Kümmel D. (2021)
  TSC1 binding to lysosomal PIPs is required for TSC complex translocation and mTORC1 regulation
  Mol Cell, doi:10.1016/j.molcel.2021.04.019

  Hoffmann S., Terhorst T.M.E., Singh R.K., Kümmel D., Pietrokovski S., Mootz H.D. (2021)
  Biochemical and structural characterization of an unusual and naturally split class 3 intein.
  Chembiochem, 22, 364-373. doi:10.1002/cbic.202000509

  Michailidou F., Klöcker N., Cornelissen N., Singh R.K., Peters A., Ovcharenko A., Kümmel D., Rentmeister A. (2021)
  Engineered SAM synthetases for enzymatic generation of AdoMet analogs with photocaging groups and reversible DNA modification in cascade reactions.
  Angew Chem Int Ed Engl, 60, 480-485. doi:10.1002%2Fanie.202012623

• 2020

  Lynagh T., Kiontke S., Meyhoff-Madsen M., Gless B.H., Johannesen J., Kattelmann S., Christiansen A., Dufva M., Laustsen A.H., Devkota K., Olsen C.A., Kümmel D., Pless S.A., Lohse B. (2020)
  Peptide Inhibitors of the ?-Cobratoxin-Nicotinic Acetylcholine Receptor Interaction.
  J Med Chem, 63, 13709?13718. doi:10.1021/acs.jmedchem.0c01202

  Hansmann P., Brückner A., Kiontke S., Berkenfeld B., Seebohm G., Brouillard P., Vikkula M., Jansen F.E., Nellist M., Oeckinghaus A., Kümmel D. (2020).
  Structural analysis of the TSC2 GAP domain: mechanistic insight into catalysis and pathogenic mutations.
  Structure, 28: 933-942. doi:10.1016/j.str.2020.05.008

  Escobar-Hoyos L.F., Penson A., Kannan R., Cho H ., Pan C-H., Singh R.K., Hobbs G.A., Luo, R, Lecomte N., Babu S., Pan F.C., Alonso-Curbelo D., Morris J.P., Askan G., Grbovic-Huezo O., Ogrodowski P., Bermeo J., Saglimbeni J., Cruz C.D., Ho Y-J., Lawrence S.A., Melchor J.P., Goda G.A., Bai K., Pastore A., Hogg S.J., Raghavan S., Bailey P., Chang D.K., Biankin A., Shroyer K.R., Wolpin B.M., Aguirre A.J., Ventura A., Taylor B., Der C.J., Dominguez D., Kümmel D., Oeckinghaus A., Lowe S., Bradley R. Abdel-Wahab O., Leach S.D. (2020)
  Altered RNA splicing by mutant p53 activates oncogenic RAS signaling in pancreatic cancer.
  Cancer Cell, 38: 198-211. doi: 10.1016/j.ccell.2020.05.010

  Langemeyer L., Borchers A.-C., Herrmann E., Füllbrunn N., Han Y., Perz A., Auffarth K., Kümmel D., Ungermann C. (2020).
  A conserved and regulated mechanism drives endosomal Rab transition.
  Elife 9: e56090   doi: 10.7554/eLife.56090

  Dufner Almeida L.G., Nanhoe S., Zonta, A., Hosseinzadeh M., Kom-Gortat R., Elfferich P., Schaaf G., Kenter A., Kümmel D., Migone N., Povey S., Ekong R., Nellist M. (2020).
  Comparison of the functional and structural characteristics of rare TSC2 variants with clinical and genetic findings.
  Hum. Mutat. 41: 759-773  doi: 10.1002/humu.23963

• 2019

  Ungermann C., Kümmel D. (2019)
  Structure of membrane tethers and their role in fusion.
  Traffic, 20:479-490  doi: 10.1111/tra.12655

• 2018

  Lürick A., Kümmel D., and Ungermann C. (2018)
  Multisubunit tethers in membrane fusion.
  Curr. Biol. 28, R417-R420.

  Gao J., Langemeyer L., Kümmel D., Reggiori F., Ungermann C. (2018)
  Molecular mechanism to target the endosomal Mon1-Ccz1 GEF complex to the pre-autophagosomal structure.
  Elife e31145.

  Fernández M.L., Quartino P.Y., Arce-Bejarano R., Fernández J., Camacho L.F., Gutiérrez J.M., Kümmel D., Fidelio G., Lomonte B. (2018)
  Intravascular hemolysis induced by phospholipases A2 from the venom of the Eastern coral snake, Micrurus fulvius: functional profiles of hemolytic and non-hemolytic isoforms.
  Toxicol Lett. 286: 39-47

  Langemeyer L., Perz A., Kümmel D., Ungermann C. (2018)
  A Guanine nucleotide exchange factor (GEF) limits Rab GTPase driven membrane fusion.
  J. Biol. Chem. 293: 731-739.

• 2017

  Hellinger R., Thell K., Vasileva M., Muhammad T., Gunasekera S., Kümmel D., Göransson U., Becker C.W., Gruber C.W. (2017)
  Chemical Proteomics for Target Discovery of Head-to-Tail Cyclized Mini-Proteins.
  Front Chem. 5, 73

  Kiontke, S., Langemeyer, L., Kuhlee, A., Schuback, S., Raunser, S., Ungermann, C., Kümmel, D. (2017)
  Architecture and mechanism of the late endosomal Rab7-like Ypt7 guanine nucleotide exchange factor complex Mon1-Ccz1.
  Nat Commun, 8: 10.1038/ncomms14034.

• 2016

  Zech, R., Kiontke, S., Mueller, U., Oeckinghaus, A., Kümmel, D. (2016)
  Structure of the Tuberous Sclerosis Complex 2 (TSC2) N-terminus Provides Insight into Complex Assembly and Tuberous Sclerosis Pathogenesis.
  J Biol Chem, 291: 20008-20020

• 2015

  Krishnakumar S.S., Li F., Coleman J., Schauder C.M., Kümmel D., Pincet F., Rothman J.E., Reinisch K.M. (2015)
  Re-visiting the trans insertion model for complexin clamping.
  Elife, e04463

  Lürick, A., Kuhlee, A., Bröcker, C., Kümmel, D., Raunser, S., Ungermann, C. (2015)
  The Habc Domain of the SNARE Vam3 Interacts with the HOPS Tethering Complex to Facilitate Vacuole Fusion.
  J Biol Chem, 290: 5405-5413.

• 2014

  Behrmann, H., Lürick, A., Kuhlee, A., Balderhaar, H.K., Bröcker, C., Kümmel D, Engelbrecht-Vandre, S., Gohlke, U., Raunser, S., Heinemann, U., Ungermann, C. (2014)
  Structural identification of the Vps18 β-propeller reveals a critical role in the HOPS complex stability and function.
  J Biol Chem, 289: 33503-33512

  Kümmel, D., Ungermann, C. (2014)
  Principles of membrane tethering and fusion in endosome and lysosome biogenesis.
  Curr Opin Cell Biol, 29C: 61-66

  Cho, R.W., Kümmel, D., Li, F., Baguley, S.W., Coleman, J., Rothman, J.E., Littleton, J.T. (2014)
  Genetic analysis of the Complexin trans-clamping model for cross-linking SNARE complexes in vivo.
  Proc Natl Acad Sci USA, 111(28):10317-10322

  Li, F., Kümmel, D., Coleman, J., Reinisch, K.M., Rothman, J.E., Pincet, F. (2014)
  A half-zippered SNARE complex represents a functional intermediate in membrane fusion.
  J. Am. Chem. Soc., 136:3456-3464

• 2013

  Krishnakumar, S.S., Kümmel, D., Jones, S.J., Radoff, D.T., Reinisch, K.M., Rothman, J.E. (2013)
  Conformational dynamics of calcium-triggered activation of fusion by synaptotagmin.
  Biophys. J., 105:2507-2516

  Shen, D., Yuan, H., Hutagalung, A., Verma, A., Kümmel, D., Wu, X., Reinisch, K., McNew, J.A., Novick, P. (2013)
  The synaptobrevin homologue Snc2p recruits the exocyst to secretory vesicles by binding to Sec6p.
  J. Cell Biol., 202:509-526