Evidence map›Paper›PMID 20208071›Full record

ArticleThe Journal of biological chemistry2010

Phosphorylation within the MafA N terminus regulates C-terminal dimerization and DNA binding.

Shuangli Guo, Nathan L Vanderford, Roland Stein

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.5field-weighted citation impact, top 17% 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

21 citing papers in PubMed, 30 citations in OpenAlex.

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  9. Proceedings of the National Academy of Sciences of the United States of America · 2018
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  20. MafA and MafB activity in pancreatic β cells.Trends in endocrinology and metabolism: TEM · 2011
    Review
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

3 authors at 1 institution in 1 country.

Shuangli GuoFrom the Department of Molecular Physiology and Biophysics, Vanderbilt University Medical Center, Nashville, Tennessee 37232.
Nathan L Vanderford
Roland Stein
Vanderbilt University Medical Center · US

Funding

TRANSGENIC MOUSE/ ES CELL SHARES RESOURCESP60DK020593 · NIDDK · VANDERBILT UNIVERSITY · PI POWERS, ALVIN C · 1986 to 2011
$28.1M
Translational Research in Endocrinology And Diabetes (TREAD)T32DK007061 · NIDDK · VANDERBILT UNIVERSITY MEDICAL CENTER · PI Sarah S Jaser, KEVIN D NISWENDER · 1986 to 2026
$8.0M
TRANSGENIC MICE COREP01DK042502 · NIDDK · VANDERBILT UNIVERSITY · PI MAGNUSON, MARK A · 1990 to 2000
$994k
NIDDK NIH HHS 5T32 DK007061-34NIDDK NIH HHS P01 DK042502NIDDK NIH HHS P01 DK42502NIDDK NIH HHS P60 DK020593NIDDK NIH HHS P60 DK20593NIDDK NIH HHS T32 DK007061
6 · The paper itself

Abstract

Phosphorylation regulates transcription factor activity by influencing dimerization, cellular localization, activation potential, and/or DNA binding. Nevertheless, precisely how this post-translation modification mediates these processes is poorly understood. Here, we examined the role of phosphorylation on the DNA-binding properties of MafA and MafB, closely related transcriptional activators of the basic-leucine zipper (b-Zip) family associated with cell differentiation and oncogenesis. Many common phosphorylation sites were identified by mass spectrometry. However, dephosphorylation only precluded the detection of MafA dimers and consequently dramatically reduced DNA-binding ability. Analysis of MafA/B chimeras revealed that sensitivity to the phosphorylation status of MafA was imparted by sequences spanning the C-terminal dimerization region (amino acids (aa) 279-359), whereas the homologous MafB region (aa 257-323) conveyed phosphorylation-independent DNA binding. Mutational analysis showed that formation of MafA dimers capable of DNA binding required phosphorylation within the distinct N-terminal transactivation domain (aa 1-72) and not the C-terminal b-Zip region. These results demonstrate a novel relationship between the phosphoamino acid-rich transactivation and b-Zip domains in controlling MafA DNA-binding activity.

Indexed as

AnimalsCell DifferentiationDNAHeLa CellsHumansMafB Transcription FactorMaf Transcription Factors, LargeMicePhosphorylationProtein BindingProtein MultimerizationProtein Processing, Post-TranslationalProtein Structure, TertiaryRecombinant Fusion ProteinsDNAMAFA protein, humanMafa protein, mouseMAFB protein, humanMafb protein, mouseMafB Transcription FactorMaf Transcription Factors, LargeRecombinant Fusion Proteins

Identifiers

PMID20208071
PMCPMC2857093
OpenAlexW2057884946

What OpenQuestion holds

Textmetadata
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.