ArticleThe Journal of biological chemistry2010
Differential effects of caldesmon on the intermediate conformational states of polymerizing actin.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 17 citations in OpenAlex.
- Multiple Mechanisms to Regulate Actin Functions: "Fundamental" Versus Lineage-Specific Mechanisms and Hierarchical Relationships.Biomolecules · 2025Review
- Comprehensive Transcriptional Profiling of the Gastrointestinal Tract of Ruminants from Birth to Adulthood Reveals Strong Developmental Stage Specific Gene Expression.G3 (Bethesda, Md.) · 2019Article
- Actin binding domain of filamin distinguishes posterior from anterior actin filaments in migratingBiophysics and physicobiology · 2016Article
- Desmoplastic infantile ganglioglioma with late presentation. A clinical, radiological and histopathological analysis.The neuroradiology journal · 2013Article
- Disulfide cross-linked antiparallel actin dimer.Biochemistry · 2013Article
- The conformational state of actin filaments regulates branching by actin-related protein 2/3 (Arp2/3) complex.The Journal of biological chemistry · 2012Article
- Pyrene: a probe to study protein conformation and conformational changes.Molecules (Basel, Switzerland) · 2011Review
- Structural studies on maturing actin filaments.Bioarchitecture · 2011Article
- Histochemical localization of caldesmon in the CNS and ganglia of the mouse.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2011Article
- New insights into the regulation of the actin cytoskeleton by tropomyosin.International review of cell and molecular biology · 2010Review
- Segregated localization of two calponin-related proteins within sarcomeric thin filaments in Caenorhabditis elegans striated muscle.Cytoskeleton (Hoboken, N.J.)Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The actin-binding protein caldesmon (CaD) reversibly inhibits smooth muscle contraction. In non-muscle cells, a shorter CaD isoform co-exists with microfilaments in the stress fibers at the quiescent state, but the phosphorylated CaD is found at the leading edge of migrating cells where dynamic actin filament remodeling occurs. We have studied the effect of a C-terminal fragment of CaD (H32K) on the kinetics of the in vitro actin polymerization by monitoring the fluorescence of pyrene-labeled actin. Addition of H32K or its phosphorylated form either attenuated or accelerated the pyrene emission enhancement, depending on whether it was added at the early or the late phase of actin polymerization. However, the CaD fragment had no effect on the yield of sedimentable actin, nor did it affect the actin ATPase activity. Our findings can be explained by a model in which nascent actin filaments undergo a maturation process that involves at least two intermediate conformational states. If present at early stages of actin polymerization, CaD stabilizes one of the intermediate states and blocks the subsequent filament maturation. Addition of CaD at a later phase accelerates F-actin formation. The fact that CaD is capable of inhibiting actin filament maturation provides a novel function for CaD and suggests an active role in the dynamic reorganization of the actin cytoskeleton.
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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.