Findings from University of Massachusetts in the Area of Cancer Gene Therapy Described (Cancer-relevant Splicing Factor CAPER alpha Engages the Essential Splicing Factor SF3b155 in a Specific Ternary Complex)
By a News Reporter-Staff News Editor at Cancer Gene Therapy Week -- Current study results on Biotechnology have been published. According to news originating from Worcester, Massachusetts, by NewsRx correspondents, research stated, "U2AF homology motifs (UHMs) mediate protein-protein interactions with U2AF ligand motifs (ULMs) of pre-mRNA splicing factors. The UHM-containing alternative splicing factor CAPER alpha regulates splicing of tumor-promoting VEGF isoforms, yet the molecular target of the CAPER alpha UHM is unknown."
Our news journalists obtained a quote from the research from the University of Massachusetts, "Here we present structures of the CAPER alpha UHM bound to a representative SF3b155 ULM at 1.7 angstrom resolution and, for comparison, in the absence of ligand at 2.2 angstrom resolution. The prototypical UHM/ULM interactions authenticate CAPER alpha as a bona fide member of the UHM family of proteins. We identify SF3b155 as the relevant ULM-containing partner of full-length CAPER alpha in human cell extracts. Isothermal titration calorimetry comparisons of the purified CAPER alpha UHM binding known ULM-containing proteins demonstrate that high affinity interactions depend on the presence of an intact, intrinsically unstructured SF3b155 domain containing seven ULM-like motifs. The interplay among bound CAPER alpha molecules gives rise to the appearance of two high affinity sites in the SF3b155 ULM-containing domain."
According to the news editors, the research concluded: "In conjunction with the previously identified, UHM/ULM-mediated complexes of U2AF(65) and SPF45 with SF3b155, this work demonstrates the capacity of SF3b155 to offer a platform for coordinated recruitment of UHM-containing splicing factors."
For more information on this research see: Cancer-relevant Splicing Factor CAPER alpha Engages the Essential Splicing Factor SF3b155 in a Specific Ternary Complex. Journal of Biological Chemistry, 2014;289(25):17325-17337. Journal of Biological Chemistry can be contacted at: Amer Soc Biochemistry Molecular Biology Inc, 9650 Rockville Pike, Bethesda, MD 20814-3996, USA. (American Society for Biochemistry and Molecular Biology - www.asbmb.org; Journal of Biological Chemistry - www.jbc.org/)
The news correspondents report that additional information may be obtained from S. Loerch, University of Massachusetts, Sch Med, Program Mol Med, Worcester, MA 01605, United States. Additional authors for this research include A. Maucuer, V. Manceau, M.R. Green and C.L. Kielkopf (see also Biotechnology).
Keywords for this news article include: Biotechnology, Oncology, Worcester, Massachusetts, United States, Cancer Gene Therapy, North and Central America
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