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Modeling RBM3, a novel RNA binding protein protooncogene to understand its function
Author(s) -
Samms Sarah,
Simmons Jerusha,
Seger Hannah,
Díaz Monica,
Dix Randy,
Anant Shrikant
Publication year - 2012
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.26.1_supplement.lb264
Subject(s) - rna binding protein , messenger rna , rna splicing , rna recognition motif , rna , alternative splicing , untranslated region , precursor mrna , carcinogenesis , biology , microbiology and biotechnology , computational biology , genetics , gene
Cancer is a major concern worldwide; over 1,200,000 cases of cancer will be diagnosed in America this year. In recent studies, RNA‐binding motif protein (RBM3) has been shown to be a protooncogene whose expression is unregulated in various cancers; the protein functions by regulating mRNA stability and translation. Within the N‐terminal region, RBM3 encodes one RNA recognition motif (RRM) domain, a 90 amino acids sequence shared by many RNA binding proteins that is implicated in the regulation of alternative splicing. This motif's structure consists of two alpha helices and four beta strands arranged in an alpha/beta sandwich. In previous studies, RBM3 has been shown to bind to AU‐rich sequences in the 3′untranslated region of mRNAs that encode cancer promoting proteins such as cyclooxygenase‐2 (COX‐2) and vascular endothelial growth factor (VEGF). Upon binding, RBM3 was shown to increase the stability and translation of these mRNAs, which is one mechanism by which the protein promotes tumorigenesis. The Olathe North SMART Team (Students Modeling A Research Topic) used 3D printing technology to model the protein RBM3 that has been found in Homo sapiens by homology of the known protein RBM39 from Mus musculus. Supported by a grant from NIH‐SEPA