Mutants of vesicular stomatitis virus blocked at different stages in maturation of the viral glycoprotein

Zilberstein, Asher; Snider, Martin D.; Porter, Mary; Lodish, Harvey F.

doi:10.1016/0092-8674(80)90478-x

Cited by 195 publications

(105 citation statements)

References 41 publications

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“…This analysis predicted that the interaction of SEC23 with p150 glued is required to stabilize the COPII prebudding complex. Consistent with this prediction, we observed that inhibiting the SEC23-p150 glued interaction with the antagonistic CT glued or downregulating p150 glued with chemically synthesized small interfering RNAs (siRNAs) prevented the concentration of the secretory cargo ts-O45-G (Zilberstein et al, 1980) at ERES in a microtubule-independent manner. Taken together, our data suggest that cargo concentration at ERES is enhanced by the SEC23-p150 glued interaction, providing a mechanism to coordinate the formation of transport intermediates with their subsequent long-range transport towards the Golgi complex along microtubules.…”

Section: Introductionsupporting

confidence: 68%

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A microtubule-independent role of p150glued in secretory cargo concentration at endoplasmic reticulum exit sites

Verı́ssimo

Halavatyi

Pepperkok

et al. 2015

Journal of Cell Science

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Newly synthesized proteins are sorted into COPII-coated transport carriers at the endoplasmic reticulum (ER). Assembly of the COPII coat complex, which occurs at ER exit sites (ERES), is initiated by membrane association and GTP loading of SAR1, followed by the recruitment of the SEC23-SEC24 and SEC13-SEC31 subcomplexes. Both of these two subcomplexes stimulate GTP hydrolysis and coat disassembly. This inherent disassembly capacity of COPII complexes needs to be regulated to allow sufficient time for cargo sorting and transport carrier formation. By performing fluorescence recovery after photobleaching (FRAP) and mathematical modeling, we show that p150 glued (also known as DCTN1), a component of the dynactin complex, stabilizes the COPII pre-budding complex on ER membranes in a microtubuleindependent manner. Concentration of the secretory marker ts-O45-G at ERES is reduced in the presence of a C-terminal p150 glued fragment that prevents binding of endogenous p150 glued to SEC23. A similar cargo reduction is observed upon p150 glued knockdown. Taken together, our data suggest that cargo concentration at ERES is regulated by p150 glued to coordinate protein sorting and transport carrier formation with the subsequent long-range transport towards the Golgi complex along microtubules.

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Section: Introductionsupporting

confidence: 68%

“…Ts-O45-G is a wellestablished secretory cargo marker (Zilberstein et al, 1980). It accumulates in the ER at 39.5°C and is transported via the Golgi complex to the plasma membrane at the permissive temperature of 32°C.…”

Section: Overexpression Of the C-terminal Fragment Of P150 Glued Affementioning

confidence: 99%

A microtubule-independent role of p150glued in secretory cargo concentration at endoplasmic reticulum exit sites

Verı́ssimo

Halavatyi

Pepperkok

et al. 2015

Journal of Cell Science

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“…In one type of a1-antitrypsin deficiency, an insoluble variant form of antitrypsin aggregates and accumulates in the endoplasmic reticulum (28,29). Some virus mutants blocked in G-protein maturation (30) and an altered HLA-A2 antigen of mutant lymphoblastoid cells (31) fail to reach the cell surface. In contrast to GM 1110, four other Tay-Sachs disease cultures tested in intact cells and in cell-free translation, and a fifth culture tested in intact cells only, failed to synthesize the a chain.…”

Section: Discussionmentioning

confidence: 99%

Synthesis of beta-hexosaminidase in cell-free translation and in intact fibroblasts: an insoluble precursor alpha chain in a rare form of Tay-Sachs disease.

Proia¹,

Neufeld²

1982

Proc. Natl. Acad. Sci. U.S.A.

104

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RNA was isolated from human term placenta or cultured fibroblasts and translated in a rabbit reticulocyte system in the presence of [3S]methionine; the translation products were immunoprecipitated with antisera made against 3-hexosaminidase or its isolated a and ( chains and analyzed by polyacrylamide gel electrophoresis. The largest translated a and (3chain polypeptides had Mrs of 65,000 and 59,000, respectively. These are a2,ooo greater than the Mrs of precursor chains synthesized by intact fibroblasts and deglycosylated with endo-,3-N-acetylglucos- , ( Hexosaminidase is a lysosomal enzyme relevant to several heritable diseases. The A isozyme of f3-hexosaminidase is composed of a and , subunits, which are structurally dissimilar and encoded on different chromosomes; the B isozyme is composed of (3 subunits only. Tay-Sachs disease affects the a subunit and, therefore, the A isozyme; Sandhoffdisease affects the (3(or common) subunit and, therefore, both isozymes A and B. A third disease entity (AB variant) allows the production of normal (3-hexosaminidase but not ofits activator. These diseases are characterized by marked accumulation of GM2 ganglioside, the major natural substrate of ,B-hexosaminidase A, resulting in progressive loss of nervous system function; they are usually fatal in early childhood. Variant forms of later onset and reduced severity are also known. The clinical, genetic, and biochemical aspects ofthesedisordershavebeen reviewed(1).We previously have studied the synthesis and processing of the two chains of (3-hexosaminidase in cultured human skin fibroblasts (2-4). 6360The publication costs ofthis article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U. S. C. §1734 solely to indicate this fact.

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“…Cells were transfected with a vector encoding VSV-G(ts045)-GFP 43 (kindly gifted from Prof Nakayama, Kyoto University) using Lipofectamine 2000 reagent (Invitrogen) and incubated at the non-permissive temperature of 39.5°C for 16 h to allow accumulation of VSV-G(ts045)-GFP in the ER 44 . The cells were then cultured at the permissive temperature of 32°C in the presence of 100 mg ml À 1 cycloheximide to induce transport of the already synthesized VSV-G(ts045)-GFP from the ER to the plasma membrane via the Golgi apparatus.…”

Section: Methodsmentioning

confidence: 99%

Prions disturb post-Golgi trafficking of membrane proteins

et al. 2013

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Mutants of vesicular stomatitis virus blocked at different stages in maturation of the viral glycoprotein

Cited by 195 publications

References 41 publications

A microtubule-independent role of p150glued in secretory cargo concentration at endoplasmic reticulum exit sites

A microtubule-independent role of p150glued in secretory cargo concentration at endoplasmic reticulum exit sites

Synthesis of beta-hexosaminidase in cell-free translation and in intact fibroblasts: an insoluble precursor alpha chain in a rare form of Tay-Sachs disease.

Prions disturb post-Golgi trafficking of membrane proteins

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