Evidence map›Paper›PMID 1907976›Full record

ArticleThe Journal of cell biology1991

Phosphorylation determines the binding of microtubule-associated protein 2 (MAP2) to microtubules in living cells.

B Brugg, A Matus

Abstract read
In one paragraph

Article in The Journal of cell biology, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

50 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. ReMAPping the microtubule landscape: How phosphorylation dictates the activities of microtubule-associated proteins.Developmental dynamics : an official publication of the American Association of Anatomists · 2018
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Spontaneous age-related neurite branching in Caenorhabditis elegans.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2011
    Article
  16. Synaptic activation modifies microtubules underlying transport of postsynaptic cargo.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  17. Article
  18. Article
  19. Uses for JNK: the many and varied substrates of the c-Jun N-terminal kinases.Microbiology and molecular biology reviews : MMBR · 2006
    Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

B BruggFriedrich Miescher Institute, Basel, Switzerland.
A Matus

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The influence of phosphorylation on the binding of microtubule-associated protein 2 (MAP2) to cellular microtubules was studied by microinjecting MAP2 in various phosphorylation states into rat-1 fibroblasts, which lack endogenous MAP2. Conventionally prepared brain MAP2, containing 10 mol of endogenous phosphate per mol (MAP2-P10), was completely bound to cellular microtubules within 2-3 min after injection. MAP2 prepared in the presence of phosphatase inhibitors, containing 25 mol/mol of phosphate (MAP2-P25), also bound completely. However, MAP2 whose phosphate content had been reduced to 2 mol phosphate per mol by treatment with alkaline phosphatase in vitro (MAP2-P2) did not initially bind to microtubules, suggesting that phosphorylation of certain sites in MAP2 is essential for binding to microtubules. MAP2-P10 was further phosphorylated in vitro via an endogenously bound protein kinase activity, adding 12 more phosphates, giving a total of 22 mol/mol. This preparation (MAP2-P10+12) also did not bind to microtubules. Assay of the binding of these preparations to taxol-stabilized tubulin polymers in vitro confirmed that their binding to tubulin depended on the state of phosphorylation, but the results obtained in microinjection experiments differed in some cases from in vitro binding. The results suggest that the site of phosphate incorporation rather than the amount is the critical factor in determining microtubule binding activity of MAP2. Furthermore, the interaction of MAP2 with cellular microtubules may be influenced by additional factors that are not evident in vitro.

Indexed as

AnimalsBrainCell LineFluorescent Antibody TechniqueMicrotubule-Associated ProteinsMicrotubulesNerve Tissue ProteinsPhosphorylationProtein BindingProtein KinasesRatstau ProteinsTubulinMicrotubule-Associated ProteinsNerve Tissue ProteinsProtein Kinasestau ProteinsTubulin

Identifiers

PMID1907976
PMCPMC2289883

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
Read underepoch 390

Registered trials

None linked

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.