Tumor protein D52 represents a negative regulator of ATM protein levels

Chen, Yuyan; Kamili, Alvin; Hardy, Jayne; Groblewski, Guy E.; Khanna, Kum Kum; Byrne, Jennifer A.

doi:10.4161/cc.26146

Cited by 25 publications

(28 citation statements)

References 66 publications

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“…Indirect immunofluorescence analyses of TPD52 show granular cytoplasmic staining with a perinuclear accentuation in MCF-7 breast cancer (Balleine et al, 2000) and TPD52-expressing 3T3 cells (Chen et al, 2013). As TPD52 further accumulated at the perinuclear region of TPD52-expressing 3T3 cells upon oleic acid treatment (supplementary material Fig.…”

Section: Tpd52 Expression Alters Fatty Acid Metabolism In 3t3 Fibroblmentioning

confidence: 99%

“…Pulldown assays employed glutathione S-transferase (GST) and His 6 -tagged recombinant mouse Tpd52 proteins expressed from pGEX3X Sathasivam et al, 2001), and GST-tagged recombinant human TPD52 expressed from pGEX6P-1 (Chen et al, 2013;Shahheydari et al, 2014). Purification of mouse or human TPD52 fusion proteins and respective GST controls was performed as previously described (Chen et al, 2013;Shahheydari et al, 2014).…”

Section: Pulldown Assaysmentioning

confidence: 99%

“…Purification of mouse or human TPD52 fusion proteins and respective GST controls was performed as previously described (Chen et al, 2013;Shahheydari et al, 2014). Purified proteins were assessed by SDS-PAGE.…”

Section: Pulldown Assaysmentioning

confidence: 99%

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TPD52 expression increases neutral lipid storage within cultured cells

Kamili

Roslan

Frost

et al. 2015

Journal of Cell Science

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Tumor protein D52 (TPD52) is amplified and/or overexpressed in cancers of diverse cellular origins. Altered cellular metabolism (including lipogenesis) is a hallmark of cancer development, and protein-protein associations between TPD52 and known regulators of lipid storage, and differential TPD52 expression in obese versus non-obese adipose tissue, suggest that TPD52 might regulate cellular lipid metabolism. We found increased lipid droplet numbers in BALB/c 3T3 cell lines stably expressing TPD52, compared with control and TPD52L1-expressing cell lines. TPD52-expressing 3T3 cells showed increased fatty acid storage in triglyceride (from both de novo synthesis and uptake) and formed greater numbers of lipid droplets upon oleic acid supplementation than control cells. TPD52 colocalised with Golgi, but not endoplasmic reticulum (ER), markers and also showed partial colocalisation with lipid droplets coated with ADRP (also known as PLIN2), with a proportion of TPD52 being detected in the lipid droplet fraction. Direct interactions between ADRP and TPD52, but not TPD52L1, were demonstrated using the yeast two-hybrid system, with ADRP-TPD52 interactions confirmed using GST pulldown assays. Our findings uncover a new isoformspecific role for TPD52 in promoting intracellular lipid storage, which might be relevant to TPD52 overexpression in cancer.

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Section: Tpd52 Expression Alters Fatty Acid Metabolism In 3t3 Fibroblmentioning

confidence: 99%

Section: Pulldown Assaysmentioning

confidence: 99%

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TPD52 expression increases neutral lipid storage within cultured cells

Kamili

Roslan

Frost

et al. 2015

Journal of Cell Science

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“…21,22 Its coiled-coil motif is indeed necessary for interactions with TPD52 proteins and these interactions could be stabilized by the C-terminal protein regions. 23 TPD52L2, a member of the tumor protein D52-like family, could interact with hABCF3 to enhance liver cancer cell proliferation, 10 suggesting that TPD52L2 may interact with the hABCF3-like protein through its coiled-coil structure and further implicate in the development of cancer.…”

Section: R E T R a C T E Dmentioning

confidence: 99%

Retracted: Tumor Protein D52-Like 2 Contributes to Proliferation of Breast Cancer Cells

Yang

Wang

Jia

et al. 2015

Cancer Biotherapy and Radiopharmaceuticals

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“…The human chromosome 8q21 region is one of the most frequently amplified regions in PCa [12,38], suggesting that TPD52 may act as a candidate oncogene in PCa. Recent reports have shown that TPD52 is overexpressed in several types of human cancers, both at the mRNA and protein levels [39,40]. Other reports have demonstrated that the prostate leucine zipper (PrLZ) gene, a member of the TPD52 family, contains a C-terminal region identical to TPD52.…”

Section: Discussionmentioning

confidence: 99%

Tumour‐suppressive microRNA‐224 inhibits cancer cell migration and invasion via targeting oncogenic TPD52 in prostate cancer

et al. 2014

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Edited by Tamas DalmayKeywords: miR-224 TPD52 Prostate cancer microRNA Tumour suppressor a b s t r a c t Our recent study of the microRNA expression signature of prostate cancer (PCa) revealed that microRNA-224 (miR-224) is significantly downregulated in PCa tissues. Here, we found that restoration of miR-224 significantly inhibits PCa cell migration and invasion. Additionally, we found that oncogenic TPD52 is a direct target of miR-224 regulation. Silencing of the TPD52 gene significantly inhibits cancer cell migration and invasion. Moreover, TPD52 expression is upregulated in cancer tissues and negatively correlates with miR-224 expression. We conclude that loss of tumour-suppressive miR-224 enhances cancer cell migration and invasion in PCa through direct regulation of oncogenic TPD52.

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Tumor protein D52 represents a negative regulator of ATM protein levels

Cited by 25 publications

References 66 publications

TPD52 expression increases neutral lipid storage within cultured cells

TPD52 expression increases neutral lipid storage within cultured cells

Retracted: Tumor Protein D52-Like 2 Contributes to Proliferation of Breast Cancer Cells

Tumour‐suppressive microRNA‐224 inhibits cancer cell migration and invasion via targeting oncogenic TPD52 in prostate cancer

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