Transport of proteins in eukaryotic cells: more questions ahead

Bar‐Peled, Maor; Bassham, Diane C.; Raikhel, Natasha V.

doi:10.1007/bf00039384

Cited by 30 publications

(5 citation statements)

References 288 publications

(316 reference statements)

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“…Secreted and membrane-spanning proteins contain targeting domains (transmembrane signal anchors or amino terminus signal peptides) that direct the protein to the endoplasmic reticulum (Bar-Peled et al, 1996) where they are exposed to N-linked glycosylation at specific sites (Asn-X-Ser/Thr; Hirschberg and Snider, 1987). The gene trap transposon used in our experiments has splice donor sites at the 5Ј end of the transposon and carries a plant intron and splice acceptor sites preceding the GUS reporter gene Sundaresan et al, 1995).…”

Section: Strategy For Gene Trap Tagging Of Secreted Proteinsmentioning

confidence: 99%

Secretion Trap Tagging of Secreted and Membrane-Spanning Proteins Using Arabidopsis Gene Traps

et al. 2003

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Secreted and membrane-spanning proteins play fundamental roles in plant development but pose challenges for genetic identification and characterization. We describe a “secretion trap” screen for gene trap insertions in genes encoding proteins routed through the secretory pathway. The gene trap transposon encodes a β-glucuronidase reporter enzyme that is inhibited by N-linked glycosylation specific to the secretory pathway. Treatment of seedlings with tunicamycin inhibits glycosylation, resulting in increased activity of secreted β-glucuronidase fusions that result from gene trap integration downstream of exons encoding signal peptides. In the 2,059 gene trap lines that we screened, 32 secretion trap expression patterns were identified in a wide variety of tissues including embryos, meristems, and the developing vasculature. Genes disrupted by the secretion traps encode putative extracellular signaling proteins, membrane transport proteins, and novel secreted proteins of unknown function missed by conventional mutagenesis and gene prediction. Secretion traps provide a unique reagent for gene expression studies and can guide the genetic combination of loss of function alleles in related genes.

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Section: Strategy For Gene Trap Tagging Of Secreted Proteinsmentioning

confidence: 99%

Secretion Trap Tagging of Secreted and Membrane-Spanning Proteins Using Arabidopsis Gene Traps

et al. 2003

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“…The deduced amino acid sequence of the BFN1, ZEN2, and ZEN3 proteins start with a typical signal peptide, indicating that these proteins also enter the secretory pathway. They also lack a KDEL-like sequence for retention in the endoplasmic reticulum or an obvious C-or N-terminal vacuolar targeting signal (Bar-Peled et al, 1996), so they too may be extracellular. It is not yet clear whether the amino acid sequences of senescenceassociated nuclease I enzymes have any distinct features, but this issue should be resolved once more genes are characterized.…”

Section: Insight From Bfn1 Structurementioning

confidence: 99%

Identification of BFN1, a Bifunctional Nuclease Induced during Leaf and Stem Senescence in Arabidopsis

et al. 2000

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Nuclease I enzymes are responsible for the degradation of RNA and single-stranded DNA during several plant growth and developmental processes, including senescence. However, in the case of senescence the corresponding genes have not been reported. We describe the identification and characterization of BFN1 of Arabidopsis, and demonstrate that it is a senescence-associated nuclease I gene. BFN1 nuclease shows high similarity to the sequence of a barley nuclease induced during germination and a zinnia (Zinnia elegans) nuclease induced during xylogenesis. In transgenic plants overexpressing the BFN1 cDNA, a nuclease activity of about 38 kD was detected on both RNase and DNase activity gels. Levels of BFN1 mRNA were extremely low or undetectable in roots, leaves, and stems. In contrast, relatively high BFN1 mRNA levels were detected in flowers and during leaf and stem senescence. BFN1 nuclease activity was also induced during leaf and stem senescence. The strong response of the BFN1 gene to senescence indicated that it would be an excellent tool with which to study the mechanisms of senescence induction, as well as the role of the BFN1 enzyme in senescence using reverse genetic approaches in Arabidopsis.

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“…Protein expression of the GST-fusion construct was induced by adding 0.2 mM isopropylthio-p-galactoside and shifting the cell culture to 28°C. The soluble GST-fusion protein was purified by affinity chromatography as described previously (Bar-Peled and Raikhel, 1996). The fusion protein (approximately 100 pg) was emulsified with Titer-Max (CytRx, Norcross, GA) in a total of 1 mL and injected into rabbits.…”

Section: Preparation Of Antibodiesmentioning

confidence: 99%

“…Upon arrival at the TGN, vacuolar and secreted proteins are sorted and transported to their respective destinations (Bar-Peled et al, 1996;Rothman, 1996). The transport of many of these cargo proteins through the secretory pathway is mediated by small vesicles, a process requiring specific soluble and membrane proteins (Rothman and Wieland, 1996).…”

mentioning

confidence: 99%

Cloning and Subcellular Location of an Arabidopsis Receptor-Like Protein That Shares Common Features with Protein-Sorting Receptors of Eukaryotic Cells

1997

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Many receptors involved in clathrin-mediated protein transport through the endocytic and secretory pathways of yeast and animal cells share common features. They are all type I integral membrane proteins containing cysteine-rich lumenal domains and cytoplasmic tails with tyrosine-containing sorting signals. The cysteine-rich domains are thought to be involved in ligand binding, whereas the cytoplasmic tyrosine motifs interact with clathrin-associated adaptor proteins during protein sorting along these pathways. In addition, tyrosine-containing signals are required for the retention and recycling of some of these membrane proteins to the trans-Golgi network. Here we report the characterization of an approximately 80-kD epidermal growth factor receptor-like type I integral membrane protein containing all of these functional motifs from Arabidopsis thaliana (called AtELP for A. thaliana Epidermal growth factor receptor-Like Protein). Biochemical analysis indicates that AtELP is a membrane protein found at high levels in the roots of both monocots and dicots. Subcellular fractionation studies indicate that the AtELP protein is present in two membrane fractions corresponding to a novel, undefined compartment and a fraction enriched in vesicles containing clathrin and its associated adaptor proteins. AtELP may therefore serve as a marker for compartments involved in intracellular protein trafficking in the plant cell.

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Transport of proteins in eukaryotic cells: more questions ahead

Cited by 30 publications

References 288 publications

Secretion Trap Tagging of Secreted and Membrane-Spanning Proteins Using Arabidopsis Gene Traps

Secretion Trap Tagging of Secreted and Membrane-Spanning Proteins Using Arabidopsis Gene Traps

Identification of BFN1, a Bifunctional Nuclease Induced during Leaf and Stem Senescence in Arabidopsis

Cloning and Subcellular Location of an Arabidopsis Receptor-Like Protein That Shares Common Features with Protein-Sorting Receptors of Eukaryotic Cells

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