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Autophagy Volume 15, 2019 - Issue 8
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Autophagic Punctum

How RB1CC1/FIP200 claws its way to autophagic engulfment of SQSTM1/p62-ubiquitin condensates

Eleonora Turcoa Department of Biochemistry and Cell Biology, Max F. Perutz Laboratories (MFPL), University of Vienna, Vienna BioCenter, Vienna, Austria
,
Marie Wittb Crystallography, Max-Delbrück-Center for Molecular Medicine, Berlin, Germany;c Institute of Chemistry and Biochemistry, Freie Universität Berlin, Berlin, Germany
,
Christine Aberta Department of Biochemistry and Cell Biology, Max F. Perutz Laboratories (MFPL), University of Vienna, Vienna BioCenter, Vienna, Austria
,
Tobias Bock-Bierbaumb Crystallography, Max-Delbrück-Center for Molecular Medicine, Berlin, Germany
,
Ming-Yuan Sud Department of Molecular and Cell Biology and California Institute for Quantitative Biosciences, University of California, Berkeley, CA, USA;e Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA
,
Riccardo Trapannonea Department of Biochemistry and Cell Biology, Max F. Perutz Laboratories (MFPL), University of Vienna, Vienna BioCenter, Vienna, Austria
,
Martin Sztachoa Department of Biochemistry and Cell Biology, Max F. Perutz Laboratories (MFPL), University of Vienna, Vienna BioCenter, Vienna, Austria
,
Alberto Danielia Department of Biochemistry and Cell Biology, Max F. Perutz Laboratories (MFPL), University of Vienna, Vienna BioCenter, Vienna, Austria
,
Xiaoshan Shid Department of Molecular and Cell Biology and California Institute for Quantitative Biosciences, University of California, Berkeley, CA, USA
,
Gabriele Zaffagninia Department of Biochemistry and Cell Biology, Max F. Perutz Laboratories (MFPL), University of Vienna, Vienna BioCenter, Vienna, AustriaORCID Iconhttps://orcid.org/0000-0002-6554-7352
ORCID Icon,
Annamaria Gampera Department of Biochemistry and Cell Biology, Max F. Perutz Laboratories (MFPL), University of Vienna, Vienna BioCenter, Vienna, Austria
,
Martina Schuschniga Department of Biochemistry and Cell Biology, Max F. Perutz Laboratories (MFPL), University of Vienna, Vienna BioCenter, Vienna, Austria
,
Dorotea Fracchiollaa Department of Biochemistry and Cell Biology, Max F. Perutz Laboratories (MFPL), University of Vienna, Vienna BioCenter, Vienna, Austria
,
Daniel Bernklaua Department of Biochemistry and Cell Biology, Max F. Perutz Laboratories (MFPL), University of Vienna, Vienna BioCenter, Vienna, Austria
,
Julia Romanova Department of Biochemistry and Cell Biology, Max F. Perutz Laboratories (MFPL), University of Vienna, Vienna BioCenter, Vienna, Austria
,
Markus Hartla Department of Biochemistry and Cell Biology, Max F. Perutz Laboratories (MFPL), University of Vienna, Vienna BioCenter, Vienna, AustriaORCID Iconhttps://orcid.org/0000-0002-4970-7336
ORCID Icon,
James H. Hurleyd Department of Molecular and Cell Biology and California Institute for Quantitative Biosciences, University of California, Berkeley, CA, USA;e Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA
,
Oliver Daumkeb Crystallography, Max-Delbrück-Center for Molecular Medicine, Berlin, Germany;c Institute of Chemistry and Biochemistry, Freie Universität Berlin, Berlin, Germany
&
Sascha Martensa Department of Biochemistry and Cell Biology, Max F. Perutz Laboratories (MFPL), University of Vienna, Vienna BioCenter, Vienna, AustriaCorrespondence[email protected]
ORCID Iconhttps://orcid.org/0000-0003-3786-8199
ORCID Icon show all
Pages 1475-1477 | Received 12 Apr 2019, Accepted 01 May 2019, Published online: 22 May 2019

Figures & data

Figure 1. Model for cargo-induced autophagosome formation. The cargo receptor SQSTM1 directly binds to RB1CC1 and recruits it to the cargo. RB1CC1, a component of the ULK1 complex, is necessary for the recruitment of the ATG12–ATG5-ATG16L1 complex, which in turn supports the conjugation of Atg8-family proteins to the growing phagophore. Concentrated Atg8-family proteins on the phagophore bind to the SQSTM1 LIR motif, thereby displacing RB1CC1 from the receptor and confining it to regions of the cargo where the phagophore has not yet formed.

Figure 1. Model for cargo-induced autophagosome formation. The cargo receptor SQSTM1 directly binds to RB1CC1 and recruits it to the cargo. RB1CC1, a component of the ULK1 complex, is necessary for the recruitment of the ATG12–ATG5-ATG16L1 complex, which in turn supports the conjugation of Atg8-family proteins to the growing phagophore. Concentrated Atg8-family proteins on the phagophore bind to the SQSTM1 LIR motif, thereby displacing RB1CC1 from the receptor and confining it to regions of the cargo where the phagophore has not yet formed.

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