ArticleNature communications2025
Amylopectin branch trimming and biosynthesis elucidated by the rice isoamylase ISA1-ISA2 heterocomplex.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed.
- Polyploidization-Driven Functional Innovation of AGPase Small Subunit GeneInternational journal of molecular sciences · 2026Article
- A structural perspective on α-glucan catabolism in oxygenic phototrophs.The Plant journal : for cell and molecular biology · 2026Review
- Noncatalytic functions of ISOAMYLASE 1 and 2 affect the proportion of insoluble and soluble α-polyglucans in maize.The Plant cell · 2025Article
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Authors and funding
13 authors.
Funding
Abstract
Amylopectin, the primary form of starch in plant leaves, seeds and tubers, features a tree-like architecture with branched glucose chains. Excess branches result in the formation of soluble phytoglycogen instead of starch granules. In higher plants and green algae, the debranching enzyme isoamylase ISA1 forms either homomultimer or hetero-multimer with ISA2 to facilitate branch trimming and starch granule formation, but the molecular basis remains largely unknown. In this study, we reconstitute the rice OsISA1-ISA2 complex in vitro and determine the cryo-EM structures of the OsISA1 homodimer, as well as the malto-oligosaccharide (MOS)-free and MOS-bound OsISA1-ISA2 heterocomplex. The OsISA1 dimer shows a tail-to-tail rod-like architecture, whereas the OsISA1-ISA2 complex mainly exhibits as a trimer, with OsISA2 flanking on the N-terminal segments of the dimeric OsISA1. Combined with comprehensive biochemical analyses, these structural data elucidate the organization of the ISA1-ISA2 heterocomplex in higher plants and demonstrate how ISA1 and ISA2 cooperate during amylopectin biosynthesis.
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