ArticleCytoskeleton (Hoboken, N.J.)2014
Autonomous and in trans functions for the two halves of Srv2/CAP in promoting actin turnover.
Article in Cytoskeleton (Hoboken, N.J.), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
18 citing papers in PubMed.
- The actin filament pointed-end depolymerase Srv2/CAP depolymerizes barbed ends, displaces capping protein, and promotes formin processivity.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Multicomponent depolymerization of actin filament pointed ends by cofilin and cyclase-associated protein depends upon filament age.European journal of cell biology · 2024Article
- Multicomponent depolymerization of actin filament pointed ends by cofilin and cyclase-associated protein depends upon filament age.bioRxiv : the preprint server for biology · 2024Article
- Cytosolic concentrations of actin binding proteins and the implications for in vivo F-actin turnover.The Journal of cell biology · 2023Article
- Mechanisms of actin disassembly and turnover.The Journal of cell biology · 2023Review
- Cyclase-associated protein interacts with actin filament barbed ends to promote depolymerization and formin displacement.The Journal of biological chemistry · 2023Article
- Dynamic remodeling of actin networks by cyclase-associated protein and CAP-Abp1 complexes.Current biology : CB · 2023Article
- Recycling of the actin monomer pool limits the lifetime of network turnover.The EMBO journal · 2023Article
- CAPt'n of Actin Dynamics: Recent Advances in the Molecular, Developmental and Physiological Functions of Cyclase-Associated Protein (CAP).Frontiers in cell and developmental biology · 2020Review
- Synergy between Cyclase-associated protein and Cofilin accelerates actin filament depolymerization by two orders of magnitude.Nature communications · 2019Article
- Srv2 Is a Pro-fission Factor that Modulates Yeast Mitochondrial Morphology and Respiration by Regulating Actin Assembly.iScience · 2019Article
- Structural basis of actin monomer re-charging by cyclase-associated protein.Nature communications · 2018Article
- Conserved hydrophobic residues in the CARP/β-sheet domain of cyclase-associated protein are involved in actin monomer regulation.Cytoskeleton (Hoboken, N.J.) · 2017Article
- Peptide regulation of cofilin activity in the CNS: A novel therapeutic approach for treatment of multiple neurological disorders.Pharmacology & therapeutics · 2017Review
- High-speed depolymerization at actin filament ends jointly catalysed by Twinfilin and Srv2/CAP.Nature cell biology · 2015Article
- Combinatorial genetic analysis of a network of actin disassembly-promoting factors.Cytoskeleton (Hoboken, N.J.) · 2015Article
- Actin and endocytosis in budding yeast.Genetics · 2015Review
- Structure and mechanism of mouse cyclase-associated protein (CAP1) in regulating actin dynamics.The Journal of biological chemistry · 2014Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
Recent evidence has suggested that Srv2/CAP (cyclase-associated protein) has two distinct functional roles in regulating actin turnover, with its N-terminus enhancing cofilin-mediated severing of actin filaments and its C-terminus catalyzing actin monomer recycling. However, it has remained unclear to what degree these two activities are coordinated by being linked in one molecule, or whether they can function autonomously. To address this, we physically divided the protein into two separate halves, N-Srv2 and C-Srv2, and asked whether they are able to function in trans both in living cells and in reconstituted assays for F-actin turnover and actin-based motility. Remarkably, in F-actin turnover assays the stimulatory effects of N-Srv2 and C-Srv2 functioning in trans were quantitatively similar to those of intact full-length Srv2. Further, in bead motility assays and in vivo, the fragments again functioned in trans, although not with the full effectiveness of intact Srv2. From these data, we conclude that the functions of the two halves of Srv2/CAP are largely autonomous, although their linkage improves coordination of the two functions in specific settings, possibly explaining why the linkage is conserved across distant plant, animal, and fungal species.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.