| Literature DB >> 30609389 |
Lukas Minus Orre1, Mattias Vesterlund2, Yanbo Pan2, Taner Arslan2, Yafeng Zhu2, Alejandro Fernandez Woodbridge2, Oliver Frings2, Erik Fredlund2, Janne Lehtiö3.
Abstract
Subcellular localization is a main determinant of protein function; however, a global view of cellular proteome organization remains relatively unexplored. We have developed a robust mass spectrometry-based analysis pipeline to generate a proteome-wide view of subcellular localization for proteins mapping to 12,418 individual genes across five cell lines. Based on more than 83,000 unique classifications and correlation profiling, we investigate the effect of alternative splicing and protein domains on localization, complex member co-localization, cell-type-specific localization, as well as protein relocalization after growth factor inhibition. Our analysis provides information about the cellular architecture and complexity of the spatial organization of the proteome; we show that the majority of proteins have a single main subcellular location, that alternative splicing rarely affects subcellular location, and that cell types are best distinguished by expression of proteins exposed to the surrounding environment. The resource is freely accessible via www.subcellbarcode.org.Keywords: mass spectrometry; organelle proteome; protein domains; protein localization; proteogenomics; proteomics; splice variants
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Year: 2019 PMID: 30609389 DOI: 10.1016/j.molcel.2018.11.035
Source DB: PubMed Journal: Mol Cell ISSN: 1097-2765 Impact factor: 17.970