Publication

Atg4 proteolytic activity can be inhibited by Atg1 phosphorylation

Sánchez-Wandelmer, J., Kriegenburg, F., Rohringer, S., Schuschnig, M., Gómez-Sánchez, R., Zens, B., Abreu, S., Hardenberg, R., Hollenstein, D., Gao, J., Ungermann, C., Martens, S., Kraft, C. & Reggiori, F., 18-Aug-2017, In : Nature Communications. 8, 10 p., 295.

Research output: Contribution to journalArticleAcademicpeer-review

APA

Sánchez-Wandelmer, J., Kriegenburg, F., Rohringer, S., Schuschnig, M., Gómez-Sánchez, R., Zens, B., ... Reggiori, F. (2017). Atg4 proteolytic activity can be inhibited by Atg1 phosphorylation. Nature Communications, 8, [295]. https://doi.org/10.1038/s41467-017-00302-3

Author

Sánchez-Wandelmer, Jana ; Kriegenburg, Franziska ; Rohringer, Sabrina ; Schuschnig, Martina ; Gómez-Sánchez, Rubén ; Zens, Bettina ; Abreu, Susana ; Hardenberg, Ralph ; Hollenstein, David ; Gao, Jieqiong ; Ungermann, Christian ; Martens, Sascha ; Kraft, Claudine ; Reggiori, Fulvio. / Atg4 proteolytic activity can be inhibited by Atg1 phosphorylation. In: Nature Communications. 2017 ; Vol. 8.

Harvard

Sánchez-Wandelmer, J, Kriegenburg, F, Rohringer, S, Schuschnig, M, Gómez-Sánchez, R, Zens, B, Abreu, S, Hardenberg, R, Hollenstein, D, Gao, J, Ungermann, C, Martens, S, Kraft, C & Reggiori, F 2017, 'Atg4 proteolytic activity can be inhibited by Atg1 phosphorylation' Nature Communications, vol. 8, 295. https://doi.org/10.1038/s41467-017-00302-3

Standard

Atg4 proteolytic activity can be inhibited by Atg1 phosphorylation. / Sánchez-Wandelmer, Jana; Kriegenburg, Franziska; Rohringer, Sabrina; Schuschnig, Martina; Gómez-Sánchez, Rubén; Zens, Bettina; Abreu, Susana; Hardenberg, Ralph; Hollenstein, David; Gao, Jieqiong; Ungermann, Christian; Martens, Sascha; Kraft, Claudine; Reggiori, Fulvio.

In: Nature Communications, Vol. 8, 295, 18.08.2017.

Research output: Contribution to journalArticleAcademicpeer-review

Vancouver

Sánchez-Wandelmer J, Kriegenburg F, Rohringer S, Schuschnig M, Gómez-Sánchez R, Zens B et al. Atg4 proteolytic activity can be inhibited by Atg1 phosphorylation. Nature Communications. 2017 Aug 18;8. 295. https://doi.org/10.1038/s41467-017-00302-3


BibTeX

@article{557b6226699d4d648130097712ca7f9c,
title = "Atg4 proteolytic activity can be inhibited by Atg1 phosphorylation",
abstract = "The biogenesis of autophagosomes depends on the conjugation of Atg8-like proteins with phosphatidylethanolamine. Atg8 processing by the cysteine protease Atg4 is required for its covalent linkage to phosphatidylethanolamine, but it is also necessary for Atg8 deconjugation from this lipid to release it from membranes. How these two cleavage steps are coordinated is unknown. Here we show that phosphorylation by Atg1 inhibits Atg4 function, an event that appears to exclusively occur at the site of autophagosome biogenesis. These results are consistent with a model where the Atg8-phosphatidylethanolamine pool essential for autophagosome formation is protected at least in part by Atg4 phosphorylation by Atg1 while newly synthesized cytoplasmic Atg8 remains susceptible to constitutive Atg4 processing.",
keywords = "VACUOLE TARGETING PATHWAY, YEAST SACCHAROMYCES-CEREVISIAE, AUTOPHAGOSOME BIOGENESIS, CAENORHABDITIS-ELEGANS, ATG8-PE DECONJUGATION, SELECTIVE AUTOPHAGY, MEMBRANE-BINDING, EARLY STEPS, MECHANISM, COMPLEX",
author = "Jana S{\'a}nchez-Wandelmer and Franziska Kriegenburg and Sabrina Rohringer and Martina Schuschnig and Rub{\'e}n G{\'o}mez-S{\'a}nchez and Bettina Zens and Susana Abreu and Ralph Hardenberg and David Hollenstein and Jieqiong Gao and Christian Ungermann and Sascha Martens and Claudine Kraft and Fulvio Reggiori",
year = "2017",
month = "8",
day = "18",
doi = "10.1038/s41467-017-00302-3",
language = "English",
volume = "8",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "Nature Publishing Group",

}

RIS

TY - JOUR

T1 - Atg4 proteolytic activity can be inhibited by Atg1 phosphorylation

AU - Sánchez-Wandelmer, Jana

AU - Kriegenburg, Franziska

AU - Rohringer, Sabrina

AU - Schuschnig, Martina

AU - Gómez-Sánchez, Rubén

AU - Zens, Bettina

AU - Abreu, Susana

AU - Hardenberg, Ralph

AU - Hollenstein, David

AU - Gao, Jieqiong

AU - Ungermann, Christian

AU - Martens, Sascha

AU - Kraft, Claudine

AU - Reggiori, Fulvio

PY - 2017/8/18

Y1 - 2017/8/18

N2 - The biogenesis of autophagosomes depends on the conjugation of Atg8-like proteins with phosphatidylethanolamine. Atg8 processing by the cysteine protease Atg4 is required for its covalent linkage to phosphatidylethanolamine, but it is also necessary for Atg8 deconjugation from this lipid to release it from membranes. How these two cleavage steps are coordinated is unknown. Here we show that phosphorylation by Atg1 inhibits Atg4 function, an event that appears to exclusively occur at the site of autophagosome biogenesis. These results are consistent with a model where the Atg8-phosphatidylethanolamine pool essential for autophagosome formation is protected at least in part by Atg4 phosphorylation by Atg1 while newly synthesized cytoplasmic Atg8 remains susceptible to constitutive Atg4 processing.

AB - The biogenesis of autophagosomes depends on the conjugation of Atg8-like proteins with phosphatidylethanolamine. Atg8 processing by the cysteine protease Atg4 is required for its covalent linkage to phosphatidylethanolamine, but it is also necessary for Atg8 deconjugation from this lipid to release it from membranes. How these two cleavage steps are coordinated is unknown. Here we show that phosphorylation by Atg1 inhibits Atg4 function, an event that appears to exclusively occur at the site of autophagosome biogenesis. These results are consistent with a model where the Atg8-phosphatidylethanolamine pool essential for autophagosome formation is protected at least in part by Atg4 phosphorylation by Atg1 while newly synthesized cytoplasmic Atg8 remains susceptible to constitutive Atg4 processing.

KW - VACUOLE TARGETING PATHWAY

KW - YEAST SACCHAROMYCES-CEREVISIAE

KW - AUTOPHAGOSOME BIOGENESIS

KW - CAENORHABDITIS-ELEGANS

KW - ATG8-PE DECONJUGATION

KW - SELECTIVE AUTOPHAGY

KW - MEMBRANE-BINDING

KW - EARLY STEPS

KW - MECHANISM

KW - COMPLEX

U2 - 10.1038/s41467-017-00302-3

DO - 10.1038/s41467-017-00302-3

M3 - Article

VL - 8

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

M1 - 295

ER -

ID: 46939954