Impairment of MAD2B–PRCC interaction in mitotic checkpoint defective t(X;1)-positive renal cell carcinomas

Weterman, Marian A. J.; Groningen, J.J.M. van; Tertoolen, Leon G.J.; Kessel, Ad Geurts van

doi:10.1073/pnas.241304198

Cited by 68 publications

(67 citation statements)

References 42 publications

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“…Therefore, Rev7 plays a key in vivo role in cell cycle regulation. Rev7 also interacts with a variety of other proteins involved in the cell cycle and regulation of cell growth: the HCCA2 transcriptional activator involved in cell cycle control (139), the Elk1 transcription factor affecting cell cycle progression and the DNA damage stress response (275), the PRCC cancer protein implicated in RNA splicing and mitotic progression (258), two metalloproteases involved in cell proliferation and signaling (186), and the adenovirus death protein (269).…”

Section: Pol (Rev3/rev7)mentioning

confidence: 99%

Eukaryotic Translesion Polymerases and Their Roles and Regulation in DNA Damage Tolerance

Waters

Minesinger

Wiltrout

et al. 2009

Microbiol Mol Biol Rev

524

647

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SUMMARY DNA repair and DNA damage tolerance machineries are crucial to overcome the vast array of DNA damage that a cell encounters during its lifetime. In this review, we summarize the current state of knowledge about the eukaryotic DNA damage tolerance pathway translesion synthesis (TLS), a process in which specialized DNA polymerases replicate across from DNA lesions. TLS aids in resistance to DNA damage, presumably by restarting stalled replication forks or filling in gaps that remain in the genome due to the presence of DNA lesions. One consequence of this process is the potential risk of introducing mutations. Given the role of these translesion polymerases in mutagenesis, we discuss the significant regulatory mechanisms that control the five known eukaryotic translesion polymerases: Rev1, Pol ζ, Pol κ, Pol η, and Pol ι.

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Section: Pol (Rev3/rev7)mentioning

confidence: 99%

Eukaryotic Translesion Polymerases and Their Roles and Regulation in DNA Damage Tolerance

Waters

Minesinger

Wiltrout

et al. 2009

Microbiol Mol Biol Rev

524

647

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“…The cells were transfected and grown overnight on glass microscope slides, fixed, and analyzed by fluorescence microscopy as described in ref. 28.…”

Section: Analysis Of Interactions In Yeastmentioning

confidence: 99%

Interaction of nephrocystin-4 and RPGRIP1 is disrupted by nephronophthisis or Leber congenital amaurosis-associated mutations

Roepman

Letteboer²,

Arts³

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

110

108

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RPGR-interacting protein 1 (RPGRIP1) is a key component of cone and rod photoreceptor cells, where it interacts with RPGR (retinitis pigmentosa GTPase regulator). Mutations in RPGRIP1lead to autosomal recessive congenital blindness [Leber congenital amaurosis (LCA)]. Most LCA-associated missense mutations in RPGRIP1 are located in a segment that encodes two C2 domains. Based on the C2 domain of novel protein kinase C (PKC ), we built a 3D-homology model for the C-terminal C2 domain of RPGRIP1. This model revealed a potential Ca 2؉ -binding site that was predicted to be disrupted by a missense mutation in RPGRIP1, which was previously identified in an LCA patient. Through yeast two-hybrid screening of a retinal cDNA library, we found this C2 domain to specifically bind to nephrocystin-4, encoded by NPHP4. Mutations in NPHP4 are associated with nephronophthisis and a combination of nephronophthisis and retinitis pigmentosa called Senior-Løken syndrome (SLSN). We show that RPGRIP1 and nephrocystin-4 interact strongly in vitro and in vivo, and that they colocalize in the retina, matching the panretinal localization pattern of specific RPGRIP1 isoforms. Their interaction is disrupted by either mutations in RPGRIP1, found in patients with LCA, or by mutations in NPHP4, found in patients with nephronophthisis or SLSN. Thus, we provide evidence for the involvement of this disrupted interaction in the retinal dystrophy of both SLSN and LCA patients.T he X-linked gene RPGR (retinitis pigmentosa GTPase regulator) is mutated in patients with retinitis pigmentosa type 3 (RP3) (1, 2), cone or cone-rod dystrophy (COD1) (3, 4), atrophic macular degeneration (5), and RP in combination with impaired hearing and sinorespiratory infections (6). All RP3-associated missense mutations in RPGR have been identified in the N-terminal RCC1-homologous domain, and they disrupt the interaction with the C-terminal domain of RPGR-interacting protein 1 (RPGRIP1) (7,8). Mutations in RPGRIP1 lead to Leber congenital amaurosis (LCA), a genetically heterogeneous recessive disorder that is regarded to be the earliest and most severe form of all retinal dystrophies (9, 10). LCA accounts for at least 5% of all retinal dystrophies and is one of the main causes for blindness in children (11). RPGR and RPGRIP1 isoforms have been found to colocalize at the connecting cilia as well as the outer segments of rod and cone photoreceptors (12, 13). Differential localization among species has also been reported (12,14), and different isoforms of RPGRIP1 have been described resulting from splicing variation (7,14,15). The distinct partitioning of a subset of RPGRIP1 isoforms between the nuclear and cytoplasmic compartments combined with the differential and limited proteolysis of RPGRIP1 among retinal neurons, and the impact of LCA-linked mutations in RPGRIP1 in these processes, support the involvement of nucleocytoplasmatic signaling processes mediated by RPGRIP1 and its interacting partners in the pathogenesis of LCA, RP3, and allied diseases (15, 16). The pres...

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“…Although the mechanism through which these fusions contribute to oncogenesis remains unclear, several studies suggest that the PRCC-TFE3 (21,22) and ASPL-TFE3 fusion proteins (M.L., unpublished observations) are transcriptional activators. One study explored the possibility that PRCC-TFE3 may interfere with mitotic checkpoint control via the PRCC domain (23), although it is unclear whether such a mechanism could apply to the other fusion partners.…”

mentioning

confidence: 99%

Cloning of an Alpha-TFEB fusion in renal tumors harboring the t(6;11)(p21;q13) chromosome translocation

Davis

Hsi

Arroyo

et al. 2003

Proc. Natl. Acad. Sci. U.S.A.

227

173

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MITF, TFE3, TFEB, and TFEC comprise a transcription factor family (MiT) that regulates key developmental pathways in several cell lineages. Like MYC, MiT members are basic helix-loop-helix-leucine zipper transcription factors. MiT members share virtually perfect homology in their DNA binding domains and bind a common DNA motif. Translocations of TFE3 occur in specific subsets of human renal cell carcinomas and in alveolar soft part sarcomas. Although multiple translocation partners are fused to TFE3, each translocation product retains TFE3's basic helix-loop-helix leucine zipper. We have identified the genes fused by the chromosomal translocation t(6;11)(p21.1;q13), characteristic of another subset of renal neoplasms. In two primary tumors we found that Alpha, an intronless gene, rearranges with the first intron of TFEB, just upstream of TFEB's initiation ATG, preserving the entire TFEB coding sequence. Fluorescence in situ hybridization confirmed the involvement of both TFEB and Alpha in this translocation. Although the Alpha promoter drives expression of this fusion gene, the Alpha gene does not contribute to the ORF. Whereas TFE3 is typically fused to partner proteins in subsets of renal tumors, we found that wild-type, unfused TFE3 stimulates clonogenic growth in a cell-based assay, suggesting that dysregulated expression, rather than altered function of TFEB or TFE3 fusions, may confer neoplastic properties, a mechanism reminiscent of MYC activation by promoter substitution in Burkitt's lymphoma. Alpha-TFEB is thus identified as a fusion gene in a subset of pediatric renal neoplasms.M ITF, TFE3, TFEB, and TFEC are closely related basic helix-loop-helix leucine zipper (bHLH-LZ) transcription factors (1-8) that may homo-or heterodimerize in all combinations to bind DNA (9). These factors share sequence homology in their DNA-contacting basic domains (10), as well as activation domains, and recognize identical DNA sequences (9), suggesting that they may regulate similar downstream targets. Genetic and biochemical studies have revealed functional overlap of MiT activity in certain developmental lineages. Specifically, use of knockout mice by Jenkins and colleagues (8) has elegantly demonstrated that, whereas mutation of either Mitf or TFE3 in mice does not disrupt osteoclast development, mutation of both genes or presence of a dominant-negative allele produces severe osteopetrosis. Homozygous mutation of MITF in the mouse is particularly devastating to the melanocyte lineage, resulting in failure of melanocyte development (5). In humans, Mitf haploinsufficiency results in type IIa Waardenburg syndrome (11). Mice homozygous null for TFE3 or TFEC had no recognized abnormalities (8), but TFEB nulls exhibited embryonic lethality associated with placental vascular defects (12). In addition, Mitf and TFE3 have been found to undergo identical modifications after cytokine stimulation (13), and MITF has been shown to directly regulate BCL2, a key apoptotic regulator, in a manner important for melanocyte and melanoma surv...

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Impairment of MAD2B–PRCC interaction in mitotic checkpoint defective t(X;1)-positive renal cell carcinomas

Cited by 68 publications

References 42 publications

Eukaryotic Translesion Polymerases and Their Roles and Regulation in DNA Damage Tolerance

Eukaryotic Translesion Polymerases and Their Roles and Regulation in DNA Damage Tolerance

Interaction of nephrocystin-4 and RPGRIP1 is disrupted by nephronophthisis or Leber congenital amaurosis-associated mutations

Cloning of an Alpha-TFEB fusion in renal tumors harboring the t(6;11)(p21;q13) chromosome translocation

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