Transport of Axl2p Depends on Erv14p, an ER–Vesicle Protein Related to the <i>Drosophila cornichon</i> Gene Product

Powers, Jacqueline; Barlowe, Charles

doi:10.1083/jcb.142.5.1209

Cited by 130 publications

(187 citation statements)

References 76 publications

(132 reference statements)

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“…Similar reductions in the transport rate of soluble secretory cargo have been observed in the absence of other specific ER cargo receptors, including Erv29p-dependent export of yeast gp␣f and CPY ) as well as the ERGIC53-dependent export of coagulation factors V/VII and procathepsin Z in animal cells (Nichols et al, 1998;Appenzeller et al, 1999). Some type I integral membrane cargo are also known to depend on cycling cargo receptors such as Erv14p (Powers and Barlowe, 1998), Emp47p (Sato and Nakano, 2003), and Vma21p (Malkus et al, 2004) for ER export. Currently, it is not known whether the cargo adaptor mechanism will be a common feature in ER export, because other transmembrane cargo proteins can bind directly to COPII subunits and are exported without apparent adaptors (Lee et al, 2004).…”

Section: Discussionmentioning

confidence: 61%

“…Our approach has been to investigate the function of abundant ER vesicle proteins (Ervs) that are enriched in purified COPII vesicle preparations (Otte et al, 2001). Several of the Erv proteins are involved in cargo sorting and when mutated they produce selective protein sorting defects (Schimmoller et al, 1995;Belden and Barlowe, 1996;Powers and Barlowe, 1998;Belden and Barlowe, 2001). In this report, we identify and characterize a new cargo-specific ER export factor, Erv26p.…”

Section: Introductionmentioning

confidence: 96%

“…In previous studies, we identified several of the abundant proteins contained on uncoated COPII vesicles by mass spectrometry, including Erv14p, Erv25p, Erv29p, Erv41p, and Erv46p (Belden and Barlowe, 1996;Powers and Barlowe, 1998;Otte et al, 2001). On further analysis of the protein species migrating with Erv25p, we detected polypeptides derived from the putative open reading frame YHR181w.…”

Section: Erv26p Is a Component Of Copii-coated Vesiclesmentioning

confidence: 99%

“…For indirect immunofluorescence, yeast cells were prepared and mounted as described previously (Powers and Barlowe, 1998). Immunofluorescent images were collected with a Hamamatsu (Bridgewater, NJ) Orca II cooled chargedcoupled device camera mounted on a Zeiss Axioplan 2 microscope (Carl Zeiss, Thornwood, NY), using OPENLAB software (Improvision, Lexington, MA).…”

Section: Fluorescence Microscopy and Green Fluorescent Protein (Gfp) mentioning

confidence: 99%

“…Subcellular fractionation was performed as described in Powers and Barlowe (1998) with minor modification as follows. Strains were grown to log phase and spheroplasted by lyticase treatment (Baker et al, 1988).…”

Section: Subcellular Fractionationmentioning

confidence: 99%

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Erv26p Directs Pro-Alkaline Phosphatase into Endoplasmic Reticulum–derived Coat Protein Complex II Transport Vesicles

Bue

Bentivoglio

Barlowe

2006

MBoC

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Secretory proteins are exported from the endoplasmic reticulum (ER) in transport vesicles formed by the coat protein complex II (COPII). We detected Erv26p as an integral membrane protein that was efficiently packaged into COPII vesicles and cycled between the ER and Golgi compartments. The erv26⌬ mutant displayed a selective secretory defect in which the pro-form of vacuolar alkaline phosphatase (pro-ALP) accumulated in the ER, whereas other secretory proteins were transported at wild-type rates. In vitro budding experiments demonstrated that Erv26p was directly required for packaging of pro-ALP into COPII vesicles. Moreover, Erv26p was detected in a specific complex with pro-ALP when immunoprecipitated from detergent-solublized ER membranes. Based on these observations, we propose that Erv26p serves as a transmembrane adaptor to link specific secretory cargo to the COPII coat. Because ALP is a type II integral membrane protein in yeast, these findings imply that an additional class of secretory cargo relies on adaptor proteins for efficient export from the ER. INTRODUCTIONThe eukaryotic secretory pathway transports a remarkable variety of cargo proteins to their proper cellular location. Several lines of evidence indicate that targeting information encoded within a secretory protein is recognized by the intracellular transport machinery to direct localization. Cytosolic coat protein complexes play an important role in deciphering targeting information and act in the selection of secretory proteins into appropriate transport intermediates (Bonifacino and Glick, 2004). However, the sorting signals and mechanisms by which coat complexes accommodate such diversity in secretory cargo remain poorly understood.Protein transport from the endoplasmic reticulum (ER) relies on coat protein complex II (COPII), which selects fully folded secretory cargo into ER-derived transport intermediates. COPII coats consist of the small GTPase Sar1p, the Sec23/24 complex, and the Sec13/31 complex (Barlowe et al., 1994). Biochemical and structural studies have demonstrated that the Sec24p subunit of this coat complex contains multiple cargo recognition sites and binds specific sorting signals displayed on the cytosolic regions of secretory proteins (Miller et al., 2003;Mossessova et al., 2003). Diacidic sequences and other polypeptide sorting signals have been identified in cargo proteins that interact with amino acid residues within defined Sec24p cargo recognition sites. Current models envisage that the cargo recognition and binding by Sec24p is stabilized through assembly of prebudding complexes consisting of Sec23/24 and Sar1p-GTP bound to secretory cargo on the ER membrane surface. These prebudding complexes are then incorporated into an outer layer Sec13/31 scaffold structure that deforms the membrane and produces COPII-coated vesicles (Lee et al., 2004;Stagg et al., 2006).In addition to the COPII coat proteins, cargo-specific accessory factors are required to accommodate the variety of secretory cargo exported from the ER in CO...

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Section: Discussionmentioning

confidence: 61%

Section: Introductionmentioning

confidence: 96%

Section: Erv26p Is a Component Of Copii-coated Vesiclesmentioning

confidence: 99%

Section: Fluorescence Microscopy and Green Fluorescent Protein (Gfp) mentioning

confidence: 99%

Section: Subcellular Fractionationmentioning

confidence: 99%

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Erv26p Directs Pro-Alkaline Phosphatase into Endoplasmic Reticulum–derived Coat Protein Complex II Transport Vesicles

Bue

Bentivoglio

Barlowe

2006

MBoC

Self Cite

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Differential expression of multiple genes during articular chondrocyte redifferentiation

Haudenschild¹,

McPherson²,

Tubo³

et al. 2001

Anat. Rec.

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Articular chondrocytes undergo a rapid change in phenotype and gene expression, termed dedifferentiation, when isolated from cartilage tissue and cultured on tissue culture plastic. On the other hand, "redifferentiation" of articular chondrocytes in suspension culture is characterized by decreased cellular proliferation and the reinitiation of synthesis of hyaline articular cartilage extracellular matrix molecules. The molecular triggers for these events have yet to be defined. Subtracted cDNA libraries representing genes involved in the early events of adult human articular chondrocyte redifferentiation were generated from human articular chondrocytes that were first cultured in monolayer, and subsequently transferred to suspension culture at 10 6 cells/ml for redifferentiation. Differential regulation of genes involved in cellular organization, nuclear structure, cellular growth regulation, and extracellular matrix deposition and remodeling were observed within 48 hr of this transfer. Many of these genes had not been previously identified in the chondrocyte differentiation pathway and a number of the isolated cDNAs did not have homologies to sequences in the public data banks. Genes involved in IL-6 signal transduction including acute phase response factor (APRF), Mn superoxide dismutase, and IL-6 itself were up-regulated in suspension culture. Membrane glycoprotein gp130, a component of the IL-6 receptor, was down-regulated. Other genes involved in cell polarity, cell adherence, apoptosis, and possibly TGF-beta signaling were differentially regulated. The differential regulation of the cytokine connective tissue growth factor (CTGF) during the early stages of articular chondrocyte redifferentiation, decreasing within 48 hours of transfer to suspension culture, was particularly interesting given its reported role in the stimulation of cellular proliferation. CTGF was highly expressed in proliferative monolayer culture, and then greatly reduced by redifferentiation in standard high-density suspension culture. When articular chondrocytes were seeded in suspension at low-density (10 4 cells/ml), however, high levels of CTGF were observed along with increased levels of mature articular cartilage extracellular matrix protein RNAs, such as type II collagen and aggrecan. Although the role of CTGF in articular cartilage biology remains to be elucidated, the results described here demonstrate the potential utility of subtractive hybridization in understanding the process of articular chondrocyte redifferentiation. Anat Rec 263: [91][92][93][94][95][96][97][98] 2001.

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The Exocytic Pathway and Development

Schotman

Rabouille

2009

Trafficking Inside Cells

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Transport of Axl2p Depends on Erv14p, an ER–Vesicle Protein Related to the Drosophila cornichon Gene Product

Cited by 130 publications

References 76 publications

Erv26p Directs Pro-Alkaline Phosphatase into Endoplasmic Reticulum–derived Coat Protein Complex II Transport Vesicles

Erv26p Directs Pro-Alkaline Phosphatase into Endoplasmic Reticulum–derived Coat Protein Complex II Transport Vesicles

Differential expression of multiple genes during articular chondrocyte redifferentiation

The Exocytic Pathway and Development

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