Sar1 promotes vesicle budding from the endoplasmic reticulum but not Golgi compartments

Osamu Kuge, Christiane Dascher, Lelio Orci, Tony Rowe, Mylène Amherdt, Helen Plutner, Mariella Ravazzola, Gary Tanigawa, James E. Rothman, William E. Balch

研究成果: ジャーナルへの寄稿記事

243 引用 (Scopus)

抄録

Two new members (Sar1a and Sar1b) of the SAR1 gene family have been identified in mammalian cells. Using immunoelectron microscopy, Sari was found to be restricted to the transitional region where the protein was enriched 20-40-fold in vesicular carriers mediating ER to Golgi traffic. Biochemical analysis revealed that Sari was essential for an early step in vesicle budding. A Sari-specific antibody potently inhibited export of vesicular stomatitis virus glycoprotein (VSV-G) from the ER in vitro. Consistent with the role of guanine nucleotide exchange in Sari function, a trans-dominant mutant (Sarla[T39N]) with a preferential affinity for GDP also strongly inhibited vesicle budding from the ER. In contrast, Sari was not found to be required for the transport of VSV-G between sequential Golgi compartments, suggesting that components active in formation of vesicular carriers mediating ER to Golgi traffic may differ, at least in part, from those involved in intra-Golgi transport. The requirement for novel components at different stages of the secretory pathway may reflect the recently recognized differences in protein transport between the Golgi stacks as opposed to the selective sorting and concentration of protein during export from the ER.

元の言語英語
ページ(範囲)51-65
ページ数15
ジャーナルJournal of Cell Biology
125
発行部数1
出版物ステータス出版済み - 4 1994
外部発表Yes

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Vesicular Stomatitis
Protein Transport
Endoplasmic Reticulum
Glycoproteins
Viruses
Guanine Nucleotides
Immunoelectron Microscopy
Secretory Pathway
Antibodies
Genes
Proteins
In Vitro Techniques

All Science Journal Classification (ASJC) codes

  • Cell Biology

これを引用

Kuge, O., Dascher, C., Orci, L., Rowe, T., Amherdt, M., Plutner, H., ... Balch, W. E. (1994). Sar1 promotes vesicle budding from the endoplasmic reticulum but not Golgi compartments. Journal of Cell Biology, 125(1), 51-65.

Sar1 promotes vesicle budding from the endoplasmic reticulum but not Golgi compartments. / Kuge, Osamu; Dascher, Christiane; Orci, Lelio; Rowe, Tony; Amherdt, Mylène; Plutner, Helen; Ravazzola, Mariella; Tanigawa, Gary; Rothman, James E.; Balch, William E.

:: Journal of Cell Biology, 巻 125, 番号 1, 04.1994, p. 51-65.

研究成果: ジャーナルへの寄稿記事

Kuge, O, Dascher, C, Orci, L, Rowe, T, Amherdt, M, Plutner, H, Ravazzola, M, Tanigawa, G, Rothman, JE & Balch, WE 1994, 'Sar1 promotes vesicle budding from the endoplasmic reticulum but not Golgi compartments', Journal of Cell Biology, 巻. 125, 番号 1, pp. 51-65.
Kuge O, Dascher C, Orci L, Rowe T, Amherdt M, Plutner H その他. Sar1 promotes vesicle budding from the endoplasmic reticulum but not Golgi compartments. Journal of Cell Biology. 1994 4;125(1):51-65.
Kuge, Osamu ; Dascher, Christiane ; Orci, Lelio ; Rowe, Tony ; Amherdt, Mylène ; Plutner, Helen ; Ravazzola, Mariella ; Tanigawa, Gary ; Rothman, James E. ; Balch, William E. / Sar1 promotes vesicle budding from the endoplasmic reticulum but not Golgi compartments. :: Journal of Cell Biology. 1994 ; 巻 125, 番号 1. pp. 51-65.
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abstract = "Two new members (Sar1a and Sar1b) of the SAR1 gene family have been identified in mammalian cells. Using immunoelectron microscopy, Sari was found to be restricted to the transitional region where the protein was enriched 20-40-fold in vesicular carriers mediating ER to Golgi traffic. Biochemical analysis revealed that Sari was essential for an early step in vesicle budding. A Sari-specific antibody potently inhibited export of vesicular stomatitis virus glycoprotein (VSV-G) from the ER in vitro. Consistent with the role of guanine nucleotide exchange in Sari function, a trans-dominant mutant (Sarla[T39N]) with a preferential affinity for GDP also strongly inhibited vesicle budding from the ER. In contrast, Sari was not found to be required for the transport of VSV-G between sequential Golgi compartments, suggesting that components active in formation of vesicular carriers mediating ER to Golgi traffic may differ, at least in part, from those involved in intra-Golgi transport. The requirement for novel components at different stages of the secretory pathway may reflect the recently recognized differences in protein transport between the Golgi stacks as opposed to the selective sorting and concentration of protein during export from the ER.",
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