Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Membrane Binding and Homodimerization of Atg16 Via Two Distinct Protein Regions is Essential for Autophagy in Yeast.

Journal of molecular biology - 5 Mar 2021

Popelka Hana, Reinhart Erin F, Metur Shree Padma, Leary Kelsie A, Ragusa Michael J, Klionsky Daniel J

Abstract excerpt

Macroautophagy is a bulk degradation mechanism in eukaryotic cells. Efficiency of an essential step of this process in yeast, Atg8 lipidation, relies on the presence of Atg16, a subunit of the Atg12-Atg5-Atg16 complex acting as the E3-like enzyme in the ubiquitination-like reaction. A current view on the functional structure of Atg16 in the yeast S. cerevisiae comes from the two crystal structures that reveal the...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Autophagy-Related Protein 5
Share to Autophagy-Related Protein 8 Family

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Autophagy-Related Proteins

Share to Hydrophobic and Hydrophilic Interactions

Share to Liposomes

Share to Protein Conformation, alpha-Helical

Share to Protein Conformation, beta-Strand

Share to Protein Interaction Domains and Motifs

Source

Open in PubMed Open full text

Identifiers

PMID: 33484718
DOI: 10.1016/j.jmb.2021.166809
PMCID: PMC7924733

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Membrane Binding and Homodimerization of Atg16 Via Two Distinct Protein Regions is Essential for Autophagy in Yeast.PMID 33484718Read ↗

ATG16L1 membrane recruitment in autophagySemantic proximity Read ↗

Dissecting the role of the Atg12-Atg5-Atg16 complex during autophagosome formation.Semantic proximity Read ↗

Insights into autophagosome maturation revealed by the structures of ATG5 with its interacting partners.Semantic proximity Read ↗

Reconstitution of autophagosomal membrane tethering reveals that Atg11 can bind and cluster vesicles on cargo mimeticsSemantic proximity Read ↗

RAB33B recruits the ATG16L1 complex to the phagophore via a noncanonical RAB binding proteinSemantic proximity Read ↗

Crystal structure of the Rab33B/Atg16L1 effector complex.Semantic proximity Read ↗

Structural basis of ATG3 recognition by the autophagic ubiquitin-like protein ATG12.Semantic proximity Read ↗

Structural and mechanistic basis for membrane recognition and activation of the vacuolar lipase Atg15.Semantic proximity Read ↗

Membrane scission driven by the PROPPIN Atg18.Semantic proximity Read ↗

Structure and Dynamics in the ATG8 Family From Experimental to Computational TechniquesSemantic proximity Read ↗

Transmembrane helix hydrophobicity is an energetic barrier during the retrotranslocation of integral membrane ERAD substrates.Semantic proximity Read ↗

Structural basis of Vps33A recruitment to the human HOPS complex by Vps16.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.