ArticleThe Journal of biological chemistry2012
MAP6-F is a temperature sensor that directly binds to and protects microtubules from cold-induced depolymerization.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed.
- SPACA9 and MNMIP1 bridge the seam of spermatid manchette microtubules.The EMBO journal · 2026Article
- Loss-of-function variants in SAXO6, encoding a microtubule inner protein of photoreceptor cilia, cause a late-onset retinal dystrophy.American journal of human genetics · 2026Article
- Thermosensitivity of TREK K2P channels is controlled by a PKA switch and depends on the microtubular network.Pflugers Archiv : European journal of physiology · 2025Article
- Article
- Cold-induced meiotic nondisjunction inmicroPublication biology · 2025Article
- Direct targeting of host microtubule and actin cytoskeletons by a chlamydial pathogenic effector protein.Journal of cell science · 2024Article
- Transcriptomic Networks Reveal the Tissue-Specific Cold Shock Responses in Japanese Flounder (Biology · 2023Article
- Cellular cartography: Towards an atlas of the neuronal microtubule cytoskeleton.Frontiers in cell and developmental biology · 2023Review
- A cryo-ET survey of microtubules and intracellular compartments in mammalian axons.The Journal of cell biology · 2022Article
- Functional implication of heat shock protein 70/90 and tubulin in cold stress of Dermacentor silvarum.Parasites & vectors · 2021Article
- The microtubule cytoskeleton at the synapse.Neuroscience letters · 2021Review
- Beyond Neuronal Microtubule Stabilization: MAP6 and CRMPS, Two Converging Stories.Frontiers in molecular neuroscience · 2021Article
- MicroRNA dynamics during hibernation of the Australian central bearded dragon (Pogona vitticeps).Scientific reports · 2020Article
- Article
- Cytoskeletal organization of axons in vertebrates and invertebrates.The Journal of cell biology · 2020Article
- MAP6 is an intraluminal protein that induces neuronal microtubules to coil.Science advances · 2020Article
- Microtubules Increase Diastolic Stiffness in Failing Human Cardiomyocytes and Myocardium.Circulation · 2020Article
- MAP4 as a New Candidate in Cardiovascular Disease.Frontiers in physiology · 2020Review
- Tau: It's Not What You Think.Trends in cell biology · 2019Review
- Deletion of the microtubule-associated protein 6 (MAP6) results in skeletal muscle dysfunction.Skeletal muscle · 2018Article
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Authors and funding
11 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Microtubules are dynamic structures that present the peculiar characteristic to be ice-cold labile in vitro. In vivo, microtubules are protected from ice-cold induced depolymerization by the widely expressed MAP6/STOP family of proteins. However, the mechanism by which MAP6 stabilizes microtubules at 4 °C has not been identified. Moreover, the microtubule cold sensitivity and therefore the needs for microtubule stabilization in the wide range of temperatures between 4 and 37 °C are unknown. This is of importance as body temperatures of animals can drop during hibernation or torpor covering a large range of temperatures. Here, we show that in the absence of MAP6, microtubules in cells below 20 °C rapidly depolymerize in a temperature-dependent manner whereas they are stabilized in the presence of MAP6. We further show that in cells, MAP6-F binding to and stabilization of microtubules is temperature- dependent and very dynamic, suggesting a direct effect of the temperature on the formation of microtubule/MAP6 complex. We also demonstrate using purified proteins that MAP6-F binds directly to microtubules through its Mc domain. This binding is temperature-dependent and coincides with progressive conformational changes of the Mc domain as revealed by circular dichroism. Thus, MAP6 might serve as a temperature sensor adapting its conformation according to the temperature to maintain the cellular microtubule network in organisms exposed to temperature decrease.
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