Evidence map›Paper›PMID 18400053›Full record

ReviewJournal of cellular and molecular medicine2008

Emerging roles for protein histidine phosphorylation in cellular signal transduction: lessons from the islet beta-cell.

Anjaneyulu Kowluru

Open access · bronzeAbstract readReview
In one paragraph

Review in Journal of cellular and molecular medicine, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
3.4field-weighted citation impact, top 9% 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

12 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Review
  3. P-Rex1 Mediates Glucose-Stimulated Rac1 Activation and Insulin Secretion in Pancreatic β-Cells.Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology · 2020
    Article
  4. Review
  5. Review
  6. Review
  7. Article
  8. Article
  9. Review
  10. Article
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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

1 author at 1 institution in 1 country.

Anjaneyulu KowluruDepartment of Pharmaceutical Sciences, Eugene Applebaum College of Pharmacy and Health Sciences, Wayne State University, Detroit, MI 48201, USA. akowluru@med.wayne.edu
Eugene Applebaum College of Pharmacy and Health Sciences · US

Funding

Protein Prenyltransferases in Glucose-Stimulated Insulin SecretionR01DK074921 · NIDDK · WAYNE STATE UNIVERSITY · PI KOWLURU, ANJANEYULU · 2007 to 2010
$1.0M
ROLE OF PROTEIN PHOSPHATASES IN INSULIN SECRETIONR01DK056005 · NIDDK · WAYNE STATE UNIVERSITY · PI KOWLURU, ANJANEYULU · 2001 to 2004
$708k
NIDDK NIH HHS R01 DK056005NIDDK NIH HHS R01 DK074921NIDDK NIH HHS R01 DK 56005NIDDK NIH HHS R01 DK 74921
6 · The paper itself

Abstract

Protein phosphorylation represents one of the key regulatory events in physiological insulin secretion from the islet beta-cell. In this context, several classes of protein kinases (e.g. calcium-, cyclic nucleotide- and phospholipid-dependent protein kinases and tyrosine kinases) have been characterized in the beta-cell. The majority of phosphorylated amino acids identified include phosphoserine, phosphothreonine and phosphotyrosine. Protein histidine phosphorylation has been implicated in the prokaryotic and eukaryotic cellular signal transduction. Most notably, phoshohistidine accounts for 6% of total protein phosphorylation in eukaryotes, which makes it nearly 100-fold more abundant than phosphotyrosine, but less abundant than phosphoserine and phosphothreonine. However, very little is known about the number of proteins with phosphohistidines, since they are highly labile and are rapidly lost during phosphoamino acid identification under standard experimental conditions. The overall objectives of this review are to: (i) summarize the existing evidence indicating the subcellular distribution and characterization of various histidine kinases in the islet beta-cell, (ii) describe evidence for functional regulation of these kinases by agonists of insulin secretion, (iii) present a working model to implicate novel regulatory roles for histidine kinases in the receptor-independent activation, by glucose, of G-proteins endogenous to the beta-cell, (iv) summarize evidence supporting the localization of protein histidine phosphatases in the islet beta-cell and (v) highlight experimental evidence suggesting potential defects in the histidine kinase signalling cascade in islets derived from the Goto-Kakizaki (GK) rat, a model for type 2 diabetes. Potential avenues for future research to further decipher regulatory roles for protein histidine phosphorylation in physiological insulin secretion are also discussed.

Indexed as

AnimalsGTP-Binding ProteinsHistidineHumansInsulinInsulin-Secreting CellsInsulin SecretionModels, BiologicalNucleoside-Diphosphate KinasePhosphorylationProteinsSignal TransductionGTP-Binding ProteinsHistidineInsulinNucleoside-Diphosphate KinaseProteins

Identifiers

PMID18400053
PMCPMC4506158
OpenAlexW1550128439

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.