ArticleJournal of protein chemistry1994
Removal of the projection domain of microtubule-associated protein 2 alters its interaction with tubulin.
Article in Journal of protein chemistry, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
5 citing papers in PubMed, 11 citations in OpenAlex.
- Different effects of vinblastine on the polymerization of isotypically purified tubulins from bovine brain.Investigational new drugs · 2003Article
- Proteolysis of microtubule associated protein 2 and sensitivity of pancreatic tumours to docetaxel.British journal of cancer · 2000Article
- Pregnenolone binds to microtubule-associated protein 2 and stimulates microtubule assembly.Proceedings of the National Academy of Sciences of the United States of America · 2000Article
- Tau expression in model adenocarcinomas correlates with docetaxel sensitivity in tumour-bearing mice.British journal of cancer · 1998Article
- The Drosophila gene abnormal spindle encodes a novel microtubule-associated protein that associates with the polar regions of the mitotic spindle.The Journal of cell biology · 1997Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Microtubule-associated proteins (MAPs) can promote microtubule assembly in vitro. One of these MAPs (MAP2) consists of a short promoter domain which binds to the microtubule and promotes assembly and a long projection domain which projects out from the microtubule and may interact with other cytoskeletal elements. We have previously shown that MAP2 and another MAP, tau, differ in their interactions with tubulin in that tau, but not MAP2, promotes extensive aggregation of tubulin into spiral clusters in the presence of vinblastine and that microtuubles formed with MAP2 are more resistant than those formed with tau to the antimitotic drug maytansine [Luduena, R. F., et al. (1984), J. Biol. Chem. 259, 12890-12898; Fellous, A., et al. (1985), Cancer Res. 45, 5004-5010]. Here we have used chymotryptic digestion to remove the projection domain of MAP2 and examined the interaction of the digested MAP2 (ctMAP2) with tubulin in the presence of vinblastine and maytansine. We have found that ctMAP2 behaves very much like tau, but not like undigested MAP2, in the presence of vinblastine, in that ctMAP2 causes tubulin to polymerize into large clusters of spirals. In contrast, microtubule assembly in the presence of ctMAP2 is much more resistant to maytansine inhibition than is assembly in the presence of tau or undigested MAP2. Our results suggest that the projection domain of MAP2 may play a role in the interaction of tubulin with MAP2 during microtubule assembly.
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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.