ArticleThe Plant cell2002
The destination for single-pass membrane proteins is influenced markedly by the length of the hydrophobic domain.
Article in The Plant cell, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 100 papers.
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Who cites it
100 citing papers in PubMed.
- Discovery and design of potent cell surface display elements.Nature biotechnology · 2026Article
- Should I stay or should I go-does protein localization to plasmodesmata depend on targeting signals?Journal of experimental botany · 2026Article
- Control of plasma membrane-associated actin polymerization specifies the pattern of the cell wall in xylem vessels.Nature communications · 2025Article
- Trafficking and localization of Golgi-residentFrontiers in plant science · 2025Review
- The CELL NUMBER REGULATOR FW2.2 protein regulates cell-to-cell communication in tomato by modulating callose deposition at plasmodesmata.Plant physiology · 2024Article
- Characterization of intracellular membrane structures derived from a massive expansion of endoplasmic reticulum (ER) membrane due to synthetic ER-membrane-resident polyproteins.Journal of experimental botany · 2024Article
- A tell tail sign: a conserved C-terminal tail-anchor domain targets a subset of pathogen effectors to the plant endoplasmic reticulum.Journal of experimental botany · 2023Article
- Dissecting the relative contribution of ECA3 and group 8/9 cation diffusion facilitators to manganese homeostasis inPlant direct · 2023Article
- Application of Green-enhanced Nano-lantern as a bioluminescent ratiometric indicator for measurement of Arabidopsis thaliana root apoplastic fluid pH.Plant, cell & environment · 2022Article
- A glossary of plant cell structures: Current insights and future questions.The Plant cell · 2022Review
- Review
- Direct trafficking pathways from the Golgi apparatus to the plasma membrane.Seminars in cell & developmental biology · 2020Review
- A novel cysteine-rich receptor-like kinase gene, TaCRK2, contributes to leaf rust resistance in wheat.Molecular plant pathology · 2020Article
- Chloroplast Acetyltransferase NSI Is Required for State Transitions inThe Plant cell · 2018Article
- Uncovering pH at both sides of the root plasma membrane interface using noninvasive imaging.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- The Cytokinin Oxidase/Dehydrogenase CKX1 Is a Membrane-Bound Protein Requiring Homooligomerization in the Endoplasmic Reticulum for Its Cellular Activity.Plant physiology · 2018Article
- Intracellular Distribution of Manganese by theThe Plant cell · 2017Article
- Structural characterization of a putative chitin synthase gene in Phytophthora spp. and analysis of its transcriptional activity during pathogenesis on potato and soybean plants.Current genetics · 2017Article
- An Update on the Intracellular and Intercellular Trafficking of Carmoviruses.Frontiers in plant science · 2017Review
- 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
40 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The tonoplast was proposed as a default destination of membrane-bound proteins without specific targeting signals. To investigate the nature of this targeting, we created type I fusion proteins with green fluorescent protein followed by the transmembrane domain of the human lysosomal protein LAMP1. We varied the length of the transmembrane domain from 23 to either 20 or 17 amino acids by deletion within the hydrophobic domain. The resulting chimeras, called TM23, TM20, and TM17, were expressed either transiently or stably in tobacco. TM23 clearly accumulated in the plasmalemma, as confirmed by immunoelectron microscopy. In contrast, TM17 clearly was retained in the endoplasmic reticulum, and TM20 accumulated in small mobile structures. The nature of the TM20-labeled compartments was investigated by coexpression with a marker localized mainly in the Golgi apparatus, AtERD2, fused to a yellow fluorescent protein. The strict colocalization of both fluorescent proteins indicated that TM20 accumulated in the Golgi apparatus. To further test the default destination of type I membrane proteins, green fluorescent protein was fused to the 19-amino acid transmembrane domain of the plant vacuolar sorting receptor BP-80. The resulting chimera also accumulated in the Golgi instead of in post-Golgi compartments, where native BP-80 localized. Additionally, when the transmembrane domain of BP-80 was lengthened to 22 amino acids, the reporter escaped the Golgi and accumulated in the plasma membrane. Thus, the tonoplast apparently is not a favored default destination for type I membrane proteins in plants. Moreover, the target membrane where the chimera concentrates is not unique and depends at least in part on the length of the membrane-spanning domain.
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