Carboxyl-Methylation of Rab3D in the Rat Pancreatic Acinar Tumor Cell Line AR42J

Qiu, Xuan; Valentijn, Jack A.; Jamieson, James D.

doi:10.1006/bbrc.2001.5224

Cited by 13 publications

(10 citation statements)

References 29 publications

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“…Thus, Rab3B and Rab3D might be important for exocrine secretory function of AR42J cells. In agreement with our data, dexamethasone-induced upregulation of Rab3B and Rab3D immunoreactivity was published during finishing the present study (32). In our previous study using full-length Rab3 cDNAs as probes in the Northern blot analysis, we found that dexamethasone caused up-regulation of Rab3B only, whereas the three other Rab3 isoforms were found down-regulated at the mRNA level (22).…”

Section: Discussionsupporting

confidence: 93%

Subcellular Distribution and Function of Rab3A-D in Pancreatic Acinar AR42J Cells

Piiper

Leser

Lutz

et al. 2001

Biochemical and Biophysical Research Communications

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Section: Discussionsupporting

confidence: 93%

Subcellular Distribution and Function of Rab3A-D in Pancreatic Acinar AR42J Cells

Piiper

Leser

Lutz

et al. 2001

Biochemical and Biophysical Research Communications

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“…Rab3D, as well as the other three Rab3 isoforms (A, B and C), are all expressed in AR42J cells [23,28]. Moreover, Rab3D is upregulated in response to Dex treatment, suggesting a role for this protein in AR42J cells as they develop a more acinar cell-like phenotype [28][29][30]. The aim of the present study was to examine the role of Rab3D in AR42J cells.…”

Section: Introductionmentioning

confidence: 93%

Rab3D regulates amylase levels, not agonist-induced amylase release, in AR42J cells

Limi

Ojakian

Raffaniello

2012

Cellular and Molecular Biology Letters

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Rab3D is a low molecular weight GTP-binding protein that associates with secretory granules in exocrine cells. AR42J cells are derived from rat pancreatic exocrine tumor cells and develop an acinar cell-like phenotype when treated with dexamethasone (Dex). In the present study, we examined the role of Rab3D in Dex-treated AR42J cells. Rab3D expression and localization were analyzed by subcellular fractionation and immunoblotting. The role of Rab3D was examined by overexpressing myc-labeled wild-type-Rab3D and a constitutively active form of Rab3D (Rab3D-Q81L) in AR42J cells. We found that Rab3D is predominantly membrane-associated in AR42J cells and co-localizes with zymogen granules (ZG). Following CCK-8-induced exocytosis, amylase-positive ZGs appeared to move towards the periphery of the cell and co-localization between Rab3D and amylase was less complete when compared to basal conditions. Overexpression of WT, but not mutant Rab3D, resulted in an increase in cellular amylase levels. Overexpression of mutant and WT Rab3D did not affect granule morphology, CCK-8-induced secretion, longterm (48 hr) basal amylase release or granule density. We conclude that Rab3D is not involved in agonist-induced exocytosis in AR42J cells. Instead, Rab3D may regulate amylase content in these cells.

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“…We next decided to investigate RAB26 scalability in a cell culture system that would facilitate analysis of RAB26 expression level relative to its subcellular distribution and function. First, we analyzed the wellestablished secretory pancreatic cell line, AR42J, which expresses MIST1 (Jia et al, 2008) and can be differentiated with dexamethasone treatment to upregulate MIST1 target gene expression (Limi et al, 2012;Qiu et al, 2001) and increase amylase-containing secretory vesicles (Logsdon, 1986;Rinn et al, 2012) (Fig. 1D).…”

Section: Introductionmentioning

confidence: 99%

RAB26 coordinates lysosome traffic and mitochondrial localization

Jin

Mills

2014

Journal of Cell Science

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As they mature, professional secretory cells like pancreatic acinar and gastric chief cells induce the transcription factor MIST1 (also known as BHLHA15) to substantially scale up production of large secretory granules in a process that involves expansion of apical cytoplasm and redistribution of lysosomes and mitochondria. How a scaling factor like MIST1 rearranges cellular architecture simply by regulating expression levels of its transcriptional targets is unknown. RAB26 is a MIST1 target whose role in MIST1-mediated secretory cell maturation is also unknown. Here, we confirm that RAB26 expression, unlike most Rabs which are ubiquitously expressed, is tissue specific and largely confined to MIST1-expressing secretory tissues. Surprisingly, functional studies showed that RAB26 predominantly associated with LAMP1/cathepsin D lysosomes and not directly with secretory granules. Moreover, increasing RAB26 expression -by inducing differentiation of zymogensecreting cells or by direct transfection -caused lysosomes to coalesce in a central, perinuclear region. Lysosome clustering in turn caused redistribution of mitochondria into distinct subcellular neighborhoods. The data elucidate a novel function for RAB26 and suggest a mechanism for how cells could increase transcription of key effectors to reorganize subcellular compartments during differentiation.

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Carboxyl-Methylation of Rab3D in the Rat Pancreatic Acinar Tumor Cell Line AR42J

Cited by 13 publications

References 29 publications

Subcellular Distribution and Function of Rab3A-D in Pancreatic Acinar AR42J Cells

Subcellular Distribution and Function of Rab3A-D in Pancreatic Acinar AR42J Cells

Rab3D regulates amylase levels, not agonist-induced amylase release, in AR42J cells

RAB26 coordinates lysosome traffic and mitochondrial localization

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