期刊
PLANT CELL
卷 31, 期 9, 页码 2010-2034出版社
OXFORD UNIV PRESS INC
DOI: 10.1105/tpc.19.00081
关键词
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资金
- U.S. Department of Energy, Office of Science, Office of Biological and Environmental Research [DE-AC02-05CH11231]
- European Commission Marie Curie Fellowship [PIEF-GA-2011-301401]
- Det Frie ForskningsralTechnologie og Produktion Fellowship [DFF-1337-00066]
- European Molecular Biology Organization Long-Term Fellowship [ALTF 1246-2013]
- Australian Research Council Discovery Early Career Researcher Award [DE170100054]
- Medical Research Council [MC_U105178783]
- National Science Foundation Plant Genome Program [DBI-0421683]
- National Science Foundation [DBI-0421683, RCN 009281]
- Vienna Science and Technology Fund [LS11-045]
- U.S. Department of Energy, Office of Science, Office of Biological and Environmental Research (U.S. Department of Energy)
- MRC [MC_U105178783] Funding Source: UKRI
- Australian Research Council [DE170100054] Funding Source: Australian Research Council
The order of enzymatic activity across Golgi cisternae is essential for complex molecule biosynthesis. However, an inability to separate Golgi cisternae has meant that the cisternal distribution of most resident proteins, and their underlying localization mechanisms, are unknown. Here, we exploit differences in surface charge of intact cisternae to perform separation of early to late Golgi subcompartments. We determine protein and glycan abundance profiles across the Golgi; over 390 resident proteins are identified, including 136 new additions, with over 180 cisternal assignments. These assignments provide a means to better understand the functional roles of Golgi proteins and how they operate sequentially. Protein and glycan distributions are validated in vivo using high-resolution microscopy. Results reveal distinct functional compartmentalization among resident Golgi proteins. Analysis of transmembrane proteins shows several sequence-based characteristics relating to pl, hydrophobicity, Ser abundance, and Phe bilayer asymmetry that change across the Golgi. Overall, our results suggest that a continuum of transmembrane features, rather than discrete rules, guide proteins to earlier or later locations within the Golgi stack.
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