Delivery of a Secreted Soluble Protein to the Vacuole via a Membrane Anchor1

Barrieu, François; Chrispeels, Maarten J.

doi:10.1104/pp.120.4.961

Cited by 30 publications

(41 citation statements)

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“…This is in agreement with all previous reports (Barrieu and Chrispeels, 1999;Benghezal et al, 2000;Brandizzi et al, 2002;daSilva et al, 2006).…”

Section: The Drag-and-drop Assay Reveals Receptor Transit Via the Pm supporting

confidence: 83%

“…Earlier studies pointed either to the PM (Benghezal et al, 2000) or the tonoplast (Barrieu and Chrispeels, 1999) as the default location. In yeast, removal of the cytosolic tail of the VSR (VPS10) results in accelerated degradation in the vacuole (Cereghino et al, 1995;Cooper and Stevens, 1996).…”

Section: Where Is the Default Location For Type 1 Membrane-spanning Pmentioning

confidence: 99%

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Golgi-Dependent Transport of Vacuolar Sorting Receptors Is Regulated by COPII, AP1, and AP4 Protein Complexes in Tobacco

et al. 2014

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The cycling of vacuolar sorting receptors (VSRs) between early and late secretory pathway compartments is regulated by signals in the cytosolic tail, but the exact pathway is controversial. Here, we show that receptor targeting in tobacco (Nicotiana tabacum) initially involves a canonical coat protein complex II-dependent endoplasmic reticulum-to-Golgi bulk flow route and that VSRligand interactions in the cis-Golgi play an important role in vacuolar sorting. We also show that a conserved Glu is required but not sufficient for rate-limiting YXXɸ-mediated receptor trafficking. Protein-protein interaction studies show that the VSR tail interacts with the m-subunits of plant or mammalian clathrin adaptor complex AP1 and plant AP4 but not that of plant and mammalian AP2. Mutants causing a detour of full-length receptors via the cell surface invariantly cause the secretion of VSR ligands. Therefore, we propose that cycling via the plasma membrane is unlikely to play a role in biosynthetic vacuolar sorting under normal physiological conditions and that the conserved Ile-Met motif is mainly used to recover mistargeted receptors. This occurs via a fundamentally different pathway from the prevacuolar compartment that does not mediate recycling. The role of clathrin and clathrin-independent pathways in vacuolar targeting is discussed.

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“…This is in agreement with all previous reports (Barrieu and Chrispeels, 1999;Benghezal et al, 2000;Brandizzi et al, 2002;daSilva et al, 2006).…”

Section: The Drag-and-drop Assay Reveals Receptor Transit Via the Pm supporting

confidence: 83%

Section: Where Is the Default Location For Type 1 Membrane-spanning Pmentioning

confidence: 99%

Golgi-Dependent Transport of Vacuolar Sorting Receptors Is Regulated by COPII, AP1, and AP4 Protein Complexes in Tobacco

et al. 2014

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“…The problem of these approaches is that the location of the membrane protein itself is not addressed directly by analyzing the location of membrane-bound reporters. Instead, conclusions are suggested indirectly from the location of a soluble reporter released from the membrane chimera.As proposed by Barrieu and Chrispeels (1999), it is possible that, while reaching a lytic compartment on its way to its default destination, a chimeric membrane protein releases its reporter. The released soluble protein then can be transported farther down the secretory pathway while the membrane portion remains in a different location.…”

mentioning

confidence: 99%

The Destination for Single-Pass Membrane Proteins Is Influenced Markedly by the Length of the Hydrophobic Domain

Brandizzí

Frangne

Marc-Martin³

et al. 2002

Plant Cell

212

255

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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. INTRODUCTIONThe sorting of integral proteins in plants is not well understood. Nevertheless, it is accepted that peptidic signals exposed in the cytosol are responsible for targeting to the correct subcellular location in plant cells. This signal-mediated sorting is opposed to a default transport that is believed to happen when no signal is present on a protein.Although the default destination within the secretory pathway for a soluble protein is secretion, the default membrane is unclear. The most informative results about the location where membrane proteins would accumulate by default were provided by a study of ␣ -TIP (Höfte and Chrispeels, 1992). In this experiment, the last 48 amino acids of ␣ -TIP, which contains the sixth transmembrane domain, were sufficient to target a reporter protein to the tonoplast. Because the deletion of the cytosolic C-terminal 15 amino acids from the ␣ -TIP sequence did not prevent the tonoplast accumulation of the truncated protein, the authors indirectly deduced a role for the sixth membrane-spanning domain. Either this ␣ -TIP transmembrane domain would be sufficient for vacuolar location or the tonoplast would be the default destination for membrane proteins.More recently, the same sixth transmembrane domain of ␣ -TIP was used in a chimeric c...

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“…This hypothesis was further tested with type I membrane-spanning reporter fusions constructed from ER residents and mutagenesis of the known ER retention signals. One of these studies confirmed the tonoplast as default (Barrieu and Chrispeels, 1999), whereas the other suggested the PM (Benghezal et al, 2000).…”

Section: Transport Of Membrane Proteinsmentioning

confidence: 65%

“…The problem with many of these studies is that the reporter fusion is proteolytically cleaved and leads to the detection of the soluble reporter in either the vacuole (Barrieu and Chrispeels, 1999;Langhans et al, 2008) or the extracellular medium (Benghezal et al, 2000). Depending on the position in the secretory pathway, cleavage can either lead to secretion from the Golgi or vacuolar transport from the PVC, but it would be ideal to have a reporter that is stable.…”

Section: Transport Of Membrane Proteinsmentioning

confidence: 99%