Top

Published in:

2022 | OriginalPaper | Chapter

12. Membrane-Remodeling Proteins

Author : Toshio Ando

Published in: High-Speed Atomic Force Microscopy in Biology

Publisher: Springer Berlin Heidelberg

Activate our intelligent search to find suitable subject content or patents.

search-config

AI-assisted search

Off

Abstract

Many cellular processes depend on membrane shape changes. Cytokinesis, exocytosis and endocytosis, phagocytosis, T-tubule formation in muscle, crista formation in mitochondria, fission and fusion of organelles, and fission and fusion of vesicular compartments as transport carriers all proceed via membrane rearrangements. Their initial process proceeds from membrane bulging and budding either toward or away from the cytoplasm.

Dont have a licence yet? Then find out more about our products and how to get one now:

Springer Professional "Wirtschaft+Technik"

Online-Abonnement

Mit Springer Professional "Wirtschaft+Technik" erhalten Sie Zugriff auf:

über 102.000 Bücher
über 537 Zeitschriften

aus folgenden Fachgebieten:

Automobil + Motoren
Bauwesen + Immobilien
Business IT + Informatik
Elektrotechnik + Elektronik
Energie + Nachhaltigkeit
Finance + Banking
Management + Führung
Marketing + Vertrieb
Maschinenbau + Werkstoffe
Versicherung + Risiko

Jetzt Wissensvorsprung sichern!

inform now

Springer Professional "Technik"

Online-Abonnement

Mit Springer Professional "Technik" erhalten Sie Zugriff auf:

über 67.000 Bücher
über 390 Zeitschriften

aus folgenden Fachgebieten:

Automobil + Motoren
Bauwesen + Immobilien
Business IT + Informatik
Elektrotechnik + Elektronik
Energie + Nachhaltigkeit
Maschinenbau + Werkstoffe

Jetzt Wissensvorsprung sichern!

inform now

previous chapter Canonical Motor Proteins

next chapter Intrinsically Disordered Proteins (IDPs)

Available only for authorised users

Bashkirov, P. V., AkimovS, A., Evseev, A. I., Schmid, S. L., Zimmerberg, J., & Frolov, V. A. (2008). GTPase cycle of dynamin is coupled to membrane squeeze and release, leading to spontaneous fission. Cell, 135, 1276–1286.CrossRef

Bassereau, P., Jin, R., Baumgart, T., Deserno, M., Dimova, R., Frolov, V. A., Bashkirov, P. V., Grubmüller, H., Jahn, R., Risselada, H. J., Johannes, L., Kozlov, M. M., Lipowsky, R., Pucadyil, T. J., Zeno, W. F., Stachowiak, J. C., Stamou, D., Breuer, A., Lauritsen, L., Simon, C., Sykes, C., Voth, G. A., & Weikl, T. R. (2018). Topical review: The 2018 biomembrane curvature and remodeling roadmap. Journal of Physics D: Applied Physics, 51, 343001.

Carlton, J. G., & Martin-Serrano, J. (2009). The ESCRT machinery: New functions in viral and cellular biology. Biochemical Society Transactions, 37, 195–199.CrossRef

Cashikar, A. G., Shim, S., Roth, R., Maldazys, M. R., Heuser, J. E., Hanson, P. I. (2014). Structure of cellular E SCRT-III spirals and their relationship to HIV budding. eLife, 3, e02184.

Chappie, J. S., Mears, J. A., Fang, S., Leonard, M., Schmid, S. L., Milligan, R. A., Hinshaw, J. E., & Dyda, F. (2011). A pseudoatomic model of the dynamin polymer identifies a hydrolysis-dependent powerstroke. Cell, 147, 209–222.CrossRef

Chen, Y., Zhang, P., Egelman, E., & Hinshaw, J. E. (2004). The stalk region of dynamin drives the constriction of dynamin tubes. Nature Structural & Molecular Biology, 11, 574–575.CrossRef

Chiaruttini, N., Redondo-Morata, L., Colom, A., Humbert, F., Lenz, M., Scheuring, S., & Roux, A. (2015). Relaxation of loaded ESCRT-III spiral springs drives membrane deformation. Cell, 163, 866–879.CrossRef

Colom, A., Redondo-Morata, L., Chiaruttini, N., Roux, A., & Scheuring, S. (2017). Dynamic remodeling of the dynamin helix during membrane constriction. Proceedings of the National Academy of Sciences of the United States of America, 114, 5449–5454.CrossRef

Daumke, O., & Unger, V. M. (2016). Special Issue Introductions: Protein-mediated membrane remodeling. Journal of Structural Biology, 196, 1–2.CrossRef

Faelber, K., Posor, Y., Gao, S., Held, M., Roske, Y., Schulze, D., Haucke, V., Noé, F., & Daumke, O. (2011). Crystal structure of nucleotide-free dynamin. Nature, 477, 561–566.CrossRefADS

Ferguson, S. M., & De Camilli, P. (2012). Dynamin, a membrane-remodelling GTPase. Nature Reviews Molecular Cell Biology, 13, 75–88.CrossRef

Ford, M. G. J., Jenni, S., & Nunnari, J. (2011). The crystal structure of dynamin. Nature, 477, 556–560.CrossRefADS

Hanson, P. I., Roth, R., Lin, Y., & Heuser, J. E. (2008). Plasma membrane deformation by circular arrays of ESCRT-III protein filaments. Journal of Cell Biology, 180, 389–402.CrossRef

Hanson, P. I., Shim, S., & Merrill, S. A. (2009). Cell biology of the ESCRT machinery. Current Opinion in Cell Biology, 21, 568–574.CrossRef

Kozlov, M. M., McMahon, H. T., & Chernomordik, L. V. (2010). Protein-driven membrane stresses in fusion and fission. Trends in Biochemical Sciences, 35, 699–706.CrossRef

Landsberg, M. J., Vajjhala, P. R., Rothnage, R., Munn, A. L., & Hankamer, B. (2009). Three-dimensional structure of AAA ATPase Vps4: Advancing structural insights into the mechanisms of endosomal sorting and enveloped virus budding. Structure, 17, 427–437.CrossRef

Lata, S., Schoehn, G., Jain, A., Pires, R., Piehler, J., Gőttlinger, H. G., & Weissenhorn, W. (2008). Helical structures of ESCRT-III are disassembled by VPS4. Science, 321, 1354–1357.CrossRefADS

Maity, S., Caillat, C., Miguet, N., Sulbaran, G., Effantin, G., Schoehn, G., Roos, W.H., & Weissenhorn, W. (2019). VPS4 triggers constriction and cleavage of ESCRT-III helical filaments. Science Advances, 5, eaau7198.

McCullough, J., Clippinger, A. K., Talledge, N., Skowyra, M. L., Saunders, M. G., Naismith, T. V., Colf, L. A., Afonine, P., Arthur, C., Sundquist, W. I., Hanson, P. I., & Frost, A. (2015). Structure and membrane remodeling activity of ESCRT-III helical polymers. Science, 350, 1548–1551.CrossRefADS

McCullough, J., Frost, A., & Sundquist, W. I. (2018). Structures, functions, and dynamics of ESCRT-III/Vps4 membrane remodeling and fission complexes. Annual Review of Cell and Developmental Biology, 34, 85–109.CrossRef

Mierzwa, B. E., Chiaruttini, N., Redondo-Morata, L., Moser Von Filseck, J., König, J., Larios, J., Poser, I., Müller-Reichert, T., Scheuring, S., Roux, A., & Gerlich, D. W. (2017). Dynamic subunit turnover in ESCRT-III assemblies is regulated by Vps4 to mediate membrane remodelling during cytokinesis. Nature Cell Biology, 19, 787–798.CrossRef

Obita, T., Saksena, S., Ghazi-Tabatabai, S., Gill, D. J., Perisic, O., Emr, S. D., & Williams, R. L. (2007). Structural basis for selective recognition of ESCRT-III by the AAA ATPase Vps4. Nature, 449, 735–739.CrossRefADS

Pucadyil, T. J., & Schmid, S. L. (2008). Real-time visualization of dynamin-catalyzed membrane fission and vesicle release. Cell, 135, 1263–1275.CrossRef

Reubold, T. F., Faelber, K. L., Plattner, N., Posor, Y., Ketel, K., Curth, U., & Schlegel, J. (2015). Crystal structure of the dynamin tetramer. Nature, 525, 404–408.CrossRefADS

Roux, A., Uyhazi, K., Frost, A., & De Camilli, P. (2006). GTP-dependent twisting of dynamin implicates constriction and tension in membrane fission. Nature, 441, 528–530.CrossRefADS

Schöneberg, J., et al. (2018). ATP-dependent force generation and membrane scission by ESCRT-III and Vps4. Science, 362, 1423–1428.CrossRefADS

Stowell, M. H., Marks, B., Wigge, P., & McMahon, H. T. (1999). Nucleotide-dependent conformational changes in dynamin: Evidence for a mechanochemical molecular spring. Nature Cell Biology, 1, 27–32.CrossRef

Stuchell-Brereton, M. D., Skalicky, J. J., Kieffer, C., Karren, M. A., Ghaffarian, S., & Sundquist, W. I. (2007). ESCRT-III recognition by VPS4 ATPases. Nature, 449, 740–744.CrossRefADS

Stuffers, S., Brech, A., & Stenmark, H. (2009). ESCRT proteins in physiology and disease. Experimental Cell Research, 315, 1619–1626.CrossRef

Sundborger, A. C., Fang, S., Heymann, J. A., Ray, P., Chappie, J. S., & Hinshaw, J. E. (2014). A dynamin mutant defines a superconstricted prefission state. Cell Reports, 8, 734–742.CrossRef

Sweitzer, S. M., & Hinshaw, J. E. (1998). Dynamin undergoes a GTP-dependent conformational change causing vesiculation. Cell, 93, 1021–1029.CrossRef

Takeda, T., Kozai, T., Yang, H., Ishikuro, D., Seyama, K., Kumagai, Y., Abe, T., Yamada, H., Uchihashi, T., Ando, T., & Takei, K. (2018). Dynamic clustering of dynamin-amphiphysin helices regulates membrane constriction and fission coupled with GTP hydrolysis. eLife, 7, e30246.

Takei, K., McPherson, P. S., Schmid, S. L., & De Camilli, P. (1995). Tubular membrane invaginations coated by dynamin rings are induced by GTP-γS in nerve terminals. Nature, 374, 186–190.CrossRefADS

Takei, K., Haucke, V., Slepnev, V., Farsad, K., Salazar, M., Chen, H., & De Camilli, P. (1998). Generation of coated intermediates of clathrin-mediated endocytosis on protein-free liposomes. Cell, 94, 131–141.CrossRef

Vietri, M., Radulovic, M., & Stenmark, H. (2020). The many functions of ESCRTs. Nature Reviews Molecular Cell Biology, 21, 25–42.CrossRef

Wollert, T., Wunder, C., Lippincott-Schwartz, J., & Hurley, J. H. (2009). Membrane scission by the ESCRT-III complex. Nature, 458, 172–177.CrossRefADS

Wollert, T., & Hurley, J. H. (2010). Molecular mechanism of multivesicular body biogenesis by the ESCRT complexes. Nature, 464, 864–869.CrossRefADS

Zhang, P., & Hinshaw, J. E. (2001). Three-dimensional reconstruction of dynamin in the constricted state. Nature Cell Biology, 3, 922–925.CrossRef

Title: Membrane-Remodeling Proteins
Author: Toshio Ando
Publisher: Springer Berlin Heidelberg
Book: High-Speed Atomic Force Microscopy in Biology
Print ISBN: 978-3-662-64783-7

Electronic ISBN: 978-3-662-64785-1

Copyright Year: 2022
DOI: https://doi.org/10.1007/978-3-662-64785-1_12