Okadaic Acid Induces Selective Arrest of Protein Transport in the Rough Endoplasmic Reticulum and Prevents Export into COPII-Coated Structures

Pryde, James G.; Farmaki, Theodora; Lucocq, John M.

doi:10.1128/mcb.18.2.1125

Cited by 16 publications

(16 citation statements)

References 66 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Treatment of cells with OKA reduced by Ͼ95% the number of budding structures on the ER (12 Ϯ 5 buds per cells). This result is similar to the recently reported morphological effects of OKA on export of the pre-Golgi intermediate marker protein p53/58 from the ER (38). Calphostin C led to an 85% reduction (40 Ϯ 10 buds per cell, respectively), whereas phorbol 12-myristate 13-acetate treatment resulted in a 2-fold increase in their number (480 Ϯ 11).…”

Section: Resultssupporting

confidence: 90%

Cargo Can Modulate COPII Vesicle Formation from the Endoplasmic Reticulum

Aridor¹,

Bannykh²,

Rowe³

et al. 1999

Journal of Biological Chemistry

View full text Add to dashboard Cite

The COPII coat complex found on endoplasmic reticulum (ER)-derived vesicles plays a critical role in cargo selection. We now address the potential role of biosynthetic cargo in modulating COPII coat assembly and vesicle budding. The ER accumulation of vesicular stomatitis glycoprotein (VSV-G), a transmembrane protein, or the soluble PiZ variant of ␣1-antitrypsin, reduced levels of general COPII vesicle formation in vivo. Consistent with this result, conditions that prevent the export of VSV-G from the ER led to a significant inhibition of general COPII vesicle budding from ER microsomes and the export of an endogenous recycling protein p58 in vitro. In contrast, synchronized export of VSV-G stimulated COPII vesicle budding both in vivo and in vitro. Under conditions where VSV-G is retained in the ER, we find that it can to be recovered in pre-budding complexes containing COPII components. These results suggest that the export of biosynthetic cargo is integrated with ER functions involved in protein folding and oligomerization. The ability of biosynthetic cargo to prevent or enhance ER export suggests that interactions of cargo with the COPII machinery contribute to the formation of vesicles budding from the ER.

show abstract

Section: Resultssupporting

confidence: 90%

Cargo Can Modulate COPII Vesicle Formation from the Endoplasmic Reticulum

Aridor¹,

Bannykh²,

Rowe³

et al. 1999

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…Specifically, changes in Golgi morphology were observed in cells overexpressing ADP-ribosylation factor , injected with rab1a mutant (Wilson et al, 1994), or anti-␤-COP antibodies (Pepperkok et al, 1993). Similarly, treatment of cells with BFA (Misumi et al, 1986;Fujiwara et al, 1988;Lippincott-Schwartz et al, 1989), nocodazole (Storrie and Yang, 1998), or okadaic acid (Pryde et al, 1998) has a dramatic effect on Golgi integrity. The exact mechanism of the disruptive action of anti-p115 antibodies on Golgi structure is currently unknown, but it is possible that the antibodies perturb transport pathways between the ER and the Golgi.…”

Section: Requirement For P115 In Maintaining Golgi Structurementioning

confidence: 97%

ER to Golgi Transport

Álvarez

Fujita

Hubbard

et al. 1999

The Journal of Cell Biology

116

View full text Add to dashboard Cite

The membrane transport factor p115 functions in the secretory pathway of mammalian cells. Using biochemical and morphological approaches, we show that p115 participates in the assembly and maintenance of normal Golgi structure and is required for ER to Golgi traffic at a pre-Golgi stage. Injection of antibodies against p115 into intact WIF-B cells caused Golgi disruption and inhibited Golgi complex reassembly after BFA treatment and wash-out. Addition of anti–p115 antibodies or depletion of p115 from a VSVtsO45 based semi-intact cell transport assay inhibited transport. The inhibition occurred after VSV glycoprotein (VSV-G) exit from the ER but before its delivery to the Golgi complex, and resulted in VSV-G protein accumulating in peripheral vesicular tubular clusters (VTCs). The p115-requiring step of transport followed the rab1-requiring step and preceded the Ca2+-requiring step. Unexpectedly, mannosidase I redistributed from the Golgi complex to colocalize with VSV-G protein arrested in pre-Golgi VTCs by p115 depletion. Redistribution of mannosidase I was also observed in cells incubated at 15°C. Our data show that p115 is essential for the translocation of pre-Golgi VTCs from peripheral sites to the Golgi stack. This defines a previously uncharacterized function for p115 at the VTC stage of ER to Golgi traffic.

show abstract

“…Moreover, recent evidence indicates that Golgi-resident enzymes slowly recycle through the ER (Cole et al, 1998;Storrie et al, 1998;Girod et al, 1999). To investigate whether O-glyc b(5) must leave the ER to become glycosylated, we treated cells with the phosphatase inhibitor OKA, a drug which blocks exit from the ER (Davidson et al, 1992;Pryde et al, 1998). Transfected cells were exposed to [ 3 H]GlcNH 2 for 3 h and then incubated further for another hour in the presence or absence of OKA.…”

Section: Glycosylation Of O-glyc B(5)mentioning

confidence: 99%

Mechanism of Residence of Cytochrome B(5), a Tail-Anchored Protein, in the Endoplasmic Reticulum

Pedrazzini

Villa

Longhi³

et al. 2000

The Journal of Cell Biology

View full text Add to dashboard Cite

Endoplasmic reticulum (ER) proteins maintain their residency by static retention, dynamic retrieval, or a combination of the two. Tail-anchored proteins that contain a cytosolic domain associated with the lipid bilayer via a hydrophobic stretch close to the COOH terminus are sorted within the secretory pathway by largely unknown mechanisms. Here, we have investigated the mode of insertion in the bilayer and the intracellular trafficking of cytochrome b(5) (b[5]), taken as a model for ER-resident tail-anchored proteins. We first demonstrated that b(5) can acquire a transmembrane topology posttranslationally, and then used two tagged versions of b(5), N-glyc and O-glyc b(5), containing potential N- and O-glycosylation sites, respectively, at the COOH-terminal lumenal extremity, to discriminate between retention and retrieval mechanisms. Whereas the N-linked oligosaccharide provided no evidence for retrieval from a downstream compartment, a more stringent assay based on carbohydrate acquisition by O-glyc b(5) showed that b(5) gains access to enzymes catalyzing the first steps of O-glycosylation. These results suggest that b(5) slowly recycles between the ER and the cis-Golgi complex and that dynamic retrieval as well as retention are involved in sorting of tail-anchored proteins.

show abstract

Okadaic Acid Induces Selective Arrest of Protein Transport in the Rough Endoplasmic Reticulum and Prevents Export into COPII-Coated Structures

Cited by 16 publications

References 66 publications

Cargo Can Modulate COPII Vesicle Formation from the Endoplasmic Reticulum

Cargo Can Modulate COPII Vesicle Formation from the Endoplasmic Reticulum

ER to Golgi Transport

Mechanism of Residence of Cytochrome B(5), a Tail-Anchored Protein, in the Endoplasmic Reticulum

Contact Info

Product

Resources

About