ArticleThe Journal of cell biology1990
Analysis of the primary sequence and microtubule-binding region of the Drosophila 205K MAP.
Article in The Journal of cell biology, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 42 citations in OpenAlex.
- Effects of three microtubule-associated proteins (MAP2, MAP4, and Tau) on microtubules' physical properties and neurite morphology.Scientific reports · 2023Article
- Site-specific microtubule-associated protein 4 dephosphorylation causes microtubule network densification in pressure overload cardiac hypertrophy.The Journal of biological chemistry · 2010Article
- Sequestration of Polo kinase to microtubules by phosphopriming-independent binding to Map205 is relieved by phosphorylation at a CDK site in mitosis.Genes & development · 2008Article
- Tumor suppressor RASSF1A is a microtubule-binding protein that stabilizes microtubules and induces G2/M arrest.Oncogene · 2004Article
- Flying through the drosophila cytoskeletal genome.The Journal of cell biology · 2000Review
- MHP1, an essential gene in Saccharomyces cerevisiae required for microtubule function.The Journal of cell biology · 1996Article
- The cell cycle-dependent localization of the CP190 centrosomal protein is determined by the coordinate action of two separable domains.The Journal of cell biology · 1995Article
- Stable expression of heterologous microtubule-associated proteins (MAPs) in Chinese hamster ovary cells: evidence for differing roles of MAPs in microtubule organization.The Journal of cell biology · 1994Article
- Identification and molecular characterization of E-MAP-115, a novel microtubule-associated protein predominantly expressed in epithelial cells.The Journal of cell biology · 1993Article
- Cell lineage-specific expression of modulo, a dose-dependent modifier of variegation in Drosophila.The EMBO journal · 1992Article
- Identification of ubiquitous high-molecular-mass, heat-stable microtubule-associated proteins (MAPs) that are related to the Drosophila 205-kDa MAP but are not related to the mammalian MAP-4.Proceedings of the National Academy of Sciences of the United States of America · 1992Article
- A novel microtubule-binding motif identified in a high molecular weight microtubule-associated protein from Trypanosoma brucei.The Journal of cell biology · 1992Article
- NuMA: an unusually long coiled-coil related protein in the mammalian nucleus.The Journal of cell biology · 1992Article
- Genetic analysis of a Drosophila microtubule-associated protein.The Journal of cell biology · 1992Article
- New nucleotide sequence data on the EMBL File Server.Nucleic acids research · 1991Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
We have sequenced cDNA clones encoding the Drosophila 205K microtubule-associated protein (MAP), a protein that may be the species specific homologue of mammalian MAP4. The peptide sequence deduced from the longest open-reading frame reveals a hydrophilic protein, which has basic and acidic regions that are similar in organization to mammalian MAP2. Using truncated forms of the 205K MAP, a 232-amino acid region could be defined that is necessary for microtubule binding. The amino acid sequence of this region shares no similarity with the binding motif of MAP2 or tau. We also analyzed several embryonic cDNA clones, which show the existence of differentially spliced mRNAs. Finally, we identified several potential protein kinase target sequences. One of these is distal to the microtubule-binding site and fits the phosphorylation consensus sequence of proteins phosphorylated by the mitosis specific protein kinase cdc2. Our data suggest that the 205K MAP uses a microtubule-binding motif unlike that found in other MAPs, and also raise the possibility that the activities of the 205K MAP may be regulated by alternative splicing and phosphorylation.
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