The expression and localization of Prune2 mRNA in the central nervous system

Li, Shimo; Itoh, Masanori; Ohta, Kazunori; Ueda, Masashi; Mizuno, Akihito; Ohta, Emi; Hida, Yoko; Wang, Miao-xing; Takeuchi, Kazunori; Nakagawa, Toshiyuki

doi:10.1016/j.neulet.2011.08.037

Cited by 9 publications

(7 citation statements)

References 33 publications

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“…4B). Prune2 is also highly expressed in the central nervous system (Li et al, 2011) but its function remains poorly characterized, and a role for Prune2 in adipocytes has not been previously described. In contrast to both the BAT and pgWAT comparisons, we found many more UCP1-TRAP-Seq iWAT-selective genes (Group 3) enriched in UCP1-TRAP versus Adipoq-TRAP (Fig.…”

Section: Resultsmentioning

confidence: 99%

A Smooth Muscle-Like Origin for Beige Adipocytes

et al. 2014

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SUMMARY Thermogenic UCP1-positive cells, which include brown and beige adipocytes, transform chemical energy into heat and increase whole body energy expenditure. Using a selective translational profiling approach, we present a comprehensive molecular description of brown and beige gene expression in vivo. This UCP1-TRAP dataset demonstrates striking similarities and important differences between these cell types, including a smooth muscle-like signature expressed by beige, but not classical brown adipocytes. In vivo fate mapping demonstrates that at least a subset of beige cells arise from a smooth muscle-like origin. Finally, ectopic expression of PRDM16 converts bona fide vascular smooth muscle cells into Ucp1-positive adipocytes in vitro. These results establish a portrait of brown and beige adipocyte gene expression in vivo and identify a previously unrecognized origin for beige cells.

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Section: Resultsmentioning

confidence: 99%

A Smooth Muscle-Like Origin for Beige Adipocytes

et al. 2014

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“…BMCC1 ( B cl2, the adenovirus E1B 19 kDa interacting protein 2 and the Cdc42 GAP homology BCH m otif- c ontaining molecule at the c arboxy-terminal region 1 ), also called PRUNE2, is a large molecule highly expressed in the brain as well as in spinal cord and dorsal root ganglia [12]–[14]. Overexpression of one of its isoforms, BNIP-XL (for BNIP-2 Extra Long), has been shown to promote the formation of short membrane protrusions, to inhibit RhoA and to suppress cell transformation initiated by Lbc, a RhoA-specific guanine nucleotide exchange factor [15].…”

Section: Introductionmentioning

confidence: 99%

Bmcc1s, a Novel Brain-Isoform of Bmcc1, Affects Cell Morphology by Regulating MAP6/STOP Functions

et al. 2012

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The BCH (BNIP2 and Cdc42GAP Homology) domain-containing protein Bmcc1/Prune2 is highly enriched in the brain and is involved in the regulation of cytoskeleton dynamics and cell survival. However, the molecular mechanisms accounting for these functions are poorly defined. Here, we have identified Bmcc1s, a novel isoform of Bmcc1 predominantly expressed in the mouse brain. In primary cultures of astrocytes and neurons, Bmcc1s localized on intermediate filaments and microtubules and interacted directly with MAP6/STOP, a microtubule-binding protein responsible for microtubule cold stability. Bmcc1s overexpression inhibited MAP6-induced microtubule cold stability by displacing MAP6 away from microtubules. It also resulted in the formation of membrane protrusions for which MAP6 was a necessary cofactor of Bmcc1s. This study identifies Bmcc1s as a new MAP6 interacting protein able to modulate MAP6-induced microtubule cold stability. Moreover, it illustrates a novel mechanism by which Bmcc1 regulates cell morphology.

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“…Evidence for the expression of the full length BMCC1-1 transcript spanning the c9orf65 and BNIPXL genes was provided by Iwama et al [8], who cloned a full-length cDNA from Hela cells. In this study and subsequently, BMCC1 transcripts have been detected in restricted regions of the mouse brain [8,9]. Clarke et al [5] demonstrated that BMCC1 RNA expression is elevated in prostate cancer and metastases compared with benign tissue, indicating that BMCC1 may be functioning differently in different cancers and tissue types.…”

Section: Introductionmentioning

confidence: 57%

“…Machida et al [7] used semi-quantitative RT-PCR to describe widespread expression of BMCC1 in tissues including the nervous system and variable expression in a variety of tumour cell lines. Use of in situ hybridization by Li et al [9] indicated that expression was high in developing neuronal tissues. Arama et al [11] demonstrated expression of a 52 kDa BMCC1s protein in neurones, which a follow-up study by Li et al [12] supports.…”

Section: Discussionmentioning

confidence: 99%

BMCC1 Is an AP-2 Associated Endosomal Protein in Prostate Cancer Cells

et al. 2013

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The prostate cancer antigen gene 3 (PCA3) is embedded in an intron of a second gene BMCC1 (Bcl2-/adenovirus E1B nineteen kDa-interacting protein 2 (BNIP-2) and Cdc42GAP homology BCH motif-containing molecule at the carboxyl terminal region 1) which is also upregulated in prostate cancer. BMCC1 was initially annotated as two genes (C9orf65/PRUNE and BNIPXL) on either side of PCA3 but our data suggest that it represents a single gene coding for a high molecular weight protein. Here we demonstrate for the first time the expression of a >300 kDa BMCC1 protein (BMCC1-1) in prostate cancer and melanoma cell lines. This protein was found exclusively in the microsomal fraction and localised to cytoplasmic vesicles. We also observed expression of BMCC1 protein in prostate cancer sections using immunohistology. GST pull down, immunoprecipitation and mass spectrometry protein interaction studies identified multiple members of the Adaptor Related Complex 2 (AP-2) as BMCC1 interactors. Consistent with a role for BMCC1 as an AP-2 interacting endosomal protein, BMCC1 co-localised with β-adaptin at the perinuclear region of the cell. BMCC1 also showed partial co-localisation with the early endosome small GTP-ase Rab-5 as well as strong co-localisation with internalised pulse-chase labelled transferrin (Tf), providing evidence that BMCC1 is localised to functional endocytic vesicles. BMCC1 knockdown did not affect Tf uptake and AP-2 knockdown did not disperse BMCC1 vesicular distribution, excluding an essential role for BMCC1 in canonical AP-2 mediated endocytic uptake. Instead, we posit a novel role for BMCC1 in post-endocytic trafficking. This study provides fundamental characterisation of the BMCC1 complex in prostate cancer cells and for the first time implicates it in vesicle trafficking.

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The expression and localization of Prune2 mRNA in the central nervous system

Cited by 9 publications

References 33 publications

A Smooth Muscle-Like Origin for Beige Adipocytes

A Smooth Muscle-Like Origin for Beige Adipocytes

Bmcc1s, a Novel Brain-Isoform of Bmcc1, Affects Cell Morphology by Regulating MAP6/STOP Functions

BMCC1 Is an AP-2 Associated Endosomal Protein in Prostate Cancer Cells

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