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Current Opinion in Genetics and Development
Volumn 3, Issue 1, 1993, Pages 55-62
Retinoblastoma protein and the cell cycle
Author keywords

[No Author keywords available]
Indexed keywords

CYCLINE; PROTEIN KINASE; REGULATOR PROTEIN;
EID: 0027528789     PISSN: 0959437X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-437X(05)80341-7     Document Type: Article
Times cited : (70)
References (54)
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    • of outstanding interest, This report describes experiments in which plasmids encoding various glutathione S-transferase (GST)-cyclin fusion proteins were co-transported with the RB gene. While transfection of RB alone arrests cells in G1, cyclins A and E are able to overcome this arrest; as can cyclin D, although partially. The phosphorylation of the exogenous Rb also increases in the presence of cyclins A and E, but not in the presence of cyclin D. Rb mutants that arrest cell division even in the presence of the cyclins are not hyperphosphorylated in their presence, implying a connection, although not necessarily direct, between cyclin-dependent phosphorylation and the inactivation of Rb's division-arresting activities.
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    • of special interest, These authors have tested the notion that binding to the E1A viral on-coprotein could negate the need for Rb phosphorylation in promoting the entry of quiescent cells into the cell cycle. They found that this notion is probably incorrect, at least in baby rat kidney cells, as E1A domain 2 mutants that are severely defective in binding to Rb can still, like wild-type E1A, induce Rb phosphorylation. Therefore, direct physical association with Rb may not be necessary for E1A-mediated entry into the cell cycle, and instead this activity may be the consequence of an induction of Rb phosphorylation.
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    • of outstanding interest, This paper describes the effects of RB gene disruptions in mice. Homozygous mutants were not viable and death occurred in utero between the 14th and 15th day of gestation, with defects in the hematopoietic system as well as the central and peripheral nervous systems. The lethal phenotype could be rescued by the transfer of a human RB mini-transgene into the mutant mice.
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    • of outstanding interest, This is an excellent summary of the numerous and sometimes confusing reports indicating that the cellular transcription factor E2F may be regulated by interactions with the Rb protein and other factors. Nevins also provides some intriguing speculation about the possible mechanisms involved.
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    • of outstanding interest, In this study, a cDNA, RBP3, encoding an E2F-like protein was cloned by its ability to bind to Rb. This binding was shown to occur in vitro, and the complex could be immunoprecipitated from cell lysates. RBP3 bound preferentially to unphosphorylated Rb, and the complex was disrupted by both cdc2 and cdk2. RBP3 also bound to p107, although with weaker affinity than for Rb. In addition, transient expression of the RBP3 protein activated transcription from the adenovirus E2 promoter dependent upon the presence of E2F binding sites.
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    • of outstanding interest, In this work, which is similar to that described in [19], an E2F-like encoding cDNA, RBAP-1, was cloned by its ability to bind to the Rb portion of a GST-Rb fusion protein. RBAP-1 co-purified with E2F, and was shown to bind to both adenovirus E4 and to the E2F recognition sequence, and to contain a transcriptional-activation domain.
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    • of outstanding interest, This report describes the use of an ‘Rb sandwich’ to screen cDNA expression libraries for Rb-associated proteins. This method led to the isolation of nine distinct cDNA clones, one of which encodes a protein with properties known to be characteristic of the transcription factor E2F (as in [19,20]). The regions on Rb required for the AP12 interaction are similar to the Rb T antigen binding domains. Several other clones are shown to be identical to previously characterized genes.
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    • of special interest, These investigators used co-transfection of TGF-β2-CAT reporter plasmids with RB-expressing plasmids to study the effect of Rb on the TGF-β2 promoter. The promoter element responsible for an observed Rb-induced transcriptional activation was found to comprise binding sites for the ATF-2 transcription factor. Further, the inclusion of an ATF-2 site renders a promoter Rb responsive, and ATF-2 in nuclear extracts can bind to a GST-Rb fusion protein. It is not clear, however, whether this phenomenon is cell type specific or whether other ATF-2-regulated promoters are influenced by Rb.
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    • of special interest, It was shown by microinjection experiments that the co-injection of Rb protein with c-myc inhibits the ability of Rb to arrest cell-cycle progression. On the other hand, co-injection of EJ-Ras, c-Fos or c-Jun with Rb did not alter the ability of Rb to arrest cell-cycle progression. The c-Myc protein did not affect the activity of another tumor suppressor, p53, indicating that c-Myc and Rb specifically antagonize one another in the cell.
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    • of special interest, In this work, a number of proteins were identified by their ability to interact with the T/E1A-binding region of Rb. GST-Rb fusion proteins containing the T/E1A-binding domain were used as affinity-binding reagents in the identification of proteins from a number of human tumor cell lines that associated with Rb.
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    • in press, of special interest, Although numerous Rb-associated proteins have now been isolated using a variety of techniques, only a few match or resemble known proteins. In this case, RbAp48, one of several proteins isolated by Rb affinity chromatography, was partially microsequenced and this sequence was used to clone the cognate gene. The predicted RbAp48 amino-acid sequence is 30% identical to that of the yeast SMI1-encoded product, and moreover, the gene encoding RbAp48 can functionally substitute for MSI1 in yeast mutants. The MSI1 gene encodes a downstream negative regulator of yeast Ras2. Because Ras proteins serve as signal transducers in probably all eukaryotes, RbAp48, and thus Rb itself, may be involved in Ras-mediated signal transduction. If this is true, then a problem that must be addressed is how the cytoplasmic Ras signal connects to RbAPp48, which is located in the nucleus.
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    • of special interest, Using PCR amplification with degenerate oligonucleotides corresponding to conserved regions of CDC2, eleven separate protein kinase genes were cloned from Hela cells, and seven of these were novel. The kinases fall into several subgroups based on various criteria including sequence similarity. Thus, together with the several cyclins already known, a family of cdc2-related proteins reveals that the regulation of cell division may be very complex.
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.