2001
DOI: 10.1078/0176-1617-00362
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The C-terminal tetrapeptide of phaseolin is sufficient to target green fluorescent protein to the vacuole

Abstract: SummaryPhaseolin is a vacuolar storage glycoprotein synthesized as a precursor with a short C-terminal propeptide. We have recently shown that deletion of the last four C-terminal amino acids (AFVY, which are part of, or constitute the propeptide) abolishes vacuolar targeting, causing phaseolin to be secreted. Here we provide biochemical and microscopical evidence that the AFVY tetrapeptide, when fused to a secreted version of green fluorescent protein (GFP), inhibits GFP secretion and leads to its accumulatio… Show more

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Cited by 42 publications
(54 citation statements)
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References 29 publications
(36 reference statements)
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“…uole (Frigerio et al, 2001a). After 1 h of pulse labeling, neither of the two GFP constructs could be coselected using anti-BiP antiserum ( Figure 3, lanes 5 to 8), indicating that permanence in the ER does not result directly in the interaction with BiP detected by our assay and that the addition of the vacuolar sorting signal of phaseolin does not stimulate interactions with BiP.…”
Section: The C-terminal Domain Of Phaseolin Stimulates the Interactiomentioning
confidence: 92%
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“…uole (Frigerio et al, 2001a). After 1 h of pulse labeling, neither of the two GFP constructs could be coselected using anti-BiP antiserum ( Figure 3, lanes 5 to 8), indicating that permanence in the ER does not result directly in the interaction with BiP detected by our assay and that the addition of the vacuolar sorting signal of phaseolin does not stimulate interactions with BiP.…”
Section: The C-terminal Domain Of Phaseolin Stimulates the Interactiomentioning
confidence: 92%
“…GFP is a small soluble protein that is secreted efficiently when introduced into the plant ER via a signal peptide (Batoko et al, 2000;Frigerio et al, 2001a). A number of C-terminal additions have been performed on ER-introduced GFP without affecting its fluorescence, and therefore its folding, in plant cells (Haseloff et al, 1997;Di Sansebastiano et al, 1998;Benghezal et al, 2000;Frigerio et al, 2001a).…”
Section: The C-terminal Domain Of Phaseolin Stimulates the Interactiomentioning
confidence: 99%
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“…D418 is a mutated form of phaseolin characterized by the absence of the tetrapeptide AFVY, which is responsible for protein delivery to the vacuole in tobacco cells (Frigerio et al, 1998(Frigerio et al, , 2001a. In this case, the ManD418 fusion protein, instead of being secreted, was mainly localized in the ER as an intact polypeptide, but its processed fragments were detected in the vacuole, indicating that the MAN2B1 200-amino acid domain can at least partially redirect the secreted protein D418 to this organelle.…”
Section: Discussionmentioning
confidence: 99%