Isolation of rsp-1, a novel cDNA capable of suppressing v-Ras transformation.

Cutler, Mary Lou; Bassin, Robert H.; Zanoni, Lorenzo; Talbot, Neil C.

doi:10.1128/mcb.12.9.3750

Cited by 84 publications

(83 citation statements)

References 31 publications

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“…The RSU1-LIMS1 interaction is notable because it implicates a potential tumor suppressor protein (RSU1) in the integrin signaling pathway. RSU1 was originally identified in a screen for genes that could inhibit Ras-mediated signaling 29 and was later shown to inhibit anchorage-independent growth of MCF7 breast cancer cells 30 . Notably, we have observed that RSU1 is consistently downregulated in prostate cancer 3,24,26 , further suggesting a tumor suppressor role for this gene; however, to date, the mechanism by which RSU1 exerts its effects has not been elucidated.…”

Section: A N a Ly S I Smentioning

confidence: 99%

Probabilistic model of the human protein-protein interaction network

et al. 2005

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A catalog of all human protein-protein interactions would provide scientists with a framework to study protein deregulation in complex diseases such as cancer. Here we demonstrate that a probabilistic analysis integrating model organism interactome data, protein domain data, genomewide gene expression data and functional annotation data predicts nearly 40,000 protein-protein interactions in humans⎯a result comparable to those obtained with experimental and computational approaches in model organisms. We validated the accuracy of the predictive model on an independent test set of known interactions and also experimentally confirmed two predicted interactions relevant to human cancer, implicating uncharacterized proteins into definitive pathways. We also applied the human interactome network to cancer genomics data and identified several interaction subnetworks activated in cancer. This integrative analysis provides a comprehensive framework for exploring the human protein interaction network.We began by assembling a collection of genomic and proteomic data potentially useful in predicting human protein-protein interactions that included model organism protein-protein interactions 1 , protein domain assignments 2 , gene expression measurements in human tissue samples 3 and biological function annotations 4 ( Table 1). Based on previous reports, we suspected that (i) model organism interactions may suggest interactions among orthologous human proteins 5,6 , (ii) similar gene expression profiles across a panel of human tissue samples may identify interacting protein products 7,8 , (iii) protein domain pairs enriched among known human protein-protein interactions may suggest novel interactions 9 , (iv) shared functional annotations from Gene Ontology 4 may suggest physical interactions, and (v) that combining evidence from independent data sources may strongly predict protein-protein interactions [10][11][12] . To test these hypotheses, we applied a naive Bayes classifier 7 , a method well-suited for integrating disparate data types.A gold standard positive set (GSP) of 11,678 distinct protein-protein interactions among 5,505 proteins was queried from the Human Protein Reference Database (HPRD) 12 , a resource that contains known protein-protein interactions manually curated from the literature by expert biologists. A gold standard negative set (GSN) of 3,106,928 protein pairs was defined, in which one protein was assigned to the plasma membrane cellular component and the other to the nuclear cellular component by the Gene Ontology Consortium 4 . Although it is known that membrane proteins can occasionally interact with nuclear proteins, we demonstrated that there are far fewer known interactions within GSN than would be expected by chance (Supplementary Methods online). By averaging the number of interactions per protein in the GSP, we estimated the prior odds of interaction among two randomly selected proteins to be 1 in 381. This is likely an underestimate of the true prior odds because all protein-protein intera...

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Section: A N a Ly S I Smentioning

confidence: 99%

Probabilistic model of the human protein-protein interaction network

et al. 2005

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“…RSP-1 is capable of suppressing v-ras transformation in vitro. 41 RSP-1 contains seven leucine-rich repeats, like LRRC2. Thus, there are both functional and positional reasons to study this gene further with regard to its possible role in tumorigenesis.…”

Section: Discussionmentioning

confidence: 99%

The transcriptional map of the common eliminated region 1 (C3CER1) in 3p21.3

et al. 2002

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“…Similarly a number of ras-speci®c suppressors have been described previously (SchaÈ fer, 1994). For example, Rsu-1 speci®cally blocks ras transformation (Cutler et al, 1992). NIH3T3 cells expressing p33 rsu-1 have been shown to resist transformation by retroviruses containing v-ki-ras and v-Ha-ras genes, but were susceptible to v-src and v-mos containing viruses.…”

Section: Growth Propertiesmentioning

confidence: 99%

Suppression of src-induced transformed phenotype by expression of tropomyosin-1

et al. 1999

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Suppression of high M r tropomyosins (TMs) is a common feature of transformed cells. Previous work from this laboratory has demonstrated that the isoform 1 of TM, TM1, acts as an anti-oncogene in rastransformed murine ®broblasts. In this study, we have investigated whether TM1 is a ras-speci®c suppressor, or a general suppressor protein of the cellular transformation. V-src transformed ®broblasts, which express decreased TM1, were transduced with a full-length cDNA to overexpress TM1. Both the control and the transduced cells expressed v-src kinase at comparable levels. TM1 expressing (src-T1) cells grew at a lower rate in monolayer, exhibited well spread,¯at morphology than the control cells. Enhanced expression of TM1 resulted in improved micro®lamental architecture. More signi®cantly, src-T1 cells completely failed to grow under anchorage independent conditions. These data demonstrate that TM1 is as an anti-oncogene of functionally diverse oncogenes, and it is a class II tumor suppressor protein.

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Isolation of rsp-1, a novel cDNA capable of suppressing v-Ras transformation.

Cited by 84 publications

References 31 publications

Probabilistic model of the human protein-protein interaction network

Probabilistic model of the human protein-protein interaction network

The transcriptional map of the common eliminated region 1 (C3CER1) in 3p21.3

Suppression of src-induced transformed phenotype by expression of tropomyosin-1

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