RESEARCH GROUPS
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Groupleader: Thomas Söllner
Thomas Söllner
Regulated Membrane Fusion: Molecular Mechanisms and Machinery
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Research
Our research aims to reveal the mechanisms and machinery underlying intracellular vesicle targeting and regulated membrane fusion. Regulated exocytosis plays a key role in short- and long-range communication and allows complex organisms to react appropriately to various stimuli by releasing mediators, such as hormones, growth factors, and neurotransmitters in a temporally and spatially controlled manner.
We are taking 2 avenues to accomplish our research goals. One is intended to isolate new components, followed by a functional analysis in an environment close to intact cells. The other shall reveal the detailed molecular mechanisms of how distinct components fulfill their functions by making use of a completely reconstituted assay employing SNARE-mediated fusion as an analysis platform. The primary model system for all of these studies is the neuronal synapse, which (like other membrane fusion) steps employs a basic targeting and fusion machinery, but in addition is characterized by its localized vesicle docking and precise regulation. The long-term goal is to reconstitute the sequential series of molecular events, starting with synaptic vesicle recruitment and docking to the active zone, followed by various steps priming the machinery and finally resulting in Ca2+ triggered fusion.
To explore the exact molecular mechanisms by which individual components or functional protein assemblies regulate vesicle fusion, we make use of our previous observation that SNAREs are the minimal machinery for membrane fusion. SNARE proteins, a family of compartmentally specific integral membrane proteins, spontaneously fuse lipid bilayers when reconstituted into liposomes. Addition of regulatory components will affect the fusion kinetics and probability. Basic machinery presently under analysis includes tethering proteins, Rab proteins and their effectors, Sec1/Munc18 proteins, and calcium-sensors. The potentially superimposed fine-tuning underlying synapse modulation during adaptive processes, such as synaptic facilitation and repression, will become another subject of investigation.
Download BZH Report Söllner 2014-2016
Lab Members
Lara Braun
TA
TA
Lab:Room 221
/ Phone: +49 6221 54-5343
Mail:lara.braun@bzh.uni-heidelberg.de
Martina Franke
secretary
secretary
Office:Room 205
/ Phone: +49 6221 54-5340
Mail:martina.franke@bzh.uni-heidelberg.de
Sekr. Söllner 2.OG: 6:45 - 10:00 Uhr
Sekr. Brunner 5. OG: 10:00 - 14:00 Uhr
Sekr. Söllner 2.OG: 14:00 - 15:15 Uhr
Susanne Kreye
TA
TA
Lab:Room 222
/ Phone: +49 6221 54-5344
Mail:susanne.kreye@bzh.uni-heidelberg.de
Silke Malmsheimer
postdoc
postdoc
Lab:Room 221
/ Phone: +49 6221 54-5343
Mail:silke.malmsheimer@bzh.uni-heidelberg.de
Andrea Malsam
TA
TA
Lab:Room 221
/ Phone: +49 6221 54-5343
Mail:andrea.scheutzow@bzh.uni-heidelberg.de
Jörg Malsam
staff scientist
staff scientist
Lab:Room 221
/ Phone: +49 6221 54-5343
Office:Room 201
/ Phone: +49 6221 54-5345
Mail:joerg.malsam@bzh.uni-heidelberg.de
Britta Petersen
PhD student
PhD student
Lab:Room 222
/ Phone: +49 6221 54-5344
Mail:britta.petersen@bzh.uni-heidelberg.de
Kerstin Rink
postdoc
postdoc
Lab:Room 222
/ Phone: +49 6221 54-5344
Mail:kerstin.rink@bzh.uni-heidelberg.de
CV
| 1980 - 1981 | Study of biology at the University of Regensburg |
| 1982 - 1986 | Study of biology at the Ludwig-Maximilians University Munich |
| 1987 - 1991 |
Ph.D. student at the Ludwig-Maximilians University Munich (laboratory of Prof. Dr. Dr. Walter Neupert) |
| 1991 – 1993 |
Post-doctoral fellow at Sloan-Kettering Institute, New York, USA (laboratory of Prof. Dr. James E. Rothman) |
| 1994 - 1997 |
Assistant Laboratory Member at Sloan-Kettering Institute, New York, USA (laboratory of Prof. Dr. James E. Rothman) |
| 1998 - 2004 |
Assistant Member (Assistant Professor) at Sloan-Kettering Institute, New York, USA |
| 2004 - 2005 |
Associate Member (Associate Professor) at Sloan-Kettering Institute, New York, USA |
| since 2005 |
Professor at the University of Heidelberg (BZH) |
| 2016 - 2018 | Director of the Heidelberg University Biochemistry Center (BZH) |
Publications
A short perinuclear amphipathic α-helix in Apq12 promotes nuclear pore complex biogenesis. Open biology, 11(11), 210250. https://doi.org/10.1098/rsob.210250
Zhang, W., Khan, A., Vitale, J., Neuner, A., Rink, K., Lüchtenborg, C., Brügger, B., Söllner, T. H., & Schiebel, E. (2021)
Arrangements of proteins at reconstituted synaptic vesicle fusion sites depend on membrane separation. FEBS Letters, https://doi.org/10.1002/1873-3468.13916
Ginger L, Malsam M, Sonnen A, Morado D, Scheutzow A, Söllner TH, Briggs J (2020)
Complexin suppresses spontaneous exocytosis by capturing the membrane-proximal regions of VAMP2 and SNAP25. Cell Reports, 32. https://doi.org/10.1016/j.celrep.2020.107926 Malsam, J., Bärfuss, S., Trimbuch, T.h, Zarebidaki, F., Sonnen, A., Wild, K., Scheutzow, A., Rohland, L., Mayer, M., Sinning, I., Briggs, J., Rosenmund, C. & Söllner, T.H. (2020)
The Interaction of Munc18-1 Helix 11 and 12 with the Central Region of the VAMP2 SNARE Motif Is Essential for SNARE Templating and Synaptic Transmission. eNeuro, 7(6), ENEURO.0278-20.2020. https://doi.org/10.1523/ENEURO.0278-20.2020 André, T., Classen, J., Brenner, P., Betts, M. J., Dörr, B., Kreye, S., Zuidinga, B., Meijer, M., Russell, R. B., Verhage, M., & Söllner, T. H. (2020)
An Electrostatic Energy Barrier for SNARE-Dependent Spontaneous and Evoked Synaptic Transmission. Cell Rep. 2019 Feb 26;26(9):2340-2352.e5. doi: 10.1016/j.celrep.2019.01.103.
Ruiter M, Kádková A, Scheutzow A, Malsam J, Söllner TH, Sørensen JB (2019)
Synaptic vesicle fusion: today and beyond Nat Struct Mol Biol. Aug;26(8):663-668. doi: 10.1038/s41594-019-0277-z.
Brose N, Brunger A, Cafiso D, Chapman ER, Diao J, Hughson FM, Jackson MB, Jahn R, Lindau M, Ma C, Rizo J, Shin YK, Söllner TH, Tamm L, Yoon TY, Zhang Y (2019)
Tyrosine phosphorylation of Munc18-1 inhibits synaptic transmission by preventin SNARE assembly. The EMBO Journal 37(2): 300-320
Meijer M., Dörr B., Lammertse H., Blithikioti C., van Weering J., Toonen R., Söllner T.H., Verhage M. (2018)
Uncovering the “secret” Lives of Vacuolar Fusion pores in living cells. EMBOJ 37 (19) DOI:10.15252/embj.2018100656.
Söllner, T. Malsam, J. (2018)
Electrostatic anchoring precedes stable membrane attachment of SNAP25/SNAP23 to the plasma membrane. eLife 6:e19394. DOI: 10.7554/eLife.19394
Weber P., Batoulis H., Rink K.M., Dahlhoff S., Pinkwart K., Söllner T.H., Lang T. (2017)
Extension of Helix 12 in Munc18-1 Induces Vesicle Priming. J. Neurosci. 36(26): 6881-6891.
Munch, A.S., Kedar, G.H., van Weering, J.R.T., Vazquez-Sanchez, S., He, E., Andre, T., Braun, T., Söllner, T.H., Verhage, M., Sørensen, J.B. (2016)
Interactions Between SNAP-25 and Synaptotagmin-1 Are Involved in Vesicle Priming, Clamping Spontaneous and Stimulating Evoked Neurotransmission. J Neurosci. 36(47):11865-11880
Schupp M, Malsam J, Ruiter M, Scheutzow A, Wierda KD, Söllner TH, Sørensen JB. (2016)
A post-docking role of synaptotagmin 1-C2B domain bottom residues R398/399 in mouse chromaffin cells. J. Neurosci. 35(42): 14172-14182.
Kedar, G.H., Munch, A.S., van Weering, J.R.T., Malsam, J., Scheutzow, A., de Wit, H., Houy, S., Tawfik, B., Söllner, T.H., Sørensen, J.B., Verhage, M. (2015)
An Extended Helical Conformation in Domain 3a of Munc18-1 Provides a Template for SNARE (Soluble N-Ethylmaleimide-sensitive Factor Attachment Protein Receptor) Complex Assembly. J.Biol.Chem. 289, 9639-9650. https://doi.org/10.1074/jbc.M113.514273 Parisotto, D., Pfau, M., Scheutzow, A., Wild, K., Mayer, M.P., Malsam, J., Sinning, I., & Söllner, T.H. (2014)
SNARE and regulatory proteins induce local membrane protrusions to prime docked vesicles for fast calsium-triggered fusion. EMBO reports 15:3, 308-314.
Bharat, T.A., Malsam, J., Hagen, W.J., Scheutzow, A., Söllner, T.H., Briggs, J.A. (2014)
Complexin arrests a pool of docked vesicles for fast Ca (2+)-dependent release. EMBO J. 31, 3270-3281
Malsam, J., Parisotto, D., Bharat, T.A., Scheutzow A., Krause, J.M., Briggs, J.A., Söllner, T.H. (2012)
SNAREpin Assembly by Munc18-1 Requires Previous Vesicle Docking by Synaptotagmin 1. J. Biol. Chem. 287, 31041-31049
Parisotto, D., Malsam, J., Scheutzow, A., Krause, J.M., Söllner, T.H. (2012)
Organization of SNAREs within the Golgi stack. in ‘The Golgi’, Coldspring Harbor Perspectives in Biology (editors Warren, G. and Rothman, J.) Cold Spring Harbor Laboratory Press
Malsam, J., and Söllner, T.H. (2011)
Resolving the Function of Distinct Munc18-1/SNARE Protein Interaction Modes in a Reconstituted Membrane Fusion. JBC 286 No. 35, 30582-30590.
Schollmeier, Y., Krause, J. M., Kreye, S., Malsam, J., Söllner, T.H. (2011)
Distinct Roles of Myosin Va in Membrane Remodeling and Exocytosis of Secretory Granules. Traffic, 11: 637-650.
Kögel, T., Rudolf, R., Hodneland, E., Hellwig, A., Kuznetsov, S., Seiler, F., Söllner, T.H., Barroso, J., Gerdes, H.-H. (2010)
A role of complexin-lipid interactions in membrane fusion. FEBS letters, 583: 2343-8.
Seiler, F., Malsam, J., Krause, JM., Söllner, T.H. (2009)
The carboxy-terminal domain of complexin I stimulates liposome fusion. Proc. Natl. Acad. Sci. USA, 106: 2001-2006.
Malsam, J., Seiler, F., Schollmeier, Y., Rusu, P., Krause, JM., Söllner, T.H. (2009)
In vitro assays to measure SNARE mediated membrane fusion. Methods in Mol. Biol. 440: 37-50.
Kreye, S., Malsam, J., Söllner, T.H. (2008)
Membrane fusion: SNAREs and regulation. Cell Mol. Life. Sci., 65: 2814-2832.
Malsam, J., Kreye, S., Söllner, T.H. (2008)
Differential localization of isoformic coatomer complexes within the Golgi apparatus. Proc. Natl. Acad. Sci. USA, 104: 4425-30.
Moelleken, J., Malsam, J., Betts, M.J., Movafeghi, A., Reckmann, I., Meissner, I., Hellwig, A., Russell, R.B., Söllner, T.H., Brügger, B., Wieland, F.T. (2007)
Lipid droplets highjack SNAREs. Nat. Cell Biol., 9:1219-20.
Söllner, T.H. (2007)
Membrane trafficking. FEBS Letters, 581: 2075.
Söllner, T.H. (2007)
Dynamic transport of SNARE proteins in the Golgi apparatus. Proc Natl Acad Sci U S A, 102:14647-52.
Cosson, P., Ravazzola, M., Varlamov, O., Söllner, T.H., Di Liberto, M., Volchuk, A., Rothman J.E., Orci, L. (2005)
Crystallographic identification of Ca2+ and Sr2+ coordination sites in synaptotagmin I C2B domain. Protein Science, 13: 2665-2672.
Cheng, Y. Sequeira, S.M., Malinina, L., Tereshko, V., Söllner, T.H., and Patel, D.J. (2004)
Intracellular and viral membrane fusion: a uniting mechanism. Curr. Opinion Cell Biol, 16: 429-435.
Söllner, T.H. (2004)
i-SNAREs, inhibitory SNAREs that fine-tune the specificity of membrane fusion. J. Cell Biol., 164: 79-88.
Varlamov, O., Volchuk, A., Rahimian, V., Doege, C.A. Paumet, F., Eng, W.S, Arango, N.C., Parlati, F., Ravazzola, M., Orci, L, Söllner, T.H., and Rothman, J.E. (2004)
Localization and activity of the SNARE Ykt6 determined by its regulatory domain and palmitoylation. Proc. Natl. Acad. Sci. USA, 101: 4815-1820.
Fukasawa, M., Varlamov, O., Eng, W.S., Söllner, T.H., and Rothman, J.E. (2004)
A SNARE required for retrograde transport to the endoplasmic reticulum. Proc. Natl. Acad. Sci. USA, 100: 9873-9877.
Burri, L., Varlamov, O., Doege, C., Hofman, K., Beilharz, T., Rothman, J.E., Söllner, T.H., and Lithgow, T. (2003)
Fusion of cells by flipped SNAREs. Science, 300: 1745-1749.
Hu, C., Ahmed, M., Melia, T.J., Söllner, T.H., Mayer, T., and Rothman, J.E. (2003)
Regulated exocytosis and SNARE function. Mol. Memb. Biol., 20: 209-220.
Söllner T.H. (2003)
S-nitrosylation of NSF controls membrane trafficking. Cell, 115: 127-129.
Söllner, T.H., and Sequeira, S. (2003)
Calcium-independent stimulation of membrane fusion and SNAREpin formation by synaptotagmin I. The Journal of cell biology, 158(2), 273–282. https://doi.org/10.1083/jcb.200203135 Mahal, L. K., Sequeira, S. M., Gureasko, J. M., & Söllner, T. H. (2002)
Distinct SNARE complexes mediating membrane fusion in Golgi transport based on combinatorial specificity. Proc. Natl. Acad. Sci. USA, 99: 5424-5429.
Parlati, F., Varlamov, O., Paz, K., McNew, J.A., Hurtado, D., Söllner, T.H., and Rothman, J.E. (2002)
Regulation of membrane fusion by the membrane-proximal coil of the t SNARE during zippering of SNAREpins. J. Cell Biol, 158: 929-940. Melia, T.J., Weber, T., McNew, J.A., Fisher, L.E., Johnston, R.J., Parlati, F., Mahal, L.K. Söllner, T.H., and Rothman, J.E. (2002)
A t-SNARE of the endocytic pathway must be activated for fusion. J Cell Biol. 155(6):961-8. Paumet F, Brügger B, Parlati F, McNew JA, Söllner TH, Rothman JE. (2001)
Close is not enough: SNARE-dependent membrane fusion requires an active mechanism that transduces force to membrane anchors. J.Cell Biol., 150: 105-117.
McNew, J.A., Weber, T., Parlati, F., Johnston, R., Melia, T.J., Söllner, T.H., and Rothman, J.E. (2000)
Compartmental specificity of cellular membrane fusion encoded in SNARE proteins. Nature, 407: 153-159.
McNew, J.A., Parlati, F., Fukuda, R., Johnston, R.J., Paz, K., Paumet, F., Söllner, T.H., and Rothman, J.E. (2000)
Functional Architecture of Intracellular t-SNAREs: Membrane Fusion by Isolated SNAREs of the Yeast Vacuole. Nature 407:198-202. Ryouichi Fukuda, James A. McNew, Thomas Weber, Francesco Parlati, Thomas Engel, Walter Nickel, James E. Rothman, and Thomas H. Söllner (2000)
Putative fusogenic activity of NSF is restricted to a lipid mixture whose coalescence is also triggered by other factors. EMBO J. 19(6):1272-8. Brügger B, Nickel W, Weber T, Parlati F, McNew JA, Rothman JE, Söllner T. (2000)
SNAREpins are functionally resistant to disruption by NSF and aSNAP. J.Cell Biol., 149: 1063-1072.
Weber, T., Parlati, F., McNew, J.A., Johnston, R.J., Westermann, B., Söllner, T.H., and Rothman, J.E. (2000)
Topological restriction of SNARE-dependent membrane fusion. Nature, 407: 194-198.
Parlati, F., McNew, J.E., Fukuda, R., Miller, R., Söllner, T.H., and Rothman, J.E. (2000)
Content mixing and membrane integrity during membrane fusion driven by pairing of isolated v-SNAREs and t-SNAREs. Proc. Natl. Acad Sci. U.S.A. 96 :12571-12576. Walter Nickel, Thomas Weber, James A. McNew, Francesco Parlati, Thomas H. Söllner, and James E. Rothman (1999)
Coupling of coat assembly and vesicle budding to packaging of putative cargo receptors. Cell 96, 495-506. M. Bremser, W. Nickel, M. Schweikert, M. Ravazzola, M. Amherd, C.A. Hughes, T.H. Söllner, J. E. Rothman, and F. T. Wieland (1999)
Arrangement of subunits in 20 S particles consisting of NSF, SNAPs, and SNARE complexes. Mol. Cell, 2: 539-548.
Hohl., T.M., Parlati, F., Wimmer, C., Rothman, J.E., Söllner, T.H., and Engelhardt, H. (1998)
SNAREpins: minimal machinery for membrane fusion. Cell, 92: 759-772.
Weber, T., Zemelman, B.V., McNew, J.A., Westermann, B., Gmachl, M., Parlati, F., Söllner, T.H., and Rothman, J.E. (1998)
Throttles and Dampers: controlling the engine of membrane fusion. Science, 276: 1212-1213.
Rothman, J.E., and Söllner, T.H. (1997)
A v-SNARE implicated in intra-Golgi transport. J. Cell. Biol, 133: 507-516
Nagahama, M., Orci, L., Ravazzola, M., Amherdt, M., Lacomis, L., Tempst, P., Rothman, J.E., and Söllner, T.H. (1996)
A rab protein is required for the assembly of SNARE complexes in the docking of transport vesicles. Cell, 78: 937-948.
Søgaard, M., Tani, K., Ye, R.R., Geromanos, S., Tempst, T., Kirchausen, T., Rothman, J.E., and Söllner, T. (1994)
A protein assembly - disassembly pathway that may correspond to sequential steps of synaptic vesicle docking, activation and fusion. Cell, 75: 409-418.
Söllner, T., Bennett, M.K., Whiteheart, S.W., Scheller, R.H., and Rothman, J.E. (1993)
SNAP receptors implicated in vesicle targeting and fusion. Nature 362, 318-324. Söllner, T., Whiteheart, S. W., Brunner, M., Erdjument-Bromage, H., Geromanos, S., Tempst, P., and Rothman, J. E. (1993)
Zhang, W., Khan, A., Vitale, J., Neuner, A., Rink, K., Lüchtenborg, C., Brügger, B., Söllner, T. H., & Schiebel, E. (2021)
Arrangements of proteins at reconstituted synaptic vesicle fusion sites depend on membrane separation. FEBS Letters, https://doi.org/10.1002/1873-3468.13916
Ginger L, Malsam M, Sonnen A, Morado D, Scheutzow A, Söllner TH, Briggs J (2020)
Complexin suppresses spontaneous exocytosis by capturing the membrane-proximal regions of VAMP2 and SNAP25. Cell Reports, 32. https://doi.org/10.1016/j.celrep.2020.107926 Malsam, J., Bärfuss, S., Trimbuch, T.h, Zarebidaki, F., Sonnen, A., Wild, K., Scheutzow, A., Rohland, L., Mayer, M., Sinning, I., Briggs, J., Rosenmund, C. & Söllner, T.H. (2020)
The Interaction of Munc18-1 Helix 11 and 12 with the Central Region of the VAMP2 SNARE Motif Is Essential for SNARE Templating and Synaptic Transmission. eNeuro, 7(6), ENEURO.0278-20.2020. https://doi.org/10.1523/ENEURO.0278-20.2020 André, T., Classen, J., Brenner, P., Betts, M. J., Dörr, B., Kreye, S., Zuidinga, B., Meijer, M., Russell, R. B., Verhage, M., & Söllner, T. H. (2020)
An Electrostatic Energy Barrier for SNARE-Dependent Spontaneous and Evoked Synaptic Transmission. Cell Rep. 2019 Feb 26;26(9):2340-2352.e5. doi: 10.1016/j.celrep.2019.01.103.
Ruiter M, Kádková A, Scheutzow A, Malsam J, Söllner TH, Sørensen JB (2019)
Synaptic vesicle fusion: today and beyond Nat Struct Mol Biol. Aug;26(8):663-668. doi: 10.1038/s41594-019-0277-z.
Brose N, Brunger A, Cafiso D, Chapman ER, Diao J, Hughson FM, Jackson MB, Jahn R, Lindau M, Ma C, Rizo J, Shin YK, Söllner TH, Tamm L, Yoon TY, Zhang Y (2019)
Tyrosine phosphorylation of Munc18-1 inhibits synaptic transmission by preventin SNARE assembly. The EMBO Journal 37(2): 300-320
Meijer M., Dörr B., Lammertse H., Blithikioti C., van Weering J., Toonen R., Söllner T.H., Verhage M. (2018)
Uncovering the “secret” Lives of Vacuolar Fusion pores in living cells. EMBOJ 37 (19) DOI:10.15252/embj.2018100656.
Söllner, T. Malsam, J. (2018)
Electrostatic anchoring precedes stable membrane attachment of SNAP25/SNAP23 to the plasma membrane. eLife 6:e19394. DOI: 10.7554/eLife.19394
Weber P., Batoulis H., Rink K.M., Dahlhoff S., Pinkwart K., Söllner T.H., Lang T. (2017)
Extension of Helix 12 in Munc18-1 Induces Vesicle Priming. J. Neurosci. 36(26): 6881-6891.
Munch, A.S., Kedar, G.H., van Weering, J.R.T., Vazquez-Sanchez, S., He, E., Andre, T., Braun, T., Söllner, T.H., Verhage, M., Sørensen, J.B. (2016)
Interactions Between SNAP-25 and Synaptotagmin-1 Are Involved in Vesicle Priming, Clamping Spontaneous and Stimulating Evoked Neurotransmission. J Neurosci. 36(47):11865-11880
Schupp M, Malsam J, Ruiter M, Scheutzow A, Wierda KD, Söllner TH, Sørensen JB. (2016)
A post-docking role of synaptotagmin 1-C2B domain bottom residues R398/399 in mouse chromaffin cells. J. Neurosci. 35(42): 14172-14182.
Kedar, G.H., Munch, A.S., van Weering, J.R.T., Malsam, J., Scheutzow, A., de Wit, H., Houy, S., Tawfik, B., Söllner, T.H., Sørensen, J.B., Verhage, M. (2015)
An Extended Helical Conformation in Domain 3a of Munc18-1 Provides a Template for SNARE (Soluble N-Ethylmaleimide-sensitive Factor Attachment Protein Receptor) Complex Assembly. J.Biol.Chem. 289, 9639-9650. https://doi.org/10.1074/jbc.M113.514273 Parisotto, D., Pfau, M., Scheutzow, A., Wild, K., Mayer, M.P., Malsam, J., Sinning, I., & Söllner, T.H. (2014)
SNARE and regulatory proteins induce local membrane protrusions to prime docked vesicles for fast calsium-triggered fusion. EMBO reports 15:3, 308-314.
Bharat, T.A., Malsam, J., Hagen, W.J., Scheutzow, A., Söllner, T.H., Briggs, J.A. (2014)
Complexin arrests a pool of docked vesicles for fast Ca (2+)-dependent release. EMBO J. 31, 3270-3281
Malsam, J., Parisotto, D., Bharat, T.A., Scheutzow A., Krause, J.M., Briggs, J.A., Söllner, T.H. (2012)
SNAREpin Assembly by Munc18-1 Requires Previous Vesicle Docking by Synaptotagmin 1. J. Biol. Chem. 287, 31041-31049
Parisotto, D., Malsam, J., Scheutzow, A., Krause, J.M., Söllner, T.H. (2012)
Organization of SNAREs within the Golgi stack. in ‘The Golgi’, Coldspring Harbor Perspectives in Biology (editors Warren, G. and Rothman, J.) Cold Spring Harbor Laboratory Press
Malsam, J., and Söllner, T.H. (2011)
Resolving the Function of Distinct Munc18-1/SNARE Protein Interaction Modes in a Reconstituted Membrane Fusion. JBC 286 No. 35, 30582-30590.
Schollmeier, Y., Krause, J. M., Kreye, S., Malsam, J., Söllner, T.H. (2011)
Distinct Roles of Myosin Va in Membrane Remodeling and Exocytosis of Secretory Granules. Traffic, 11: 637-650.
Kögel, T., Rudolf, R., Hodneland, E., Hellwig, A., Kuznetsov, S., Seiler, F., Söllner, T.H., Barroso, J., Gerdes, H.-H. (2010)
A role of complexin-lipid interactions in membrane fusion. FEBS letters, 583: 2343-8.
Seiler, F., Malsam, J., Krause, JM., Söllner, T.H. (2009)
The carboxy-terminal domain of complexin I stimulates liposome fusion. Proc. Natl. Acad. Sci. USA, 106: 2001-2006.
Malsam, J., Seiler, F., Schollmeier, Y., Rusu, P., Krause, JM., Söllner, T.H. (2009)
In vitro assays to measure SNARE mediated membrane fusion. Methods in Mol. Biol. 440: 37-50.
Kreye, S., Malsam, J., Söllner, T.H. (2008)
Membrane fusion: SNAREs and regulation. Cell Mol. Life. Sci., 65: 2814-2832.
Malsam, J., Kreye, S., Söllner, T.H. (2008)
Differential localization of isoformic coatomer complexes within the Golgi apparatus. Proc. Natl. Acad. Sci. USA, 104: 4425-30.
Moelleken, J., Malsam, J., Betts, M.J., Movafeghi, A., Reckmann, I., Meissner, I., Hellwig, A., Russell, R.B., Söllner, T.H., Brügger, B., Wieland, F.T. (2007)
Lipid droplets highjack SNAREs. Nat. Cell Biol., 9:1219-20.
Söllner, T.H. (2007)
Membrane trafficking. FEBS Letters, 581: 2075.
Söllner, T.H. (2007)
Dynamic transport of SNARE proteins in the Golgi apparatus. Proc Natl Acad Sci U S A, 102:14647-52.
Cosson, P., Ravazzola, M., Varlamov, O., Söllner, T.H., Di Liberto, M., Volchuk, A., Rothman J.E., Orci, L. (2005)
Crystallographic identification of Ca2+ and Sr2+ coordination sites in synaptotagmin I C2B domain. Protein Science, 13: 2665-2672.
Cheng, Y. Sequeira, S.M., Malinina, L., Tereshko, V., Söllner, T.H., and Patel, D.J. (2004)
Intracellular and viral membrane fusion: a uniting mechanism. Curr. Opinion Cell Biol, 16: 429-435.
Söllner, T.H. (2004)
i-SNAREs, inhibitory SNAREs that fine-tune the specificity of membrane fusion. J. Cell Biol., 164: 79-88.
Varlamov, O., Volchuk, A., Rahimian, V., Doege, C.A. Paumet, F., Eng, W.S, Arango, N.C., Parlati, F., Ravazzola, M., Orci, L, Söllner, T.H., and Rothman, J.E. (2004)
Localization and activity of the SNARE Ykt6 determined by its regulatory domain and palmitoylation. Proc. Natl. Acad. Sci. USA, 101: 4815-1820.
Fukasawa, M., Varlamov, O., Eng, W.S., Söllner, T.H., and Rothman, J.E. (2004)
A SNARE required for retrograde transport to the endoplasmic reticulum. Proc. Natl. Acad. Sci. USA, 100: 9873-9877.
Burri, L., Varlamov, O., Doege, C., Hofman, K., Beilharz, T., Rothman, J.E., Söllner, T.H., and Lithgow, T. (2003)
Fusion of cells by flipped SNAREs. Science, 300: 1745-1749.
Hu, C., Ahmed, M., Melia, T.J., Söllner, T.H., Mayer, T., and Rothman, J.E. (2003)
Regulated exocytosis and SNARE function. Mol. Memb. Biol., 20: 209-220.
Söllner T.H. (2003)
S-nitrosylation of NSF controls membrane trafficking. Cell, 115: 127-129.
Söllner, T.H., and Sequeira, S. (2003)
Calcium-independent stimulation of membrane fusion and SNAREpin formation by synaptotagmin I. The Journal of cell biology, 158(2), 273–282. https://doi.org/10.1083/jcb.200203135 Mahal, L. K., Sequeira, S. M., Gureasko, J. M., & Söllner, T. H. (2002)
Distinct SNARE complexes mediating membrane fusion in Golgi transport based on combinatorial specificity. Proc. Natl. Acad. Sci. USA, 99: 5424-5429.
Parlati, F., Varlamov, O., Paz, K., McNew, J.A., Hurtado, D., Söllner, T.H., and Rothman, J.E. (2002)
Regulation of membrane fusion by the membrane-proximal coil of the t SNARE during zippering of SNAREpins. J. Cell Biol, 158: 929-940. Melia, T.J., Weber, T., McNew, J.A., Fisher, L.E., Johnston, R.J., Parlati, F., Mahal, L.K. Söllner, T.H., and Rothman, J.E. (2002)
A t-SNARE of the endocytic pathway must be activated for fusion. J Cell Biol. 155(6):961-8. Paumet F, Brügger B, Parlati F, McNew JA, Söllner TH, Rothman JE. (2001)
Close is not enough: SNARE-dependent membrane fusion requires an active mechanism that transduces force to membrane anchors. J.Cell Biol., 150: 105-117.
McNew, J.A., Weber, T., Parlati, F., Johnston, R., Melia, T.J., Söllner, T.H., and Rothman, J.E. (2000)
Compartmental specificity of cellular membrane fusion encoded in SNARE proteins. Nature, 407: 153-159.
McNew, J.A., Parlati, F., Fukuda, R., Johnston, R.J., Paz, K., Paumet, F., Söllner, T.H., and Rothman, J.E. (2000)
Functional Architecture of Intracellular t-SNAREs: Membrane Fusion by Isolated SNAREs of the Yeast Vacuole. Nature 407:198-202. Ryouichi Fukuda, James A. McNew, Thomas Weber, Francesco Parlati, Thomas Engel, Walter Nickel, James E. Rothman, and Thomas H. Söllner (2000)
Putative fusogenic activity of NSF is restricted to a lipid mixture whose coalescence is also triggered by other factors. EMBO J. 19(6):1272-8. Brügger B, Nickel W, Weber T, Parlati F, McNew JA, Rothman JE, Söllner T. (2000)
SNAREpins are functionally resistant to disruption by NSF and aSNAP. J.Cell Biol., 149: 1063-1072.
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Topological restriction of SNARE-dependent membrane fusion. Nature, 407: 194-198.
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Content mixing and membrane integrity during membrane fusion driven by pairing of isolated v-SNAREs and t-SNAREs. Proc. Natl. Acad Sci. U.S.A. 96 :12571-12576. Walter Nickel, Thomas Weber, James A. McNew, Francesco Parlati, Thomas H. Söllner, and James E. Rothman (1999)
Coupling of coat assembly and vesicle budding to packaging of putative cargo receptors. Cell 96, 495-506. M. Bremser, W. Nickel, M. Schweikert, M. Ravazzola, M. Amherd, C.A. Hughes, T.H. Söllner, J. E. Rothman, and F. T. Wieland (1999)
Arrangement of subunits in 20 S particles consisting of NSF, SNAPs, and SNARE complexes. Mol. Cell, 2: 539-548.
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SNAREpins: minimal machinery for membrane fusion. Cell, 92: 759-772.
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Throttles and Dampers: controlling the engine of membrane fusion. Science, 276: 1212-1213.
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A v-SNARE implicated in intra-Golgi transport. J. Cell. Biol, 133: 507-516
Nagahama, M., Orci, L., Ravazzola, M., Amherdt, M., Lacomis, L., Tempst, P., Rothman, J.E., and Söllner, T.H. (1996)
A rab protein is required for the assembly of SNARE complexes in the docking of transport vesicles. Cell, 78: 937-948.
Søgaard, M., Tani, K., Ye, R.R., Geromanos, S., Tempst, T., Kirchausen, T., Rothman, J.E., and Söllner, T. (1994)
A protein assembly - disassembly pathway that may correspond to sequential steps of synaptic vesicle docking, activation and fusion. Cell, 75: 409-418.
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SNAP receptors implicated in vesicle targeting and fusion. Nature 362, 318-324. Söllner, T., Whiteheart, S. W., Brunner, M., Erdjument-Bromage, H., Geromanos, S., Tempst, P., and Rothman, J. E. (1993)
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