ArticleThe Plant cell2000
Structural requirements for ligand binding by a probable plant vacuolar sorting receptor.
Article in The Plant cell, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 110 citations in OpenAlex.
- Structural insights into how vacuolar sorting receptor recognizes the C-terminal sorting determinant of a vicilin-like seed storage protein.The FEBS journal · 2026Article
- Functional implication of the homotrimeric multidomain vacuolar sorting receptor 1 (VSR1) from Arabidopsis thaliana.Scientific reports · 2024Article
- Structural insights into how vacuolar sorting receptors recognize the sorting determinants of seed storage proteins.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- MTV proteins unveil ER- and microtubule-associated compartments in the plant vacuolar trafficking pathway.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Nanobody-triggered lockdown of VSRs reveals ligand reloading in the Golgi.Nature communications · 2018Article
- A vacuolar sorting receptor-independent sorting mechanism for storage vacuoles in soybean seeds.Scientific reports · 2018Article
- The Multivesicular Body and Autophagosome Pathways in Plants.Frontiers in plant science · 2018Article
- Dimerization of the Vacuolar Receptors AtRMR1 and -2 from Arabidopsis thaliana Contributes to Their Localization in the trans-Golgi Network.International journal of molecular sciences · 2016Article
- Preliminary X-ray analysis of the binding domain of the soybean vacuolar sorting receptor complexed with a sorting determinant of a seed storage protein.Acta crystallographica. Section F, Structural biology communications · 2015Article
- Article
- Vacuolar Sorting Receptor-Mediated Trafficking of Soluble Vacuolar Proteins in Plant Cells.Plants (Basel, Switzerland) · 2014Review
- Contribution of chitinase A's C-terminal vacuolar sorting determinant to the study of soluble protein compartmentation.International journal of molecular sciences · 2014Review
- Functional identification of sorting receptors involved in trafficking of soluble lytic vacuolar proteins in vegetative cells of Arabidopsis.Plant physiology · 2013Article
- Mechanisms and concepts paving the way towards a complete transport cycle of plant vacuolar sorting receptors.The Plant cell · 2012Review
- Vacuolar transport in tobacco leaf epidermis cells involves a single route for soluble cargo and multiple routes for membrane cargo.The Plant cell · 2011Article
- Structural basis for Ca2+-independence and activation by homodimerization of tomato subtilase 3.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Sorting and anterograde trafficking at the Golgi apparatus.Plant physiology · 2008Article
- Wall associated kinases from plants - an overview.Physiology and molecular biology of plants : an international journal of functional plant biology · 2008Article
- The secretory system of Arabidopsis.The arabidopsis book · 2008Article
- Protein mobilization in germinating mung bean seeds involves vacuolar sorting receptors and multivesicular bodies.Plant physiology · 2007Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
How sorting receptors recognize amino acid determinants on polypeptide ligands and respond to pH changes for ligand binding or release is unknown. The plant vacuolar sorting receptor BP-80 binds polypeptide ligands with a central Asn-Pro-Ile-Arg (NPIR) motif. tBP-80, a soluble form of the receptor lacking transmembrane and cytoplasmic sequences, binds the peptide SSSFADSNPIRPVTDRAASTYC as a monomer with a specificity indistinguishable from that of BP-80. tBP-80 contains an N-terminal region homologous to ReMembR-H2 (RMR) protein lumenal domains, a unique central region, and three C-terminal epidermal growth factor (EGF) repeats. By protease digestion of purified secreted tBP-80, and from ligand binding studies with a secreted protein lacking the EGF repeats, we defined three protease-resistant structural domains: an N-terminal/RMR homology domain connected to a central domain, which together determine the NPIR-specific ligand binding site, and a C-terminal EGF repeat domain that alters the conformation of the other two domains to enhance ligand binding. A fragment representing the central domain plus the C-terminal domain could bind ligand but was not specific for NPIR. These results indicate that two tBP-80 binding sites recognize two separate ligand determinants: a non-NPIR site defined by the central domain-EGF repeat domain structure and an NPIR-specific site contributed by the interaction of the N-terminal/RMR homology domain and the central domain.
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