The Arabidopsis endoplasmic reticulum retention receptor functions in yeast.

Lee, Hyungyil; Gal, Susannah; Newman, Thomas C.; Raikhel, Natasha V.

doi:10.1073/pnas.90.23.11433

Cited by 102 publications

(100 citation statements)

References 51 publications

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“…This is reminiscent of the results observed for another secretory pathway gene, AtERD2, which is involved in the retrieval of resident ER proteins from the Golgi complex (Lee et al, 1993). This indicates that AtVPS45p is functionally related to yeast Vps45p and can substitute for the protein in yeast vacuolar transport.…”

Section: Function Of Vps45-like Proteinssupporting

confidence: 61%

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: Function Of Vps45-like Proteinssupporting

confidence: 61%

An Arabidopsis VPS45p Homolog Implicated in Protein Transport to the Vacuole1

Bassham

Raikhel

1998

Plant Physiology

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“…ERD2 must recycle between the ER and Golgi apparatus to carry out its function and, although its recycling via COPI vesicles is well established (Lee et al, 1993), much less is known about its ER export properties. Because it has been shown that a COPII-independent pathway for ER export exists in plants (Törmäkangas et al, 2001), we first wanted to ensure that the ER export of ERD2 is dependent on COPII machinery.…”

Section: Overexpression Of Sec24 Does Not Affect Movement Of Proteinsmentioning

confidence: 99%

“…ERD2-GFP is a well-known receptor that retrieves escaped soluble proteins to the ER and cycles continuously between the ER and Golgi apparatus (Lee et al, 1993;Brandizzi et al, 2002c) in a COPII-dependent manner (Fig. 2).…”

Section: Eres Biogenesis Is Cargo Inducedmentioning

confidence: 99%

“…The binary vector pVKH18En6 (Batoko et al, 2000) is the binary vector used for Agrobacterium tumefaciens-mediated transformation in this study. The GFP-Golgi markers used were the Arabidopsis (Arabidopsis thaliana) H/KDEL receptor ERD2 (Lee et al, 1993;Boevink et al, 1998;Brandizzi et al, 2002c;Saint-Jore et al, 2002) and the synthetic secretory membrane cargo protein TMcCCASP (Hanton et al, 2005b). A mutant of TMcCCASP (TMcCCASP DXE1 ) that is impaired in ER to Golgi transport was also utilized (Hanton et al, 2005b).…”

Section: Fluorescent Proteins and Molecular Cloningmentioning

confidence: 99%

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De Novo Formation of Plant Endoplasmic Reticulum Export Sites Is Membrane Cargo Induced and Signal Mediated

et al. 2007

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The plant endoplasmic reticulum (ER) contains functionally distinct subdomains at which cargo molecules are packed into transport carriers. To study these ER export sites (ERES), we used tobacco (Nicotiana tabacum) leaf epidermis as a model system and tested whether increased cargo dosage leads to their de novo formation. We have followed the subcellular distribution of the known ERES marker based on a yellow fluorescent protein (YFP) fusion of the Sec24 COPII coat component (YFP-Sec24), which, differently from the previously described ERES marker, tobacco Sar1-YFP, is visibly recruited at ERES in both the presence and absence of overexpressed membrane cargo. This allowed us to quantify variation in the ERES number and in the recruitment of Sec24 to ERES upon expression of cargo. We show that increased synthesis of membrane cargo leads to an increase in the number of ERES and induces the recruitment of Sec24 to these ER subdomains. Soluble proteins that are passively secreted were found to leave the ER with no apparent up-regulation of either the ERES number or the COPII marker, showing that bulk flow transport has spare capacity in vivo. However, de novo ERES formation, as well as increased recruitment of Sec24 to ERES, was found to be dependent on the presence of the diacidic ER export motif in the cytosolic domain of the membrane cargo. Our data suggest that the plant ER can adapt to a sudden increase in membrane cargo-stimulated secretory activity by signal-mediated recruitment of COPII machinery onto existing ERES, accompanied by de novo generation of new ERES.

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“…A membrane-bound receptor encoded by the yeast ERD2 gene retrieves escaping HDEL-marked proteins from the Golgi apparatus or salvage compartment back to the ER Semenza et al, 1990). Homologs of the Erd2 receptor have been cloned from mammals Pelham, 1990, 1992; Tang et al, 1993) and plants ( Lee et al, 1993), highlighting conservation of the H/KDEL motif and retrieval mechanism.In mammals and yeast, the cytosolic dilysine motif is critical for ER localization of type I membrane proteins (Nilsson et al, 1989;Jackson et al, 1990). The two lysine residues need to be in either the Ϫ 3, Ϫ 4 (KKXX) or Ϫ 3, Ϫ 5 (KXKXX) positions relative to the C terminus, and no other basic amino acid can be substituted (Jackson et al, 1990(Jackson et al, , 1993.…”

mentioning

confidence: 99%

The C-Terminal Dilysine Motif Confers Endoplasmic Reticulum Localization to Type I Membrane Proteins in Plants

2000

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The tomato Cf-9 disease resistance gene encodes a type I membrane protein carrying a cytosolic dilysine motif. In mammals and yeast, this motif promotes the retrieval of type I membrane proteins from the Golgi apparatus to the endoplasmic reticulum (ER). To test whether the C-terminal KKXX signal of Cf-9 is functional as a retrieval motif and to investigate its role in plants, green fluorescent protein (GFP) was fused to the transmembrane domain of Cf-9 and expressed in yeast, Arabidopsis, and tobacco cells. The fusion protein was targeted to the ER in each of these expression systems, and mutation of the KKXX motif to NNXX led to secretion of the fusion protein. In yeast, the mutant protein reached the vacuole, but plants secreted it as a soluble protein after proteolytic removal of the transmembrane domain. Triple hemagglutinin (HA)-tagged full-length Cf-9 was also targeted to the ER in tobacco cells, and cleavage was also observed for the NNXX mutant protein, suggesting an endoprotease recognition site located within the Cf-9 lumenal sequence common to both the GFP-and the HA-tagged fusions. Our results indicate that the KKXX motif confers ER localization in plants as well as mammals and yeast and that Cf-9 is a resident protein of the ER. INTRODUCTIONProteins resident in the endoplasmic reticulum (ER) contain structural motifs responsible for their correct subcellular localization. Many soluble ER proteins, such as BiP or protein disulfide isomerase, carry a C-terminal tetrapeptide H/KDEL motif for localization in the ER (Munro and Pelham, 1987;Pelham et al., 1988;Mazzarella et al., 1990;Andres et al., 1991; Denecke et al., 1992 Denecke et al., , 1993Napier et al., 1992). A membrane-bound receptor encoded by the yeast ERD2 gene retrieves escaping HDEL-marked proteins from the Golgi apparatus or salvage compartment back to the ER Semenza et al., 1990). Homologs of the Erd2 receptor have been cloned from mammals Pelham, 1990, 1992; Tang et al., 1993) and plants ( Lee et al., 1993), highlighting conservation of the H/KDEL motif and retrieval mechanism.In mammals and yeast, the cytosolic dilysine motif is critical for ER localization of type I membrane proteins (Nilsson et al., 1989;Jackson et al., 1990). The two lysine residues need to be in either the Ϫ 3, Ϫ 4 (KKXX) or Ϫ 3, Ϫ 5 (KXKXX) positions relative to the C terminus, and no other basic amino acid can be substituted (Jackson et al., 1990(Jackson et al., , 1993. Mutation of lysine residues leads to expression of the reporter protein on the cell surface in mammals (Nilsson et al., 1989;Jackson et al., 1990) and to its vacuolar delivery in yeast (Gaynor et al., 1994). Studies of the post-translational modification kinetics of dilysine-tagged reporter proteins have demonstrated a constant cycling of the reporter from the ER to the Golgi apparatus and back to the ER (Jackson et al., 1993;Gaynor et al., 1994). The retrieval mechanism is mediated by vesicular Golgi apparatus-to-ER retrograde transport, involving the coat protein I (COPI) complex (Cosson and...

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The Arabidopsis endoplasmic reticulum retention receptor functions in yeast.

Cited by 102 publications

References 51 publications

An Arabidopsis VPS45p Homolog Implicated in Protein Transport to the Vacuole1

An Arabidopsis VPS45p Homolog Implicated in Protein Transport to the Vacuole1

De Novo Formation of Plant Endoplasmic Reticulum Export Sites Is Membrane Cargo Induced and Signal Mediated

The C-Terminal Dilysine Motif Confers Endoplasmic Reticulum Localization to Type I Membrane Proteins in Plants

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