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2008 ; 12
(5B
): 1885-908
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Emerging roles for protein histidine phosphorylation in cellular signal
transduction: lessons from the islet beta-cell
#MMPMID18400053
Kowluru A
J Cell Mol Med
2008[Oct]; 12
(5B
): 1885-908
PMID18400053
show ga
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.
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