ArticleThe Journal of cell biology1976
The role of actin in the temperature-dependent gelation and contraction of extracts of Acanthamoeba.
Article in The Journal of cell biology, 1976. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.
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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
68 citing papers in PubMed, 217 citations in OpenAlex.
- Article
- Rheology in the Biological Sciences.Rheology bulletin · 2024Article
- Temperature-dependent structural plasticity of hippocampal synapses.Frontiers in cellular neuroscience · 2022Article
- Review
- Actin Cytoskeletal Reorganization Function of JRAB/MICAL-L2 Is Fine-tuned by Intramolecular Interaction between First LIM Zinc Finger and C-terminal Coiled-coil Domains.Scientific reports · 2019Article
- Cellulose fibrils formation and organisation of cytoskeleton during encystment are essential for Acanthamoeba cyst wall architecture.Scientific reports · 2019Article
- Article
- In vitro efficacies of clinically available drugs against growth and viability of an Acanthamoeba castellanii keratitis isolate belonging to the T4 genotype.Antimicrobial agents and chemotherapy · 2013Article
- Molecular control of animal cell cytokinesis.Nature cell biology · 2012Review
- Actin behavior in bulk cytoplasm is cell cycle regulated in early vertebrate embryos.Journal of cell science · 2011Article
- Extraction and assembly of tissue-derived gels for cell culture and tissue engineering.Tissue engineering. Part C, Methods · 2009Article
- A quantitative analysis of contractility in active cytoskeletal protein networks.Biophysical journal · 2008Article
- Hypothermia-associated loss of dendritic spines.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2004Article
- Drosophila Kelch regulates actin organization via Src64-dependent tyrosine phosphorylation.The Journal of cell biology · 2002Article
- Microtubules remodel actomyosin networks in Xenopus egg extracts via two mechanisms of F-actin transport.The Journal of cell biology · 2000Article
- Central root cap cells are depleted of endoplasmic microtubules and actin microfilament bundles: implications for their role as gravity-sensing statocytes.Protoplasma · 1997Article
- Hypertension-associated point mutations in the adducin alpha and beta subunits affect actin cytoskeleton and ion transport.The Journal of clinical investigation · 1996Article
- The role of solation-contraction coupling in regulating stress fiber dynamics in nonmuscle cells.The Journal of cell biology · 1991Article
- Stopped-flow measurement of cytoskeletal contraction: Dictyostelium myosin II is specifically required for contraction of amoeba cytoskeletons.The Journal of cell biology · 1991Article
- Modulation of contraction by gelation/solation in a reconstituted motile model.The Journal of cell biology · 1991Article
8 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The temperature-dependent assembly and the interaction of Acanthamoeba contractile proteins have been studied in a crude extract. A cold extract of soluble proteins from Acanthamoeba castellanii is prepared by homogenizing the cells in a sucrose-ATP-ethyleneglycol-bis-(beta-aminoethyl ether) N,N'-tetraacetic acid buffer and centrifuging at 136,000 g for 1 h. When this supernate of soluble proteins is warmed to room temperature, it forms a solid gel. Upon standing at room temperature, the gel slowly contracts and squeezes out soluble components. The rates of gelation and contraction are both highly temperature dependent, with activation energies of about 20 kcal per mol. Gel formation is dependent upon the presence of ATP and Mg++. Low concentrations of Ca++ accelerate the contractile phase of this phenomenon. The major protein component of the gel is actin. It is associated with myosin, cofactor, a high molecular weight protein tentatively identfied as actin-binding protein, and several other unidentified proteins. Actin has been purified from these gels and was found to be capable of forming a solid gel when polymerized in the presence of ATP, MgCl3, and KCL. The rate of purified actin polymerication is very temperature dependent and is accelerated by the addition of fragments of muscle actin filaments. These data suggest that Acanthamoeba contractile proteins have a dual role in the cell; they may generate the forces for cellular movements and also act as cytoskeletal elements by controlling the consistency of the cytoplasm.
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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.