Expression and Regulation of aERD2, a Gene Encoding the KDEL Receptor Homolog in Plants, and Other Genes Encoding Proteins Involved in ER-Golgi Vesicular Trafficking.

Bar‐Peled, Maor; Conceição, Alexandre da Silva; Frigerio, Lorenzo; Raikhel, Natasha V.

doi:10.1105/tpc.7.6.667

Cited by 52 publications

(29 citation statements)

References 35 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Both animals and fungi possess multiple members of each of the four subfamilies. While plants have been shown to encode components of COPcoated vesicles (d 'Enfert et al, 1992;Bar-Peled et al, 1995;Movafenghi et al, 1999;Contreras et al, 2000;Pimpl et al, 2000;Couchy, et al 2003), the sequenced genomes represented by Arabidopsis thaliana and Oryza sativa only contain members of the delta and beta p24 subfamilies. Given that these represent all of the p24 members in the fully sequenced Arabidopsis genome, this suggests that all four subfamilies are not necessary for normal COP-coated vesicle function as has been suggested previously (Dominguez et al, 1998;Fullekrug et al, 1999;Marzioch et al, 1999).…”

Section: Phylogenetic Relationships Of P24 Proteinsmentioning

confidence: 99%

p24 proteins, intracellular trafficking, and behavior: Drosophila melanogaster provides insights and opportunities

Carney

Bowen

2004

Biology of the Cell

View full text Add to dashboard Cite

The p24 transmembrane proteins, also known as EMP24/GP25 (endomembrane protein precursor of 24kD (Schimmoller et al., 1995)) proteins, are components of coat protein (COP)-coated vesicles and are present in species as diverse as fungi, plants, flies, worms, and mammals, indicating that they have important conserved functions. Genetic, molecular, and biochemical characterization of these proteins and the loci that encode them has provided insights into their potential cellular roles, including postulated functions in vesicle cargo protein selection and sorting, COPI and COPII vesicle formation and budding, and quality control of proteins that mature through the secretory pathway. Recently, the first mutations in a Drosophila melanogaster p24 gene have been isolated and characterized. These alleles produce an interesting behavioral phenotype in females, affecting their ability to oviposit. This identification and mutant characterization of a p24 locus in Drosophila will pave the way for a better understanding of cell-type-specific functions and interactions among p24 proteins.

show abstract

Section: Phylogenetic Relationships Of P24 Proteinsmentioning

confidence: 99%

p24 proteins, intracellular trafficking, and behavior: Drosophila melanogaster provides insights and opportunities

Carney

Bowen

2004

Biology of the Cell

View full text Add to dashboard Cite

show abstract

“…How this regulation is achieved is currently unclear, but is likely to be coordinated for many proteins involved in vesicular trafficking to the vacuole. Indeed, the level of many proteins of the secretory pathway appears to be higher in roots than in most other tissues (Bar-Peled et al, 1995;Ahmed et al, 1997;Conceição et al, 1997). The role of these proteins in general vacuolar targeting in all cell types and in specialized tissues such as developing seeds is currently under investigation.…”

Section: Expression Pattern Of Plant Secretory Pathway Proteinsmentioning

confidence: 99%

“…RNA was isolated from leaves, roots, flowers, and inflorescence stems of A. thaliana (ecotype Columbia) as described previously (Bar-Peled et al, 1995). Equal amounts (30 g) of total RNA were separated on a 1.2% agarose/6% formaldehyde gel and transferred to nylon membrane.…”

Section: Rna-blot Analysismentioning

confidence: 99%

“…To generate large quantities of root tissue, A. thaliana was grown in liquid culture as described in Bar-Peled et al (1995). Roots were ground in extraction buffer (100 mm Tris-HCl, pH 7.5, 400 mm Suc, 1 mm EDTA, and 0.1 mm PMSF) using a mortar and pestle, and debris were pelleted by centrifugation at 1,000g for 5 min.…”

Section: Preparation Of Microsomal Fractionsmentioning

confidence: 99%

See 1 more Smart Citation

An Arabidopsis VPS45p Homolog Implicated in Protein Transport to the Vacuole1

Bassham

Raikhel

1998

Plant Physiology

View full text Add to dashboard Cite

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...

show abstract

“…Budding of vesicles from the ER involves a number of periphera1 membrane proteins (Sarlp, Sec23 / 24p complex, and Secl3 / 31p form a complex collectively termed the COPII coat), together with at least one integral ER-membrane protein, Secl2p (Salama et al, 1993;Barlowe et al, 1994;Salama and Schekman, 1995). Functional plant genes with homology to the SAR1, SEC12, SEC13, and SEC23 genes have been isolated (dEnfert et al, 1992;Bar-Peled et al, 1995;M. Bar-Peled and N.V. Raikhel, unpublished data).…”

mentioning

confidence: 99%

Characterization of AtSEC12 and AtSAR1 (Proteins Likely Involved in Endoplasmic Reticulum and Golgi Transport)

1997

Self Cite

View full text Add to dashboard Cite

Transport of cargo proteins from the endoplasmic reticulum (ER) to the cis-Golgi network is mediated by protein-coated vesicles. The coat, called COPII coat, consists of proteins that are recruited from the cytosol and interact with integral membrane proteins of the ER. In yeast, both cytosolic proteins (Sec13/31, Sec23/24, and Sar1) and ER-associated proteins (Sec12 and others) have been purified and characterized and it has been possible to demonstrate transport vesicle formation in vitro. Arabidopsis thaliana homologs of Sar1 and Sec12 have recently been identified, but little is known about the properties of the proteins or their subcellular distribution. Here we demonstrate that AtSAR1, a 22-kD protein that binds GTP, and AtSEC12, a 43-kD GTP-exchange protein, are both associated with the ER. However, about one-half of the cellular AtSAR1 is present in the cytosol. When AtSAR1 is overexpressed in transgenic plants, the additional protein is also cytosolic. When tissue-culture cells are cold-shocked (12 h at 8[deg]C), AtSAR1 levels appeared to decline and a larger proportion of the total protein was found in the cytosol. Given the known function of AtSAR1 in yeast, we propose that the amount of ER-associated AtSAR1 is an indication of the intensity of the secretory process. Thus, we expect that such a cold shock will adversely affect ER-to-Golgi transport of proteins.

show abstract

Expression and Regulation of aERD2, a Gene Encoding the KDEL Receptor Homolog in Plants, and Other Genes Encoding Proteins Involved in ER-Golgi Vesicular Trafficking.

Cited by 52 publications

References 35 publications

p24 proteins, intracellular trafficking, and behavior: Drosophila melanogaster provides insights and opportunities

p24 proteins, intracellular trafficking, and behavior: Drosophila melanogaster provides insights and opportunities

An Arabidopsis VPS45p Homolog Implicated in Protein Transport to the Vacuole1

Characterization of AtSEC12 and AtSAR1 (Proteins Likely Involved in Endoplasmic Reticulum and Golgi Transport)

Contact Info

Product

Resources

About