ArticleMolecular biology of the cell2019
Steric regulation of tandem calponin homology domain actin-binding affinity.
Article in Molecular biology of the cell, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- In silico conformational dynamics of the α-actinin-2 actin-binding domain upon phosphorylation.Biophysical journal · 2026Article
- FAST - filamentous actin segmentation tool for quantifying cytoskeletal organization.Journal of cell science · 2026Article
- Human Plastins are Novel Cytoskeletal pH Sensors with a Reduced F-actin Bundling Capacity at Basic pH.Journal of molecular biology · 2025Article
- Conserved function of the HAUS6 calponin homology domain in anchoring augmin for microtubule branching.Nature communications · 2025Article
- Spatial proteomics of ER tubules reveals CLMN, an ER-actin tether at focal adhesions that promotes cell migration.Cell reports · 2025Article
- Cellular mechanisms of traumatic brain injury.npj biological physics and mechanics · 2025Review
- Turn-on protein switches for controlling actin binding in cells.Nature communications · 2024Article
- The Shot CH1 domain recognises a distinct form of F-actin during Drosophila oocyte determination.Development (Cambridge, England) · 2024Article
- Spatial proteomics of ER tubules reveals CLMN, an ER-actin tether at focal adhesions that promotes cell migration.bioRxiv : the preprint server for biology · 2024Article
- Turn-On Protein Switches for Controlling Actin Binding in Cells.bioRxiv : the preprint server for biology · 2023Article
- Exploring the Role of the Plant Actin Cytoskeleton: From Signaling to Cellular Functions.International journal of molecular sciences · 2023Review
- Expression of genes regulating cell division in porcine follicular granulosa cells.Cell division · 2023Article
- Quantifying cytoskeletal organization from optical microscopy data.Frontiers in cell and developmental biology · 2023Review
- β-III-spectrin N-terminus is required for high-affinity actin binding and SCA5 neurotoxicity.Scientific reports · 2022Article
- Dynamics and Functional Interplay of Nonhistone Lysine Crotonylome and Ubiquitylome in Vascular Smooth Muscle Cell Phenotypic Remodeling.Frontiers in cardiovascular medicine · 2022Article
- Biased localization of actin binding proteins by actin filament conformation.Nature communications · 2020Article
- A Weak Link with Actin Organizes Tight Junctions to Control Epithelial Permeability.Developmental cell · 2020Article
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- Structural Characteristics, Binding Partners and Related Diseases of the Calponin Homology (CH) Domain.Frontiers in cell and developmental biology · 2020Review
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Authors and funding
7 authors.
Funding
Abstract
Tandem calponin homology (CH1-CH2) domains are common actin-binding domains in proteins that interact with and organize the actin cytoskeleton. Despite regions of high sequence similarity, CH1-CH2 domains can have remarkably different actin-binding properties, with disease-associated point mutants known to increase as well as decrease affinity for F-actin. To investigate features that affect CH1-CH2 affinity for F-actin in cells and in vitro, we perturbed the utrophin actin-binding domain by making point mutations at the CH1-CH2 interface, replacing the linker domain, and adding a polyethylene glycol (PEG) polymer to CH2. Consistent with a previous model describing CH2 as a steric negative regulator of actin binding, we find that utrophin CH1-CH2 affinity is both increased and decreased by modifications that change the effective "openness" of CH1 and CH2 in solution. We also identified interface mutations that caused a large increase in affinity without changing solution "openness," suggesting additional influences on affinity. Interestingly, we also observe nonuniform subcellular localization of utrophin CH1-CH2 that depends on the N-terminal flanking region but not on bulk affinity. These observations provide new insights into how small sequence changes, such as those found in diseases, can affect CH1-CH2 binding properties.
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