ArticleThe Plant cell2009
The rice alpha-amylase glycoprotein is targeted from the Golgi apparatus through the secretory pathway to the plastids.
Article in The Plant cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.
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Who cites it
70 citing papers in PubMed, 148 citations in OpenAlex.
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- Stress on the Endoplasmic Reticulum Impairs the Photosynthetic Efficiency of Chlamydomonas.International journal of molecular sciences · 2024Article
- A cargo sorting receptor mediates chloroplast protein trafficking through the secretory pathway.The Plant cell · 2024Article
- Transcriptomic Profiling of Two Rice Thermo-Sensitive Genic Male Sterile Lines with Contrasting Seed Storability after Artificial Accelerated Aging Treatment.Plants (Basel, Switzerland) · 2024Article
- Genome-Wide Identification, Characterization, and Expression Analysis of Four Subgroup Members of the GH13 Family in Wheat (International journal of molecular sciences · 2024Article
- Morphological, Molecular Structural and Physicochemical Characterization of Starch Granules Formed in Endosperm of Rice with Ectopic Overexpression of α-Amylase.Journal of applied glycoscience · 2024Article
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- Tracking N-terminal protein processing from the Golgi to the chromatophore of a rhizarian amoeba.Plant physiology · 2022Article
- A bipartite chromatophore transit peptide and N-terminal protein processing in the Paulinella chromatophore.Plant physiology · 2022Article
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- Recent Advances in Carbon and Nitrogen Metabolism in C3 Plants.International journal of molecular sciences · 2020Review
- The Lipid Transfer Protein 1 fromViruses · 2020Article
- Inhibition of endosomal trafficking by brefeldin A interferes with long-distance interaction between chloroplasts and plasma membrane transporters.Physiologia plantarum · 2020Article
- A Cytosol-Localized Geranyl Diphosphate Synthase fromPlant physiology · 2020Article
- Functional Analysis of Rice Long-Chain Acyl-CoA Synthetase 9 (International journal of molecular sciences · 2020Article
- Fluorescent reporters for functional analysis in rice leaves.Plant direct · 2020Article
- HS1 Is Involved in Hygromycin Resistance Through Facilitating Hygromycin Phosphotransferase Transportation From Cytosol to Chloroplast.Frontiers in plant science · 2020Article
10 more citing papers are in PubMed but not listed here.
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Authors and funding
12 authors at 6 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The well-characterized secretory glycoprotein, rice (Oryza sativa) alpha-amylase isoform I-1 (AmyI-1), was localized within the plastids and proved to be involved in the degradation of starch granules in the organelles of rice cells. In addition, a large portion of transiently expressed AmyI-1 fused to green fluorescent protein (AmyI-1-GFP) colocalized with a simultaneously expressed fluorescent plastid marker in onion (Allium cepa) epidermal cells. The plastid targeting of AmyI-1 was inhibited by both dominant-negative and constitutively active mutants of Arabidopsis thaliana ARF1 and Arabidopsis SAR1, which arrest endoplasmic reticulum-to-Golgi traffic. In cells expressing fluorescent trans-Golgi and plastid markers, these fluorescent markers frequently colocalized when coexpressed with AmyI-1. Three-dimensional time-lapse imaging and electron microscopy of high-pressure frozen/freeze-substituted cells demonstrated that contact of the Golgi-derived membrane vesicles with cargo and subsequent absorption into plastids occur within the cells. The transient expression of a series of C-terminal-truncated AmyI-1-GFP fusion proteins in the onion cell system showed that the region from Trp-301 to Gln-369 is necessary for plastid targeting of AmyI-1. Furthermore, the results obtained by site-directed mutations of Trp-302 and Gly-354, located on the surface and on opposite sides of the AmyI-1 protein, suggest that multiple surface regions are necessary for plastid targeting. Thus, Golgi-to-plastid traffic appears to be involved in the transport of glycoproteins to plastids and plastid targeting seems to be accomplished in a sorting signal-dependent manner.
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