RLIP76 and Cancer

Awasthi, Sanjay; Singhal, Sharad S.; Awasthi, Yogesh C.; Martin, Bryan; Woo, Jeong Soo; Cunningham, Casey; Frankel, Arthur E.

doi:10.1158/1078-0432.ccr-08-0145

Cited by 77 publications

(81 citation statements)

References 52 publications

(93 reference statements)

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“…MRP1/GS-X is one of the two MRP proteins involved in extruding DOX conjugated with glutathione from the cytoplasm in cardiomyocytes. RLIP76 (RALBP1), the other GS-X pump involved in the transport of GSH-conjugated DOX out of the heart muscle, seems to be expressed 1.5 times more in heart muscle compared with skeletal muscle (Awasthi et al, 2008). A marked difference in the expression of MRPs between skeletal and cardiac muscle might be an explanation for the differences in the reaction to antioxidants observed.…”

Section: Discussionmentioning

confidence: 92%

Direct effects of doxorubicin on skeletal muscle contribute to fatigue

et al. 2009

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Chemotherapy-induced fatigue is a multidimensional symptom. Oxidative stress has been proposed as a working mechanism for anthracycline-induced cardiotoxicity. In this study, doxorubicin (DOX) was tested on skeletal muscle function. Doxorubicin induced impaired ex vivo skeletal muscle relaxation followed in time by contraction impediment, which could be explained by DOXinduced changes in Ca 2 þ responses of myotubes in vitro. The Ca 2 þ responses in skeletal muscle, however, could not be explained by oxidative stress.

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Section: Discussionmentioning

confidence: 92%

Direct effects of doxorubicin on skeletal muscle contribute to fatigue

et al. 2009

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“…On the other hand, this work points to these proteins as suitable targets for the development of therapeutics, particularly for control of metastatic cancers. In fact, RalBP1 regulation is already considered a feasible target for new anticancer therapies (22,50). Our studies showed that epsins, similar to RalBP1, are also involved in motility of and invasion by malignant cells suggesting a role for epsins in tumor growth and metastasis.…”

Section: Discussionmentioning

confidence: 60%

“…17,18) and has been found in complexes with epsin1 (17,19). RalBP1 is a ubiquitously expressed, plasma membrane-associated protein (20,21), involved in drug resistance (22,23) and NIH3T3 fibroblast migration (14).…”

Section: Epsin Enth Domain Directlymentioning

confidence: 99%

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The Epsin Family of Endocytic Adaptors Promotes Fibrosarcoma Migration and Invasion*

Coon

Burgner

Camonis

et al. 2010

Journal of Biological Chemistry

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Abnormalities in the process of endocytosis are classically linked to malignant transformation through the deficient down-regulation of signaling receptors. The present study describes a non-classical mechanism that does not require internalization by which endocytic proteins affect cell migration and basement membrane invasion. Specifically, we found that the endocytic adaptor epsin binds and regulates the biological properties of the signaling molecule RalBP1 (Ral-binding protein 1). Epsin interacted with the N terminus of RalBP1 via its characteristic epsin N-terminal homology (ENTH) domain. A combination of siRNA-mediated knock-down and transfection of siRNA-resistant constructs in fibrosarcoma cells demonstrated that impairment of the epsin-RalBP1 interaction led to cell migration and basement membrane invasion defects. We found the ENTH domain was necessary and sufficient to sustain normal cell migration and invasion. Because all the epsin endocytic motifs reside in the C-terminal part of the molecule, these results suggest that this novel regulatory circuit does not require endocytosis. In addition, cells depleted of epsin-RalBP1 complex displayed deficient activation of Rac1 and Arf6 suggesting a signaling function for this novel interaction. Further, overexpression of either epsin or RalBP1 enhanced migration and invasion of fibrosarcoma cells. Collectively, our results indicate that epsin regulates RalBP1 function in Rac1-and Arf6-dependent pathways to ultimately affect cell migration and invasion. We propose that the observed up-regulation of both epsin and RalBP1 in certain cancers contributes to their invasive characteristics.

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“…Inhibition of RAL-A, an activator of RALBP1, leads to reduction of cell proliferation in cells derived from non-small cell lung cancers (38). RALBP1 has an important antiapoptotic role with the transport of glutathione conjugates of electrophilic proapoptotic compounds produced during oxidative stress (32,39) and is involved in the oxidative stress response through its interaction with HSF1 (heat shock factor 1) (40).…”

Section: Discussionmentioning

confidence: 99%

Early Steps of Jaagsiekte Sheep Retrovirus-Mediated Cell Transformation Involve the Interaction between Env and the RALBP1 Cellular Protein

Monot

Erny

Gineys

et al. 2015

J Virol

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Ovine pulmonary adenocarcinoma is a naturally occurring lung cancer in sheep induced by the Jaagsiekte sheep retrovirus (JSRV). Its envelope glycoprotein (Env) carries oncogenic properties, and its expression is sufficient to induce in vitro cell transformation and in vivo lung adenocarcinoma. The identification of cellular partners of the JSRV envelope remains crucial for deciphering mechanisms leading to cell transformation. We initially identified RALBP1 (RalA binding protein 1; also known as RLIP76 or RIP), a cellular protein implicated in the ras pathway, as a partner of JSRV Env by yeast two-hybrid screening and confirmed formation of RALBP1/Env complexes in mammalian cells. Expression of the RALBP1 protein was repressed in tumoral lungs and in tumor-derived alveolar type II cells. Through its inhibition using specific small interfering RNA (siRNA), we showed that RALBP1 was involved in envelope-induced cell transformation and in modulation of the mTOR (mammalian target of rapamycin)/p70S6K pathway by the retroviral envelope.

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RLIP76 and Cancer

Cited by 77 publications

References 52 publications

Direct effects of doxorubicin on skeletal muscle contribute to fatigue

Direct effects of doxorubicin on skeletal muscle contribute to fatigue

The Epsin Family of Endocytic Adaptors Promotes Fibrosarcoma Migration and Invasion*

Early Steps of Jaagsiekte Sheep Retrovirus-Mediated Cell Transformation Involve the Interaction between Env and the RALBP1 Cellular Protein

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