Oligomeric Structure of the Human EphB2 Receptor SAM Domain

Thanos, Christopher D.; Goodwill, Kenneth E.; Bowie, James U.

doi:10.1126/science.283.5403.833

Cited by 221 publications

(202 citation statements)

References 43 publications

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“…Our ®ndings thus suggest that the pointed/B domain homophilic interaction is a candidate target for drug development. In this context, the recently reported structures of the pointed/B domain of Ets-1, and of the structurally related SAM domains of the Eph4A and EphB2 receptor tyrosine kinases, are of great interest (Slupsky et al, 1998, Stapleton et al, 1999Thanos et al, 1999).…”

Section: Discussionmentioning

confidence: 99%

Characterization of the chronic myelomonocytic leukemia associated TEL-PDGFβR fusion protein

et al. 1999

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Section: Discussionmentioning

confidence: 99%

Characterization of the chronic myelomonocytic leukemia associated TEL-PDGFβR fusion protein

et al. 1999

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“…[21][22][23][24] SAM domains are protein-protein interaction modules found in a variety of cytoplasmic signaling proteins and several transcriptional regulatory proteins. 21,22,24 In hematological malignancies, aberrant SAM-mediated oligomerization of the TEL, ETS family causes some leukemias in human. 25 Hagiwara et al's 26 mutation was detected in the SAM domain of an ovarian cancer cell line (codon 560, Ser→Ala).…”

Section: Discussionmentioning

confidence: 99%

Mutation of the p51/p63 gene is associated with blastic crisis in chronic myelogenous leukemia

et al. 2001

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The p51/p63 gene, a novel member of the p53 gene family, has recently been identified at 3q27-9. There are at least six major isotypes of p51/p63 mRNA transcripts. p51A/TAp63␥ has the potential to induce apoptosis and growth suppression in a manner similar to p53, and other isotypes may suppress the p53 and p51A/TAp63␥ genes in a dominant-negative manner. We analyzed the mutation and expression of the p51/p63 gene in 80 cases of chronic myelogenous leukemia (CML) to evaluate its role in blastic transformation. Expression of the p51/p63 gene was detected in 74 cases. The ␣ isotype of p51/p63 transcripts was dominantly expressed in 72 of these 74 cases. There was no correlation between the isotypes of p51/p63 transcripts and the clinical phase. Mutations of the p51/p63 gene were found in six cases. All these mutated cases expressed p51B/TAp63 ␣. In four of the six cases, the mutations were within a limited region (codon 151-170) corresponding to the DNA-binding domain. We hypothesized that this limited region is a hot spot for mutation of the p51/p63 gene. Mutations of the p53 gene were found in four cases of CML in blastic crisis (BC). Frequencies of the p51/p63 and p53 gene mutations were higher in BC (p51/p63 gene, 11.8%; p53 gene, 7.8%) than in the chronic phase (p51/p63 gene, 1.5%; p53 gene, 0%). The p51/p63 gene mutation may act similarly to the p53 gene mutation as a genetic alteration potentially responsible for the progression of CML. Leukemia (2001) 15, 1729-1734.

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“…The SAM domains of the Eph receptors have been shown to homo-dimerize in a crystal environment and weakly dimerize in solution. 25,26 This SAM-mediated dimerization has been proposed as a mechanism for Eph receptor activation. The pointed domain (a SAM-like domain) of the ETS transcription factor, TEL, can also self-associate, 31 and has been found fused to other signaling and regulatory proteins in many leukemias, resulting in constitutive activation of these fusion proteins via dimerization.…”

Section: A C-terminal Sam Domain In P63a and P73amentioning

confidence: 99%

Structure and function in the p53 family

1999

Cell Death Differ

101

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The recent discovery of several p53 homologs has uncovered a p53 superfamily of transcription factors that can trigger cell cycle arrest and apoptosis. The challenge now is to understand the similarities and differences between family members especially in terms of their regulation and potential for physical or genetic interactions with one another. This review summarizes recent progress in understanding the structure-function relationship within the p53 family. The new family members, p63 and p73, have an additional conserved domain at their C-termini which may have a regulatory function. The structure of this domain (a SAM domain) suggests that it is a protein-protein interaction module that may be involved in developmental processes. The oligomerization domains of p53 family members, while conserved in sequence and three-dimensional structure do not interact appreciably with other family members, but do mediate interactions between the multiple splice variants from an individual gene.

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Oligomeric Structure of the Human EphB2 Receptor SAM Domain

Cited by 221 publications

References 43 publications

Characterization of the chronic myelomonocytic leukemia associated TEL-PDGFβR fusion protein

Characterization of the chronic myelomonocytic leukemia associated TEL-PDGFβR fusion protein

Mutation of the p51/p63 gene is associated with blastic crisis in chronic myelogenous leukemia

Structure and function in the p53 family

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