ArticleMolecular biology of the cell2000
Phosphorylation-dependent localization of microtubule-associated protein MAP2c to the actin cytoskeleton.
Article in Molecular biology of the cell, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 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
48 citing papers in PubMed, 124 citations in OpenAlex.
- Exploring the potential role of microtubule associated proteins-2 in the pathogenesis of HIV associated neurocognitive disorders.Neurotoxicity research · 2025Review
- MAP2 phosphorylation: mechanisms, functional consequences, and emerging insights.Frontiers in cellular neuroscience · 2025Review
- Amyloid-β and Phosphorylated Tau are the Key Biomarkers and Predictors of Alzheimer's Disease.Aging and disease · 2024Review
- Protein complexes from mouse and chick brain that interact with phospho-KXGS motif tau/microtubule associated protein antibody.Biology open · 2024Article
- MARCKS and PI(4,5)PMolecular biology of the cell · 2024Article
- Temporal Quantitative Proteomic and Phosphoproteomic Profiling of SH-SY5Y and IMR-32 Neuroblastoma Cells during All-International journal of molecular sciences · 2024Article
- Tubulin Complexity in Cancer and Metastasis.Advances in experimental medicine and biology · 2024Review
- Differential regulation of MAP2 by phosphorylation events in proline-rich versus C-terminal domains.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2023Article
- More than a marker: potential pathogenic functions of MAP2.Frontiers in molecular neuroscience · 2022Article
- Beyond Neuronal Microtubule Stabilization: MAP6 and CRMPS, Two Converging Stories.Frontiers in molecular neuroscience · 2021Article
- Melatonin Rescues the Dendrite Collapse Induced by the Pro-Oxidant Toxin Okadaic Acid in Organotypic Cultures of Rat Hilar Hippocampus.Molecules (Basel, Switzerland) · 2020Article
- MAP4 as a New Candidate in Cardiovascular Disease.Frontiers in physiology · 2020Review
- Structure and Functions of Microtubule Associated Proteins Tau and MAP2c: Similarities and Differences.Biomolecules · 2019Review
- AMPK-dependent phosphorylation of cingulin reversibly regulates its binding to actin filaments and microtubules.Scientific reports · 2018Article
- Article
- Functionally specific binding regions of microtubule-associated protein 2c exhibit distinct conformations and dynamics.The Journal of biological chemistry · 2018Article
- Consistent prediction of GO protein localization.Scientific reports · 2018Article
- 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
- Quantitative mapping of microtubule-associated protein 2c (MAP2c) phosphorylation and regulatory protein 14-3-3ζ-binding sites reveals key differences between MAP2c and its homolog Tau.The Journal of biological chemistry · 2017Article
- Distinct Features of Doublecortin as a Marker of Neuronal Migration and Its Implications in Cancer Cell Mobility.Frontiers in molecular neuroscience · 2017Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Microtubule-associated protein 2 (MAP2) is a neuronal phosphoprotein that promotes net microtubule growth and actin cross-linking and bundling in vitro. Little is known about MAP2 regulation or its interaction with the cytoskeleton in vivo. Here we investigate the in vivo function of three specific sites of phosphorylation on MAP2. cAMP-dependent protein kinase activity disrupts the MAP2-microtubule interaction in living HeLa cells and promotes MAP2c localization to peripheral membrane ruffles enriched in actin. cAMP-dependent protein kinase phosphorylates serines within three KXGS motifs, one within each tubulin-binding repeat. These highly conserved motifs are also found in homologous proteins tau and MAP4. Phosphorylation at two of these sites was detected in brain tissue. Constitutive phosphorylation at these sites was mimicked by single, double, and triple mutations to glutamic acid. Biochemical and microscopy-based assays indicated that mutation of a single residue was adequate to disrupt the MAP2-microtubule interaction in HeLa cells. Double or triple point mutation promoted MAP2c localization to the actin cytoskeleton. Specific association between MAP2c and the actin cytoskeleton was demonstrated by retention of MAP2c-actin colocalization after detergent extraction. Specific phosphorylation states may enhance the interaction of MAP2 with the actin cytoskeleton, thereby providing a regulated mechanism for MAP2 function within distinct cytoskeletal domains.
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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.