The ADP-ribosylation factor GTPase-activating protein Glo3p is involved in ER retrieval

Dagmar Dogic; Benoit De Chassey; Elah Pick; Dan Cassel; Yaya Lefkir; Silke Hennecke; Pierre Cosson; François Letourneur

doi:10.1016/S0171-9335(99)80064-8

The ADP-ribosylation factor GTPase-activating protein Glo3p is involved in ER retrieval

Dagmar Dogic, Benoit De Chassey, Elah Pick, Dan Cassel, Yaya Lefkir, Silke Hennecke, Pierre Cosson, François Letourneur

Research output: Contribution to journal › Article › peer-review

Abstract

Retrograde transport of proteins from the Golgi to the endoplasmic reticulum (ER) has been the subject of some interest in the recent past. Here a new thermosensitive yeast mutant defective in retrieval of dilysine-tagged proteins from the Golgi back to the endoplasmic reticulum was characterized. The ret4-1 mutant also exhibited a selective defect in forward ER-to-Golgi transport of some secreted proteins at the non-permissive temperature. The corresponding RET4 gene was found to encode Glo3p, a GTPase-activating protein (GAP) specific for ADP-ribosylation factor (ARF). In vitro, the Glo3 thermosensitive mutant showed a reduced ARF1-GAP activity. The Glo3 protein belongs to a family of zinc finger proteins that may include additional ARF-GAPs. Gene deletion experiments of other family members showed that only GLO3 deletion resulted in impaired retrieval of dilysine-tagged proteins back to the ER. These results demonstrate that Glo3p is the main ARF-GAP specifically involved in ER retrieval.

Original language	English
Pages (from-to)	305-310
Number of pages	6
Journal	European Journal of Cell Biology
Volume	78
Issue number	5
DOIs	https://doi.org/10.1016/S0171-9335(99)80064-8
State	Published - 1999
Externally published	Yes

Bibliographical note

Funding Information:
Acknowledgments_ We thank Alain Bosch and Christian Van Herrewege for art works, Monika Bajorek for technical help and Dr. Ian Parsons for critical reading of the manuscript. D. Cassel is supported by the Israel Science Foundation and the Fund for the Promotion of Research at the Technion. P. Cosson is financed by a Start fellowship of the Fonds National Suisse de la Recherche Scientifique. The laboratory of F. Letourneur is funded by the French Centre National pour la Recherche Scientifique (ATIPE), the Association pour la Recherche contre Ie Cancer and the Fondation pour la Recherche Medicale. The Basel Institute for Immunology was founded and is financed by F. Hoffman-LaRoche and Company, Limited, CH4002 Basel, Switzerland.

Keywords

ARF
COPI
Endoplasmic reticulum
GAP
Golgi

ASJC Scopus subject areas

Pathology and Forensic Medicine
Histology
Cell Biology

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10.1016/S0171-9335(99)80064-8

Cite this

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title = "The ADP-ribosylation factor GTPase-activating protein Glo3p is involved in ER retrieval",

abstract = "Retrograde transport of proteins from the Golgi to the endoplasmic reticulum (ER) has been the subject of some interest in the recent past. Here a new thermosensitive yeast mutant defective in retrieval of dilysine-tagged proteins from the Golgi back to the endoplasmic reticulum was characterized. The ret4-1 mutant also exhibited a selective defect in forward ER-to-Golgi transport of some secreted proteins at the non-permissive temperature. The corresponding RET4 gene was found to encode Glo3p, a GTPase-activating protein (GAP) specific for ADP-ribosylation factor (ARF). In vitro, the Glo3 thermosensitive mutant showed a reduced ARF1-GAP activity. The Glo3 protein belongs to a family of zinc finger proteins that may include additional ARF-GAPs. Gene deletion experiments of other family members showed that only GLO3 deletion resulted in impaired retrieval of dilysine-tagged proteins back to the ER. These results demonstrate that Glo3p is the main ARF-GAP specifically involved in ER retrieval.",

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author = "Dagmar Dogic and {De Chassey}, Benoit and Elah Pick and Dan Cassel and Yaya Lefkir and Silke Hennecke and Pierre Cosson and Fran{\c c}ois Letourneur",

note = "Funding Information: Acknowledgments_ We thank Alain Bosch and Christian Van Herrewege for art works, Monika Bajorek for technical help and Dr. Ian Parsons for critical reading of the manuscript. D. Cassel is supported by the Israel Science Foundation and the Fund for the Promotion of Research at the Technion. P. Cosson is financed by a Start fellowship of the Fonds National Suisse de la Recherche Scientifique. The laboratory of F. Letourneur is funded by the French Centre National pour la Recherche Scientifique (ATIPE), the Association pour la Recherche contre Ie Cancer and the Fondation pour la Recherche Medicale. The Basel Institute for Immunology was founded and is financed by F. Hoffman-LaRoche and Company, Limited, CH4002 Basel, Switzerland.",

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AU - Dogic, Dagmar

AU - De Chassey, Benoit

AU - Pick, Elah

AU - Cassel, Dan

AU - Lefkir, Yaya

AU - Hennecke, Silke

AU - Cosson, Pierre

AU - Letourneur, François

N1 - Funding Information: Acknowledgments_ We thank Alain Bosch and Christian Van Herrewege for art works, Monika Bajorek for technical help and Dr. Ian Parsons for critical reading of the manuscript. D. Cassel is supported by the Israel Science Foundation and the Fund for the Promotion of Research at the Technion. P. Cosson is financed by a Start fellowship of the Fonds National Suisse de la Recherche Scientifique. The laboratory of F. Letourneur is funded by the French Centre National pour la Recherche Scientifique (ATIPE), the Association pour la Recherche contre Ie Cancer and the Fondation pour la Recherche Medicale. The Basel Institute for Immunology was founded and is financed by F. Hoffman-LaRoche and Company, Limited, CH4002 Basel, Switzerland.

PY - 1999

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N2 - Retrograde transport of proteins from the Golgi to the endoplasmic reticulum (ER) has been the subject of some interest in the recent past. Here a new thermosensitive yeast mutant defective in retrieval of dilysine-tagged proteins from the Golgi back to the endoplasmic reticulum was characterized. The ret4-1 mutant also exhibited a selective defect in forward ER-to-Golgi transport of some secreted proteins at the non-permissive temperature. The corresponding RET4 gene was found to encode Glo3p, a GTPase-activating protein (GAP) specific for ADP-ribosylation factor (ARF). In vitro, the Glo3 thermosensitive mutant showed a reduced ARF1-GAP activity. The Glo3 protein belongs to a family of zinc finger proteins that may include additional ARF-GAPs. Gene deletion experiments of other family members showed that only GLO3 deletion resulted in impaired retrieval of dilysine-tagged proteins back to the ER. These results demonstrate that Glo3p is the main ARF-GAP specifically involved in ER retrieval.

AB - Retrograde transport of proteins from the Golgi to the endoplasmic reticulum (ER) has been the subject of some interest in the recent past. Here a new thermosensitive yeast mutant defective in retrieval of dilysine-tagged proteins from the Golgi back to the endoplasmic reticulum was characterized. The ret4-1 mutant also exhibited a selective defect in forward ER-to-Golgi transport of some secreted proteins at the non-permissive temperature. The corresponding RET4 gene was found to encode Glo3p, a GTPase-activating protein (GAP) specific for ADP-ribosylation factor (ARF). In vitro, the Glo3 thermosensitive mutant showed a reduced ARF1-GAP activity. The Glo3 protein belongs to a family of zinc finger proteins that may include additional ARF-GAPs. Gene deletion experiments of other family members showed that only GLO3 deletion resulted in impaired retrieval of dilysine-tagged proteins back to the ER. These results demonstrate that Glo3p is the main ARF-GAP specifically involved in ER retrieval.

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ER -

The ADP-ribosylation factor GTPase-activating protein Glo3p is involved in ER retrieval

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

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