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Widespread Expansion of Protein Interaction Capabilities by Alternative Splicing
Dana Farber Canc Inst, Genom Anal Network Perturbat Ctr Excellence Genom, Boston, MA 02215 USA.;Dana Farber Canc Inst, Ctr Canc Syst Biol CCSB, Boston, MA 02215 USA.;Dana Farber Canc Inst, Dept Canc Biol, Boston, MA 02215 USA.;Harvard Univ, Sch Med, Dept Genet, Boston, MA 02115 USA.;Southern Med Univ, Nanfang Hosp, Dept Obstet & Gynecol, Guangzhou 510515, Guangdong, Peoples R China..
McGill Univ, Dept Bioengn, Montreal, PQ H3A 0C3, Canada.;Univ Montreal, Inst Res Immunol & Canc, Montreal, PQ H3C 3J7, Canada..
Univ Calif San Diego, Dept Psychiat, La Jolla, CA 92093 USA.;Univ So Calif, Dept Biol Sci, Mol & Computat Biol Program, Los Angeles, CA 90089 USA..
Dana Farber Canc Inst, Genom Anal Network Perturbat Ctr Excellence Genom, Boston, MA 02215 USA.;Dana Farber Canc Inst, Ctr Canc Syst Biol CCSB, Boston, MA 02215 USA.;Dana Farber Canc Inst, Dept Canc Biol, Boston, MA 02215 USA.;Harvard Univ, Sch Med, Dept Genet, Boston, MA 02115 USA..
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2016 (English)In: Cell, ISSN 0092-8674, E-ISSN 1097-4172, Vol. 164, no 4, 805-817 p.Article in journal (Refereed) Published
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Abstract [en]

While alternative splicing is known to diversify the functional characteristics of some genes, the extent to which protein isoforms globally contribute to functional complexity on a proteomic scale remains unknown. To address this systematically, we cloned full-length open reading frames of alternatively spliced transcripts for a large number of human genes and used protein-protein interaction profiling to functionally compare hundreds of protein isoform pairs. The majority of isoform pairs share less than 50% of their interactions. In the global context of interactome network maps, alternative isoforms tend to behave like distinct proteins rather than minor variants of each other. Interaction partners specific to alternative isoforms tend to be expressed in a highly tissue-specific manner and belong to distinct functional modules. Our strategy, applicable to other functional characteristics, reveals a widespread expansion of protein interaction capabilities through alternative splicing and suggests that many alternative "isoforms'' are functionally divergent (i.e., "functional alloforms'').

Place, publisher, year, edition, pages
2016. Vol. 164, no 4, 805-817 p.
National Category
Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)
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URN: urn:nbn:se:uu:diva-280244DOI: 10.1016/j.cell.2016.01.029ISI: 000369998300024PubMedID: 26871637OAI: oai:DiVA.org:uu-280244DiVA: diva2:910582
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Swedish Research Council
Available from: 2016-03-09 Created: 2016-03-09 Last updated: 2017-11-30Bibliographically approved

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Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)

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