The p24 proteins are not essential for vesicular transport in Saccharomyces cerevisiae

Sebastian Springer; Eric Chen; Rainer Duden; Martina Marzioch; Adele Rowley; Susan Hamamoto; Sabeeha Merchant; Randy Schekman

doi:10.1073/pnas.070044097

The p24 proteins are not essential for vesicular transport in Saccharomyces cerevisiae

Sebastian Springer, Eric Chen, Rainer Duden, Martina Marzioch, Adele Rowley, Susan Hamamoto, Sabeeha Merchant, Randy Schekman^*

^*Corresponding author for this work

Institute of Biology

101 Citations (Scopus)

Abstract

To investigate the factors involved in the sorting of cargo proteins into COPII endoplasmic reticulum (ER) to Golgi apparatus transport vesicles, we have created a strain of S. cerevisiae (p24Δ8) that lacks all eight members of the p24 family of transmembrane proteins (Emp24p, Erv25p, and Erp1p to Erp6p). The p24 proteins have been implicated in COPI and COPII vesicle formation, cargo protein sorting, and regulation of vesicular transport in eukaryotic cells. We find that p24Δ8 cells grow identically to wild type and show delays of invertase and Gas1p ER-to-Golgi transport identical to those seen in a single Δemp24 deletion strain. Thus, p24 proteins do not have an essential function in the secretory pathway. Instead, they may serve as quality control factors to restrict the entry of proteins into COPII vesicles.

Original language	English
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	97
Issue number	8
Pages (from-to)	4034-4039
Number of pages	6
ISSN	0027-8424
DOIs	https://doi.org/10.1073/pnas.070044097
Publication status	Published - 11.04.2000

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Academic Focus: Center for Infection and Inflammation Research (ZIEL)

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10.1073/pnas.070044097

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title = "The p24 proteins are not essential for vesicular transport in Saccharomyces cerevisiae",

abstract = "To investigate the factors involved in the sorting of cargo proteins into COPII endoplasmic reticulum (ER) to Golgi apparatus transport vesicles, we have created a strain of S. cerevisiae (p24Δ8) that lacks all eight members of the p24 family of transmembrane proteins (Emp24p, Erv25p, and Erp1p to Erp6p). The p24 proteins have been implicated in COPI and COPII vesicle formation, cargo protein sorting, and regulation of vesicular transport in eukaryotic cells. We find that p24Δ8 cells grow identically to wild type and show delays of invertase and Gas1p ER-to-Golgi transport identical to those seen in a single Δemp24 deletion strain. Thus, p24 proteins do not have an essential function in the secretory pathway. Instead, they may serve as quality control factors to restrict the entry of proteins into COPII vesicles.",

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T1 - The p24 proteins are not essential for vesicular transport in Saccharomyces cerevisiae

AU - Springer, Sebastian

AU - Chen, Eric

AU - Duden, Rainer

AU - Marzioch, Martina

AU - Rowley, Adele

AU - Hamamoto, Susan

AU - Merchant, Sabeeha

AU - Schekman, Randy

PY - 2000/4/11

Y1 - 2000/4/11

N2 - To investigate the factors involved in the sorting of cargo proteins into COPII endoplasmic reticulum (ER) to Golgi apparatus transport vesicles, we have created a strain of S. cerevisiae (p24Δ8) that lacks all eight members of the p24 family of transmembrane proteins (Emp24p, Erv25p, and Erp1p to Erp6p). The p24 proteins have been implicated in COPI and COPII vesicle formation, cargo protein sorting, and regulation of vesicular transport in eukaryotic cells. We find that p24Δ8 cells grow identically to wild type and show delays of invertase and Gas1p ER-to-Golgi transport identical to those seen in a single Δemp24 deletion strain. Thus, p24 proteins do not have an essential function in the secretory pathway. Instead, they may serve as quality control factors to restrict the entry of proteins into COPII vesicles.

AB - To investigate the factors involved in the sorting of cargo proteins into COPII endoplasmic reticulum (ER) to Golgi apparatus transport vesicles, we have created a strain of S. cerevisiae (p24Δ8) that lacks all eight members of the p24 family of transmembrane proteins (Emp24p, Erv25p, and Erp1p to Erp6p). The p24 proteins have been implicated in COPI and COPII vesicle formation, cargo protein sorting, and regulation of vesicular transport in eukaryotic cells. We find that p24Δ8 cells grow identically to wild type and show delays of invertase and Gas1p ER-to-Golgi transport identical to those seen in a single Δemp24 deletion strain. Thus, p24 proteins do not have an essential function in the secretory pathway. Instead, they may serve as quality control factors to restrict the entry of proteins into COPII vesicles.

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JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

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The p24 proteins are not essential for vesicular transport in Saccharomyces cerevisiae

Abstract

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