期刊
CELL
卷 164, 期 4, 页码 805-817出版社
CELL PRESS
DOI: 10.1016/j.cell.2016.01.029
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资金
- NHGRI CEGS grant [P50HG004233]
- NHGRI grant [U01HG001715]
- Ellison Foundation
- NCI grant [R33CA132073]
- Krembil Foundation (Canada)
- Canada Excellence Research Chair Award
- Ontario Research Fund-Research Excellence Award
- E.K. Shriver NICHD grant [R01HD065288]
- NIMH grants [R01MH091350, R01MH105524, R21MH104766]
- NSF [CCF-1219007]
- NSERC grant (Canada) [RGPIN-2014-03892]
- Canada Foundation for Innovation grant [JELF-33732]
- Canada Research Chairs Program
- NIH training grant [T32CA009361]
- NSERC fellowship (Canada)
- NIGMS grant [R01GM105431]
- Swedish Research Council International Postdoc Grant
- ICREA Funding Source: Custom
- Division of Computing and Communication Foundations
- Direct For Computer & Info Scie & Enginr [1219007] Funding Source: National Science Foundation
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'').
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