The syntaxin homolog AtPEP12p resides on a late post-Golgi compartment in plants.

Conceição, Alexandre da Silva; Marty-Mazars, Danièle; Bassham, Diane C.; Sanderfoot, Anton A.; Marty, Francis; Raikhel, Natasha V.

doi:10.1105/tpc.9.4.571

Cited by 119 publications

(70 citation statements)

References 42 publications

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“…6). AtPEP12p, a syntaxin homolog that may be involved in vacuolar protein transport, resides on prevacuolar compartments (Conceição et al, 1997). AtELP (epidermal growth factor receptor-like Figure 5.…”

Section: Suc-gradient Fractionation Of Arabidopsis Membranesmentioning

confidence: 99%

“…Protein in each fraction was precipitated using TCA, and was analyzed by SDS-PAGE and immunoblotting. Blots were probed using AtVPS45p antibodies, AtPEP12p antibodies (Conceição et al, 1997), or AtELP antibodies (Ahmed et al, 1997), followed by secondary antibodies conjugated to alkaline phosphatase or horseradish peroxidase. The blots were digitized on a flat-bed scanner, and protein amounts were quantitated by densitometry using NIH Image software (National Institutes of Health, Bethesda, MD).…”

Section: Suc Gradientsmentioning

confidence: 99%

“…AtPEP12p is a homolog of yeast Pep12p, a syntaxin-like protein required for the correct targeting of several vacuolar hydrolases (Becherer et al, 1996). The ability of AtPEP12 to complement the yeast pep12⌬ mutant indicates that the protein may play a role in targeting proteins to the plant vacuole , possibly by acting as a receptor for vesicle trafficking from the Golgi complex to a post-Golgi, prevacuolar compartment (Conceição et al, 1997).…”

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confidence: 99%

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An Arabidopsis VPS45p Homolog Implicated in Protein Transport to the Vacuole1

Bassham

Raikhel

1998

Plant Physiology

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The Sec1p family of proteins is required for vesicle-mediated protein trafficking between various organelles of the endomembrane system. This family includes Vps45p, which is required for transport to the vacuole in yeast (Saccharomyces cerevisiae). We have isolated a cDNA encoding a VPS45 homolog from Arabidopsis thaliana (AtVPS45). The cDNA is able to complement both the temperature-sensitive growth defect and the vacuolar-targeting defect of a yeast vps45 mutant, indicating that the two proteins are functionally related. AtVPS45p is a peripheral membrane protein that associates with microsomal membranes. Sucrose-density gradient fractionation demonstrated that AtVPS45p co-fractionates with AtELP, a potential vacuolar protein sorting receptor, implying that they may reside on the same membrane populations. These results indicate that AtVPS45p is likely to function in the transport of proteins to the vacuole in plants.Soluble proteins that reside in the plant vacuole are initially translocated into the ER lumen and are then transported through the secretory pathway to the TGN, where vacuolar proteins are sorted from those that are to be secreted by virtue of a vacuolar-targeting signal. These signals are presumably recognized by receptor proteins in the TGN that allow transport to the vacuole. Two types of cleavable targeting signals have been identified: C-terminal propeptides and N-terminal propeptides, both of which are removed during deposition in the vacuole. Different mechanisms may be responsible for the transport of proteins containing different classes of signals Robinson and Hinz, 1997).Proteins are transported between organelles of the secretory pathway in vesicles that bud from one compartment and fuse with the next. The mechanism by which transport vesicles containing cargo proteins fuse with a target membrane has begun to be elucidated through a combination of biochemical studies of synaptic vesicle fusion with the presynaptic plasma membrane in mammalian neurons, and in genetic studies of secretion in yeast (Rothman, 1996). Similar sets of proteins were shown to be involved in the highly regulated fusion events in neurotransmission and the constitutive secretory system of yeast.These studies led to the proposal of the SNARE hypothesis to explain how a transport vesicle could be targeted to and fused with the correct organelle out of the many membrane-bound compartments of the cell. It was proposed that certain membrane proteins on the transport vesicle (v-SNAREs) and the target organelle (t-SNAREs) interact with each other and with several soluble proteins to allow docking of the vesicle with the target membrane and to promote vesicle fusion. For example, at the presynaptic membrane, a complex is formed between the v-SNARE synaptobrevin/vesicle-associated membrane protein and the t-SNAREs syntaxin and SNAP-25 (synaptosomeassociated protein of 25 kD), allowing the soluble factors N-ethylmaleimide-sensitive factor and ␣-SNAP (soluble N-ethylmaleimide-sensitive factor attachment protein) to bind. Hy...

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Section: Suc-gradient Fractionation Of Arabidopsis Membranesmentioning

confidence: 99%

Section: Suc Gradientsmentioning

confidence: 99%

mentioning

confidence: 99%

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An Arabidopsis VPS45p Homolog Implicated in Protein Transport to the Vacuole1

Bassham

Raikhel

1998

Plant Physiology

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“…Perhaps the solution to this enigma is to be found in splicing variants that give rise to alternative translation products. Isoenzyme formation in this manner has been proposed on several occasions Conceicao et al, 1997), and a cDNA coding for an ' anchorless ' human syntaxin Hsyn11 was recently described (Tang et al, 1998). The AtSyr1 sequence is also peculiar in this respect : it predicts a protein with an exceptionally long Cterminus containing a stretch of consecutive glycines.…”

Section: Placing Syntaxins In Ordermentioning

confidence: 99%

“…However, the pattern of At-Vam3 accumulation, prevalent on mature vacuolar membranes (Sato et al, 1997), is clearly different from that of At-Pep12. Conceicao et al (1997) reported that At-Pep12 associated with a prevacuolar compartment thought to be an intermediary step in vesicle transport from the transGolgi network (TGN). The vacuolar sorting receptor BP-80 and its orthologue AtELP (Ahmed et al, 1997 ;Paris et al, 1997 ;Sanderfoot et al, 1998) localize to equivalent prevacuolar compartments as well as to the TGN.…”

Section: Functional Analysis Of Plant Snares In Vesicle Traffickingmentioning

confidence: 99%

Tansley Review No. 108

1999

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Eukaryotic cells share a set of secretory pathways for the flux of membrane and protein material. In 1993, ideas about the functioning of three major proteins of the neurosecretory complex were consolidated in the SNARE hypothesis, which proposed that the interaction of these proteins provides both the specificity for vesicle targeting and the molecular machinery for fusion between vesicle and target membranes. Subsequetly, the organization, molecular mechanics and control of vesicle trafficking have become topics of intense research, and the hypothesis has evolved to accommodate new discoveries from the analysis of secretion in yeast and mammals. It is likely to be challenged again as more information comes to light about secretory processes in plants. New tools for measuring and manipulating vesicle traffic and secretion are now being used, drawing on in vivo fluorescence and capacitance recording as well as genetic engineering. These new technologies have already begun to yield details wholly unexpected from past studies. Here we focus on recent findings relating to the mechanisms of vesicle trafficking and the background to these developments, highlighting both current understanding of the molecular events of secretion and the gaps therein, as well as discussing emerging themes from work with plants.

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The Secretory System and Machinery for Protein Targeting

Gal

2018

Annual Plant Reviews Online

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The syntaxin homolog AtPEP12p resides on a late post-Golgi compartment in plants.

Cited by 119 publications

References 42 publications

An Arabidopsis VPS45p Homolog Implicated in Protein Transport to the Vacuole1

An Arabidopsis VPS45p Homolog Implicated in Protein Transport to the Vacuole1

Tansley Review No. 108

The Secretory System and Machinery for Protein Targeting

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