Recycling of the actin monomer pool limits the lifetime of network turnover
Intracellular organization is largely mediated by actin turnover. Cellular actin networks continuously assemble and disassemble, while maintaining their overall appearance. This behavior, called “dynamic steady state,” allows cells to sense and adapt to their environment. However, how structural sta...
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| Published in | The EMBO journal Vol. 42; no. 9; pp. e112717 - n/a |
|---|---|
| Main Authors | , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
London
Nature Publishing Group UK
02.05.2023
Springer Nature B.V EMBO Press John Wiley and Sons Inc |
| Subjects | |
| Online Access | Get full text |
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| Abstract | Intracellular organization is largely mediated by actin turnover. Cellular actin networks continuously assemble and disassemble, while maintaining their overall appearance. This behavior, called “dynamic steady state,” allows cells to sense and adapt to their environment. However, how structural stability can be maintained during the constant turnover of a limited actin monomer pool is poorly understood. To answer this question, we developed an experimental system where polystyrene beads are propelled by an actin comet in a microwell containing a limited amount of components. We used the speed and the size of the actin comet tails to evaluate the system's monomer consumption and its lifetime. We established the relative contribution of actin assembly, disassembly, and recycling for a bead movement over tens of hours. Recycling mediated by cyclase‐associated protein (CAP) is the key step in allowing the reuse of monomers for multiple assembly cycles. ATP supply and protein aging are also factors that limit the lifetime of actin turnover. This work reveals the balancing mechanism for long‐term network assembly with a limited amount of building blocks.
Synopsis
Mechanisms enabling the maintenance of cellular structural stability during the constant turnover of a limited actin monomer pool are poorly understood. Here, reconstitution of actin in a dynamic steady state using a combination of purified proteins and cell‐sized compartments reveals the parameters influencing actin lifetime.
Sustained actin turnover over multiple hours was reconstituted in cell‐sized microwells containing a limited amount of components
A recycling step is required for reuse of actin monomers and other actin‐binding proteins in multiple assembly cycles
Actin monomers age and limit the lifetime of the reconstituted system
Changes in the availability of actin monomers enable a feedback loop between assembly and disassembly
Graphical Abstract
Reconstitution of actin in a dynamic steady state using cell‐sized compartments reveals the parameters influencing long‐term assembly upon limited component availability. |
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| AbstractList | Intracellular organization is largely mediated by actin turnover. Cellular actin networks continuously assemble and disassemble, while maintaining their overall appearance. This behavior, called “dynamic steady state,” allows cells to sense and adapt to their environment. However, how structural stability can be maintained during the constant turnover of a limited actin monomer pool is poorly understood. To answer this question, we developed an experimental system where polystyrene beads are propelled by an actin comet in a microwell containing a limited amount of components. We used the speed and the size of the actin comet tails to evaluate the system's monomer consumption and its lifetime. We established the relative contribution of actin assembly, disassembly, and recycling for a bead movement over tens of hours. Recycling mediated by cyclase‐associated protein (CAP) is the key step in allowing the reuse of monomers for multiple assembly cycles. ATP supply and protein aging are also factors that limit the lifetime of actin turnover. This work reveals the balancing mechanism for long‐term network assembly with a limited amount of building blocks.
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Mechanisms enabling the maintenance of cellular structural stability during the constant turnover of a limited actin monomer pool are poorly understood. Here, reconstitution of actin in a dynamic steady state using a combination of purified proteins and cell‐sized compartments reveals the parameters influencing actin lifetime.
Sustained actin turnover over multiple hours was reconstituted in cell‐sized microwells containing a limited amount of components
A recycling step is required for reuse of actin monomers and other actin‐binding proteins in multiple assembly cycles
Actin monomers age and limit the lifetime of the reconstituted system
Changes in the availability of actin monomers enable a feedback loop between assembly and disassembly Intracellular organization is largely mediated by actin turnover. Cellular actin networks continuously assemble and disassemble, while maintaining their overall appearance. This behavior, called “dynamic steady state,” allows cells to sense and adapt to their environment. However, how structural stability can be maintained during the constant turnover of a limited actin monomer pool is poorly understood. To answer this question, we developed an experimental system where polystyrene beads are propelled by an actin comet in a microwell containing a limited amount of components. We used the speed and the size of the actin comet tails to evaluate the system's monomer consumption and its lifetime. We established the relative contribution of actin assembly, disassembly, and recycling for a bead movement over tens of hours. Recycling mediated by cyclase‐associated protein (CAP) is the key step in allowing the reuse of monomers for multiple assembly cycles. ATP supply and protein aging are also factors that limit the lifetime of actin turnover. This work reveals the balancing mechanism for long‐term network assembly with a limited amount of building blocks. Synopsis Mechanisms enabling the maintenance of cellular structural stability during the constant turnover of a limited actin monomer pool are poorly understood. Here, reconstitution of actin in a dynamic steady state using a combination of purified proteins and cell‐sized compartments reveals the parameters influencing actin lifetime. Sustained actin turnover over multiple hours was reconstituted in cell‐sized microwells containing a limited amount of components A recycling step is required for reuse of actin monomers and other actin‐binding proteins in multiple assembly cycles Actin monomers age and limit the lifetime of the reconstituted system Changes in the availability of actin monomers enable a feedback loop between assembly and disassembly Reconstitution of actin in a dynamic steady state using cell‐sized compartments reveals the parameters influencing long‐term assembly upon limited component availability. Intracellular organization is largely mediated by actin turnover. Cellular actin networks continuously assemble and disassemble, while maintaining their overall appearance. This behavior, called "dynamic steady state," allows cells to sense and adapt to their environment. However, how structural stability can be maintained during the constant turnover of a limited actin monomer pool is poorly understood. To answer this question, we developed an experimental system where polystyrene beads are propelled by an actin comet in a microwell containing a limited amount of components. We used the speed and the size of the actin comet tails to evaluate the system's monomer consumption and its lifetime. We established the relative contribution of actin assembly, disassembly, and recycling for a bead movement over tens of hours. Recycling mediated by cyclase-associated protein (CAP) is the key step in allowing the reuse of monomers for multiple assembly cycles. ATP supply and protein aging are also factors that limit the lifetime of actin turnover. This work reveals the balancing mechanism for long-term network assembly with a limited amount of building blocks.Intracellular organization is largely mediated by actin turnover. Cellular actin networks continuously assemble and disassemble, while maintaining their overall appearance. This behavior, called "dynamic steady state," allows cells to sense and adapt to their environment. However, how structural stability can be maintained during the constant turnover of a limited actin monomer pool is poorly understood. To answer this question, we developed an experimental system where polystyrene beads are propelled by an actin comet in a microwell containing a limited amount of components. We used the speed and the size of the actin comet tails to evaluate the system's monomer consumption and its lifetime. We established the relative contribution of actin assembly, disassembly, and recycling for a bead movement over tens of hours. Recycling mediated by cyclase-associated protein (CAP) is the key step in allowing the reuse of monomers for multiple assembly cycles. ATP supply and protein aging are also factors that limit the lifetime of actin turnover. This work reveals the balancing mechanism for long-term network assembly with a limited amount of building blocks. Intracellular organization is largely mediated by actin turnover. Cellular actin networks continuously assemble and disassemble, while maintaining their overall appearance. This behavior, called "dynamic steady state," allows cells to sense and adapt to their environment. However, how structural stability can be maintained during the constant turnover of a limited actin monomer pool is poorly understood. To answer this question, we developed an experimental system where polystyrene beads are propelled by an actin comet in a microwell containing a limited amount of components. We used the speed and the size of the actin comet tails to evaluate the system's monomer consumption and its lifetime. We established the relative contribution of actin assembly, disassembly, and recycling for a bead movement over tens of hours. Recycling mediated by cyclase-associated protein (CAP) is the key step in allowing the reuse of monomers for multiple assembly cycles. ATP supply and protein aging are also factors that limit the lifetime of actin turnover. This work reveals the balancing mechanism for long-term network assembly with a limited amount of building blocks. Intracellular organization is largely mediated by actin turnover. Cellular actin networks continuously assemble and disassemble, while maintaining their overall appearance. This behavior, called “dynamic steady state,” allows cells to sense and adapt to their environment. However, how structural stability can be maintained during the constant turnover of a limited actin monomer pool is poorly understood. To answer this question, we developed an experimental system where polystyrene beads are propelled by an actin comet in a microwell containing a limited amount of components. We used the speed and the size of the actin comet tails to evaluate the system's monomer consumption and its lifetime. We established the relative contribution of actin assembly, disassembly, and recycling for a bead movement over tens of hours. Recycling mediated by cyclase‐associated protein (CAP) is the key step in allowing the reuse of monomers for multiple assembly cycles. ATP supply and protein aging are also factors that limit the lifetime of actin turnover. This work reveals the balancing mechanism for long‐term network assembly with a limited amount of building blocks. Synopsis Mechanisms enabling the maintenance of cellular structural stability during the constant turnover of a limited actin monomer pool are poorly understood. Here, reconstitution of actin in a dynamic steady state using a combination of purified proteins and cell‐sized compartments reveals the parameters influencing actin lifetime. Sustained actin turnover over multiple hours was reconstituted in cell‐sized microwells containing a limited amount of components A recycling step is required for reuse of actin monomers and other actin‐binding proteins in multiple assembly cycles Actin monomers age and limit the lifetime of the reconstituted system Changes in the availability of actin monomers enable a feedback loop between assembly and disassembly Graphical Abstract Reconstitution of actin in a dynamic steady state using cell‐sized compartments reveals the parameters influencing long‐term assembly upon limited component availability. Intracellular organization is largely mediated by actin turnover. Cellular actin networks continuously assemble and disassemble, while maintaining their overall appearance. This behavior, called “dynamic steady state,” allows cells to sense and adapt to their environment. However, how structural stability can be maintained during the constant turnover of a limited actin monomer pool is poorly understood. To answer this question, we developed an experimental system where polystyrene beads are propelled by an actin comet in a microwell containing a limited amount of components. We used the speed and the size of the actin comet tails to evaluate the system's monomer consumption and its lifetime. We established the relative contribution of actin assembly, disassembly, and recycling for a bead movement over tens of hours. Recycling mediated by cyclase‐associated protein (CAP) is the key step in allowing the reuse of monomers for multiple assembly cycles. ATP supply and protein aging are also factors that limit the lifetime of actin turnover. This work reveals the balancing mechanism for long‐term network assembly with a limited amount of building blocks. Reconstitution of actin in a dynamic steady state using cell‐sized compartments reveals the parameters influencing long‐term assembly upon limited component availability. |
| Author | Mogilner, Alex Vianay, Benoit Lappalainen, Pekka Théry, Manuel Kotila, Tommi Colin, Alexandra Guérin, Christophe Orhant‐Prioux, Magali Blanchoin, Laurent |
| AuthorAffiliation | 5 Department of Biology New York University New York NY USA 3 CytoMorpho Lab, Institut de Recherche Saint Louis, U976 Human Immunology Pathophysiology Immunotherapy (HIPI) University of Paris, INSERM, CEA Paris France 4 Courant Institute of Mathematical Sciences New York University New York NY USA 1 CytoMorpho Lab, Laboratoire de Physiologie Cellulaire & Végétale, Interdisciplinary Research Institute of Grenoble University of Grenoble‐Alpes, CEA, CNRS, INRA Grenoble France 2 Institute of Biotechnology and Helsinki Institute of Life Science University of Helsinki Helsinki Finland |
| AuthorAffiliation_xml | – name: 4 Courant Institute of Mathematical Sciences New York University New York NY USA – name: 1 CytoMorpho Lab, Laboratoire de Physiologie Cellulaire & Végétale, Interdisciplinary Research Institute of Grenoble University of Grenoble‐Alpes, CEA, CNRS, INRA Grenoble France – name: 2 Institute of Biotechnology and Helsinki Institute of Life Science University of Helsinki Helsinki Finland – name: 5 Department of Biology New York University New York NY USA – name: 3 CytoMorpho Lab, Institut de Recherche Saint Louis, U976 Human Immunology Pathophysiology Immunotherapy (HIPI) University of Paris, INSERM, CEA Paris France |
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| Keywords | lifetime actin turnover aging reconstituted system microwells actin turnover aging lifetime microwells reconstituted system Subject Category Cell Adhesion reconstituted system Subject Category Cell Adhesion Polarity & Cytoskeleton |
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| SubjectTerms | Actin Actin Cytoskeleton - metabolism actin turnover Actins - metabolism aging Beads Cellular Biology Cellular communication Cellular structure Comet tails Cycle protein Dismantling EMBO05 Feedback loops Life Sciences lifetime microwells Monomers Polystyrene Polystyrene resins Proteins reconstituted system Steady state Structural stability |
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| Title | Recycling of the actin monomer pool limits the lifetime of network turnover |
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