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Loss of the Golgi-localized v-ATPase subunit does not alter insulin granule formation or pancreatic islet β-cell function
Journal article   Peer reviewed

Loss of the Golgi-localized v-ATPase subunit does not alter insulin granule formation or pancreatic islet β-cell function

Cierra K Boyer, Sandra E Blom, Ashleigh E Machado, Kristen E Rohli, Michelle E Maxson and Samuel B Stephens
American journal of physiology: endocrinology and metabolism, Vol.326(3), pp.E245-E257
03/01/2024
DOI: 10.1152/ajpendo.00342.2023
PMCID: PMC11193524
PMID: 38265287
url
https://www.ncbi.nlm.nih.gov/pmc/articles/11193524View
Open Access

Abstract

Delayed Golgi export of proinsulin has recently been identified as an underlying mechanism leading to insulin granule loss and β-cell secretory defects in Type 2 diabetes (T2D). Because acidification of the Golgi lumen is critical for proinsulin sorting and delivery into the budding secretory granule, we reasoned that dysregulation of Golgi pH may contribute to proinsulin trafficking defects. In this report, we examined pH regulation of the Golgi and identified a partial alkalinization of the Golgi lumen in a diabetes model. To further explore this, we generated a β-cell specific KO of the v0a2 subunit of the v-ATPase pump, which anchors the v-ATPase to the Golgi membrane. While loss of v0a2 partially neutralized Golgi pH and was accompanied by distension of the Golgi cisternae, proinsulin export from the Golgi and insulin granule formation were not affected. Furthermore, β-cell function was well-preserved. β-cell v0a2 KO mice exhibited normal glucose tolerance in both sexes, no genotypic difference to diet-induced obesity, and normal insulin secretory responses. Collectively, our data demonstrate the v0a2 subunit contributes to β-cell Golgi pH regulation but suggest that additional disturbances to Golgi structure and function contribute to proinsulin trafficking defects in diabetes.
proinsulin trafficking Golgi insulin granule beta-cell v-ATPase

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