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3. Actin dynamics drive cell-like membrane deformation

Author

Simon, Camille, Kusters, Rémy, Caorsi, Valentina, Allard, Antoine, Abou-Ghali, Majdouline, Manzi, John, Di Cicco, Aurélie, Lévy, Daniel, Lenz, Martin, Joanny, Jean-François, Campillo, Clément, Plastino, Julie, Sens, Pierre, and Sykes, Cécile

Published
2019
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14. Mechanistic comparison of the cobalt-substituted and wild-type copper amine oxidase from Hansenula polymorpha

Author

Mills, Stephen A., Goto, Yoshio, Su, Qiaojuan, Plastino, Julie, and Klinman, Judith P.

Subjects
Oxidases -- Research, Enzyme kinetics -- Analysis, Catalysis -- Analysis, Mechanical chemistry -- Research, Biological sciences, Chemistry
Abstract

The mechanisms of catalysis by the copper amine oxidase and its cobalt-substituted form from Hansenula polymorpha are very similar with respect to molecular oxygen reaction although the K(sub)m for oxygen is about 70-fold higher in the latter. This difference is due to a change in the net charge at the metal site.

Published
2002

23. A direct proof that sole actin dynamics drive membrane deformations

Author

Simon, Camille, primary, Kusters, Rémy, additional, Caorsi, Valentina, additional, Allard, Antoine, additional, Abou-Ghali, Majdouline, additional, Manzi, John, additional, Di Cicco, Aurélie, additional, Lévy, Daniel, additional, Lenz, Martin, additional, Joanny, Jean-François, additional, Campillo, Clément, additional, Plastino, Julie, additional, Sens, Pierre, additional, and Sykes, Cécile, additional

Published
2018
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27. Dynamic stability of the actin ecosystem.

Author

Plastino, Julie and Blanchoin, Laurent

Subjects
*CYTOSKELETON, *DYNAMIC stability, *ACTIN
Abstract

In cells, actin filaments continuously assemble and disassemble while maintaining an apparently constant network structure. This suggests a perfect balance between dynamic processes. Such behavior, operating far out of equilibrium by the hydrolysis of ATP, is called a dynamic steady state. This dynamic steady state confers a high degree of plasticity to cytoskeleton networks that allows them to adapt and optimize their architecture in response to external changes on short time-scales, thus permitting cells to adjust to their environment. In this Review, we summarize what is known about the cellular actin steady state, and what gaps remain in our understanding of this fundamental dynamic process that balances the different forms of actin organization in a cell. We focus on the minimal steps to achieve a steady state, discuss the potential feedback mechanisms at play to balance this steady state and conclude with an outlook on what is needed to fully understand its molecular nature. [ABSTRACT FROM AUTHOR]

Published
2019
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30. Actin filaments up against a wall

Author

Sykes, Cecile and Plastino, Julie

Subjects
Actin -- Physiological aspects -- Genetic aspects, Cell membranes -- Physiological aspects -- Genetic aspects, Environmental issues, Science and technology, Zoology and wildlife conservation
Abstract

The front of motile cells is thought to be pushed out by branched filaments of actin protein abutting the cell membrane. New work challenges this textbook view, showing that actin [...]

Published
2010

47. An unexpected role for the active site base in cofactor orientation and flexibility in the copper amine oxidase from Hansenula polymorpha

Author

Plastino, Julie, Green, Edward L., Sanders-Loehr, Joann, and Klinman, Judith P.

Subjects
Binding sites (Biochemistry) -- Research, Oxidases -- Research, Aspartate aminotransferase -- Research, Mutagenesis -- Usage, Biological sciences, Chemistry
Abstract

Research was conducted to examine the effects of mutation of the active site aspartate, residue 319 in HPAO using a combination of resonance Raman spectroscopy, ultraviolet-vis spectroscopy and kinetic analysis of site-directed mutants. It was observed that it was not possible to prepare and characterize stable substrate imine complexes of the cofactor. However, evidence is presented for altered cofactor conformations which influence the stability and the reactivity of catalytic intermediates and implicate the active site base as an important residue in the maintenance of the cofactor orientation during turnover.

Published
1999

49. Limited proteolysis of Hansenula polymorphayeast amine oxidase: isolation of a C-terminal fragment containing both a copper and quino-cofactor

Author

Plastino, Julie and Klinman, Judith P.

Abstract

Limited proteolysis of recombinant Hansenula polymorphayeast amino oxidase produces a 48 kDa fragment which corresponds to the C-terminal two-thirds of the protein. The fragment contains both TOPA (2,4,5-trihydroxyphenylalanine) and copper, as well as the histidine ligands implicated in copper binding. The fragment is proposed to be the domain responsible for cofactor production in yeast amine oxidase.

Published
1995
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