Early steps in autophagy depend on direct phosphorylation of Atg9 by the Atg1 kinase

to connected objects

Abstract: Bulk degradation of cytoplasmic material is mediated by a highly conserved intracellular trafficking pathway termed autophagy. This pathway is characterized by the formation of double-membrane vesicles termed autophagosomes engulfing the substrate and transporting it to the vacuole/lysosome for breakdown and recycling. The Atg1/ULK1 kinase is essential for this process; however, little is known about its targets and the means by which it controls autophagy. Here we have screened for Atg1 kinase substrates using consensus peptide arrays and identified three components of the autophagy machinery. The multimembrane-spanning protein Atg9 is a direct target of this kinase essential for autophagy. Phosphorylated Atg9 is then required for the efficient recruitment of Atg8 and Atg18 to the site of autophagosome formation and subsequent expansion of the isolation membrane, a prerequisite for a functioning autophagy pathway. These findings show that the Atg1 kinase acts early in autophagy by regulating the outgrowth of autophagosomal membranes

Location: Deutsche Nationalbibliothek Frankfurt am Main

Extent: Online-Ressource

Language: Englisch

Notes: ISSN: 1097-2765

Classification: Biowissenschaften, Biologie

Event: Veröffentlichung

(where): Freiburg

(who): Universität

(when): 2024

Creator: Papinski, Daniel
Schuschnig, Martina
Reiter, Wolfgang
Wilhelm, Larissa
Barnes, Christopher A
Maiolica, Alessio
Hansmann, Isabella
Pfaffenwimmer, Thaddäus
Kijanska, Monika
Stoffel, Ingrid
Lee, Sung Sik
Brezovich, Andrea
Lou, Jane Hua
Turk, Benjamin E.
Aebersold, Rudolf
Ammerer, Gustav
Peter, Matthias
Kraft, Claudine

DOI: 10.1016/j.molcel.2013.12.011

URN: urn:nbn:de:bsz:25-freidok-2441408

Rights: Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.

Last update: 25.03.2025, 1:54 PM CET

Data provider

This object is provided by:
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.

Show original at data provider

Associated

Papinski, Daniel
Schuschnig, Martina
Reiter, Wolfgang
Wilhelm, Larissa
Barnes, Christopher A
Maiolica, Alessio
Hansmann, Isabella
Pfaffenwimmer, Thaddäus
Kijanska, Monika
Stoffel, Ingrid
Lee, Sung Sik
Brezovich, Andrea
Lou, Jane Hua
Turk, Benjamin E.
Aebersold, Rudolf
Ammerer, Gustav
Peter, Matthias
Kraft, Claudine
Universität

Time of origin

2024

Other Objects (12)

FIP200 phosphorylation regulates late steps in mitophagy

Beclin 1 phosphorylation – at the center of autophagy regulation

Hochschulschrift

Autophagy regulation by the p38 MAP kinase

ULK1-mediated phosphorylation regulates the conserved role of YKT6 in autophagy

Hochschulschrift

Phosphorylation-dependent regulation of ubiquitin-binding protein optineurin in selective autophagy

Phosphorylation of Beclin 1 by BCR-ABL suppresses autophagy in CML

Hochschulschrift

Molecular mechanism of Atg1 kinase and autophagy activation

Phosphorylation of the mitochondrial autophagy receptor Nix enhances its interaction with LC3 proteins

Phosphorylation of BECLIN-1 by BCR-ABL suppresses autophagy in chronic myeloid leukemia

Hochschulschrift

Regulation of Mammalian Autophagy by Unc-51-Like Kinase 1

Hochschulschrift

Regulation of mammalian autophagy by Unc-51-like kinase 1

Hochschulschrift

Deciphering Human Cytoplasmic Protein Tyrosine Kinase Phosphorylation Specificity In Yeast

FIP200 phosphorylation regulates late steps in mitophagy

Beclin 1 phosphorylation – at the center of autophagy regulation

Hochschulschrift

Autophagy regulation by the p38 MAP kinase

ULK1-mediated phosphorylation regulates the conserved role of YKT6 in autophagy

Hochschulschrift

Phosphorylation-dependent regulation of ubiquitin-binding protein optineurin in selective autophagy

Phosphorylation of Beclin 1 by BCR-ABL suppresses autophagy in CML

Hochschulschrift

Molecular mechanism of Atg1 kinase and autophagy activation

Phosphorylation of the mitochondrial autophagy receptor Nix enhances its interaction with LC3 proteins

Phosphorylation of BECLIN-1 by BCR-ABL suppresses autophagy in chronic myeloid leukemia

Hochschulschrift

Regulation of Mammalian Autophagy by Unc-51-Like Kinase 1

Hochschulschrift

Regulation of mammalian autophagy by Unc-51-like kinase 1

Hochschulschrift

Deciphering Human Cytoplasmic Protein Tyrosine Kinase Phosphorylation Specificity In Yeast

FIP200 phosphorylation regulates late steps in mitophagy

Beclin 1 phosphorylation – at the center of autophagy regulation

Hochschulschrift

Autophagy regulation by the p38 MAP kinase

ULK1-mediated phosphorylation regulates the conserved role of YKT6 in autophagy

Hochschulschrift

Phosphorylation-dependent regulation of ubiquitin-binding protein optineurin in selective autophagy

Phosphorylation of Beclin 1 by BCR-ABL suppresses autophagy in CML

Hochschulschrift

Molecular mechanism of Atg1 kinase and autophagy activation

Phosphorylation of the mitochondrial autophagy receptor Nix enhances its interaction with LC3 proteins

Phosphorylation of BECLIN-1 by BCR-ABL suppresses autophagy in chronic myeloid leukemia

Hochschulschrift

Regulation of Mammalian Autophagy by Unc-51-Like Kinase 1

Hochschulschrift

Regulation of mammalian autophagy by Unc-51-like kinase 1

Hochschulschrift

Deciphering Human Cytoplasmic Protein Tyrosine Kinase Phosphorylation Specificity In Yeast

Cultural heritage institutions wishing to register will find more information here.

Fields marked * need to be filled in.

Username*

Please enter your username

Email*

Please enter your email address

Please do not fill this field

First name

Last name

Password*

Please enter your password

Confirm password*

Please enter the same password

I have read the terms of use and the privacy policy for the collection of personal data and accept them. *

This field is required.

I would like to subscribe to the newsletter of the Deutsche Digitale Bibliothek. See newsletter subscription info.

Account created

Your "My DDB" account has been successfully created. Before you can log in to your account, you must click the confirmation link in the message we just sent to the email address you provided.

Early steps in autophagy depend on direct phosphorylation of Atg9 by the Atg1 kinase

Object Details

Classification and Topics

Contributors, Places and Time

Further information

Data provider

Associated

Time of origin

Other Objects (12)

FIP200 phosphorylation regulates late steps in mitophagy

Beclin 1 phosphorylation – at the center of autophagy regulation

Autophagy regulation by the p38 MAP kinase

ULK1-mediated phosphorylation regulates the conserved role of YKT6 in autophagy

Phosphorylation-dependent regulation of ubiquitin-binding protein optineurin in selective autophagy

Phosphorylation of Beclin 1 by BCR-ABL suppresses autophagy in CML

Molecular mechanism of Atg1 kinase and autophagy activation

Phosphorylation of the mitochondrial autophagy receptor Nix enhances its interaction with LC3 proteins

Phosphorylation of BECLIN-1 by BCR-ABL suppresses autophagy in chronic myeloid leukemia

Regulation of Mammalian Autophagy by Unc-51-Like Kinase 1

Regulation of mammalian autophagy by Unc-51-like kinase 1

Deciphering Human Cytoplasmic Protein Tyrosine Kinase Phosphorylation Specificity In Yeast

FIP200 phosphorylation regulates late steps in mitophagy

Beclin 1 phosphorylation – at the center of autophagy regulation

Autophagy regulation by the p38 MAP kinase

ULK1-mediated phosphorylation regulates the conserved role of YKT6 in autophagy

Phosphorylation-dependent regulation of ubiquitin-binding protein optineurin in selective autophagy

Phosphorylation of Beclin 1 by BCR-ABL suppresses autophagy in CML

Molecular mechanism of Atg1 kinase and autophagy activation

Phosphorylation of the mitochondrial autophagy receptor Nix enhances its interaction with LC3 proteins

Phosphorylation of BECLIN-1 by BCR-ABL suppresses autophagy in chronic myeloid leukemia

Regulation of Mammalian Autophagy by Unc-51-Like Kinase 1

Regulation of mammalian autophagy by Unc-51-like kinase 1

Deciphering Human Cytoplasmic Protein Tyrosine Kinase Phosphorylation Specificity In Yeast

FIP200 phosphorylation regulates late steps in mitophagy

Beclin 1 phosphorylation – at the center of autophagy regulation

Autophagy regulation by the p38 MAP kinase

ULK1-mediated phosphorylation regulates the conserved role of YKT6 in autophagy

Phosphorylation-dependent regulation of ubiquitin-binding protein optineurin in selective autophagy

Phosphorylation of Beclin 1 by BCR-ABL suppresses autophagy in CML

Molecular mechanism of Atg1 kinase and autophagy activation

Phosphorylation of the mitochondrial autophagy receptor Nix enhances its interaction with LC3 proteins

Phosphorylation of BECLIN-1 by BCR-ABL suppresses autophagy in chronic myeloid leukemia

Regulation of Mammalian Autophagy by Unc-51-Like Kinase 1

Regulation of mammalian autophagy by Unc-51-like kinase 1

Deciphering Human Cytoplasmic Protein Tyrosine Kinase Phosphorylation Specificity In Yeast

Related objects

Reset password