ArticleThe Journal of biological chemistry2013
Structural basis for the association of MAP6 protein with microtubules and its regulation by calmodulin.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 28 citations in OpenAlex.
- Microtubule-Associated Proteins: From Dynamic Regulation of Microtubules to Cellular Architecture.Cells · 2026Review
- Lithium-induced neuroprotection in bipolar disorder: Translational insights into cytoskeletal and proteomic mechanisms.IBRO neuroscience reports · 2025Review
- Discovering functional interactions among schizophrenia-risk genes by combining behavioral genetics with cell biology.Neuroscience and biobehavioral reviews · 2024Review
- Antagonistic roles of tau and MAP6 in regulating neuronal development.Journal of cell science · 2024Article
- A cytoskeleton-membrane interaction conserved in fast-spiking neurons controls movement, emotion, and memory.Molecular psychiatry · 2023Article
- Article
- Experience-Regulated Neuronal Signaling in Maternal Behavior.Frontiers in molecular neuroscience · 2022Review
- Beyond Neuronal Microtubule Stabilization: MAP6 and CRMPS, Two Converging Stories.Frontiers in molecular neuroscience · 2021Article
- Epothilone D alters normal growth, viability and microtubule dependent intracellular functions of cortical neurons in vitro.Scientific reports · 2020Article
- Tau: It's Not What You Think.Trends in cell biology · 2019Review
- Role of Microtubule-Associated Protein in Autism Spectrum Disorder.Neuroscience bulletin · 2018Review
- ReMAPping the microtubule landscape: How phosphorylation dictates the activities of microtubule-associated proteins.Developmental dynamics : an official publication of the American Association of Anatomists · 2018Review
- Identification of novel Ack1-interacting proteins and Ack1 phosphorylated sites in mouse brain by mass spectrometry.Oncotarget · 2017Article
- Neurobiology of axonal transport defects in motor neuron diseases: Opportunities for translational research?Neurobiology of disease · 2017Review
- Potential Role of Microtubule Stabilizing Agents in Neurodevelopmental Disorders.International journal of molecular sciences · 2017Review
- Spindle function in Xenopus oocytes involves possible nanodomain calcium signaling.Molecular biology of the cell · 2016Article
- Parvulin 17-catalyzed Tubulin Polymerization Is Regulated by Calmodulin in a Calcium-dependent Manner.The Journal of biological chemistry · 2015Article
- A novel ER-microtubule-binding protein, ERLIN2, stabilizes Cyclin B1 and regulates cell cycle progression.Cell discovery · 2015Article
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Authors and funding
9 authors at 6 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Microtubules are highly dynamic αβ-tubulin polymers. In vitro and in living cells, microtubules are most often cold- and nocodazole-sensitive. When present, the MAP6/STOP family of proteins protects microtubules from cold- and nocodazole-induced depolymerization but the molecular and structure determinants by which these proteins stabilize microtubules remain under debate. We show here that a short protein fragment from MAP6-N, which encompasses its Mn1 and Mn2 modules (MAP6(90-177)), recapitulates the function of the full-length MAP6-N protein toward microtubules, i.e. its ability to stabilize microtubules in vitro and in cultured cells in ice-cold conditions or in the presence of nocodazole. We further show for the first time, using biochemical assays and NMR spectroscopy, that these effects result from the binding of MAP6(90-177) to microtubules with a 1:1 MAP6(90-177):tubulin heterodimer stoichiometry. NMR data demonstrate that the binding of MAP6(90-177) to microtubules involve its two Mn modules but that a single one is also able to interact with microtubules in a closely similar manner. This suggests that the Mn modules represent each a full microtubule binding domain and that MAP6 proteins may stabilize microtubules by bridging tubulin heterodimers from adjacent protofilaments or within a protofilament. Finally, we demonstrate that Ca(2+)-calmodulin competes with microtubules for MAP6(90-177) binding and that the binding mode of MAP6(90-177) to microtubules and Ca(2+)-calmodulin involves a common stretch of amino acid residues on the MAP6(90-177) side. This result accounts for the regulation of microtubule stability in cold condition by Ca(2+)-calmodulin.
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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.