Evidence map›Paper›PMID 20979614›Full record

ArticleBMC biochemistry2010

Regulation of Ack1 localization and activity by the amino-terminal SAM domain.

Victoria Prieto-Echagüe, Azad Gucwa, Deborah A Brown, W Todd Miller

Open access · hybridAbstract read
In one paragraph

Article in BMC biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
0.9field-weighted citation impact, top 26% of its field
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

20 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. Article
  20. Regulation of ack-family nonreceptor tyrosine kinases.Journal of signal transduction · 2011
    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

4 authors at 1 institution in 1 country.

Victoria Prieto-EchagüeDepartment of Physiology and Biophysics, School of Medicine, Stony Brook University, Stony Brook, NY 11794-8661, USA.
Azad Gucwa
Deborah A Brown
W Todd Miller
Stony Brook University · US

Funding

Regulation of insulin-like growth factor I receptor tyrosine kinaseR01CA122091 · NCI · STATE UNIVERSITY NEW YORK STONY BROOK · PI MILLER, W TODD · 2008 to 2011
$1.2M
NCI NIH HHS CA122091NCI NIH HHS R01 CA122091
6 · The paper itself

Abstract

backgroundThe mechanisms that regulate the activity of the nonreceptor tyrosine kinase Ack1 (activated Cdc42-associated kinase) are poorly understood. The amino-terminal region of Ack1 is predicted to contain a sterile alpha motif (SAM) domain. SAM domains share a common fold and mediate protein-protein interactions in a wide variety of proteins. Here, we addressed the importance of the Ack1 SAM domain in kinase activity.

resultsWe used immunofluorescence and Western blotting to show that Ack1 deletion mutants lacking the N-terminus displayed significantly reduced autophosphorylation in cells. A minimal construct comprising the N-terminus and kinase domain (NKD) was autophosphorylated, while the kinase domain alone (KD) was not. When expressed in mammalian cells, NKD localized to the plasma membrane, while KD showed a more diffuse cytosolic localization. Co-immunoprecipitation experiments showed a stronger interaction between full length Ack1 and NKD than between full length Ack1 and KD, indicating that the N-terminus was important for Ack1 dimerization. Increasing the local concentration of purified Ack1 kinase domain at the surface of lipid vesicles stimulated autophosphorylation and catalytic activity, consistent with a requirement for dimerization and trans-phosphorylation for activity.

conclusionsCollectively, the data suggest that the N-terminus of Ack1 promotes membrane localization and dimerization to allow for autophosphorylation.

Indexed as

Amino Acid SequenceAnimalsBlotting, WesternCell MembraneChlorocebus aethiopsCOS CellsFluorescent Antibody TechniqueIntracellular SpacePhosphorylationProtein MultimerizationProtein Structure, QuaternaryProtein Structure, TertiaryProtein TransportProtein-Tyrosine KinasesSequence DeletionProtein-Tyrosine Kinases

Identifiers

PMID20979614
PMCPMC2987765
OpenAlexW2039377638

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.