Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Quality control of glycogen through direct ubiquitylation by RNF213.
Journal, issue, pages	Nature, Year 2026
Publish date	Sep 15, 2026
Authors	Matthew C J Yip / Katerina Naydenova / Elsje G Otten / Alexander Heatley / Agnes Moe / Leonie Anton / Lucía de Los Reyes-Ramírez / Helen E Jolin / Frederic Langevin / Michal Wiacek / Catarina Franco / Anne Bertolotti / Wanda Kukulski / Andrew N J McKenzie / Felix Randow /
PubMed Abstract	Quality control of biomolecules is vital for organismal health. While DNA repair and protein quality control are well understood, how cells monitor other important biomolecules such as glycogen ...Quality control of biomolecules is vital for organismal health. While DNA repair and protein quality control are well understood, how cells monitor other important biomolecules such as glycogen remains ill-defined. The accumulation of aberrant, poorly branched glycogen into insoluble polyglucosan bodies causes severe disease. Here, we discover autophagy of ubiquitylated aberrant glycogen as a previously unrecognized quality control mechanism safeguarding the brain from polyglucosan buildup. This mechanism depends on the E3 ubiquitin ligase RNF213. Mice lacking ligase activity in RNF213 accumulate polyglucosan in cerebellum, pons, and hippocampus. Using cells engineered to produce polyglucosan, we show that RNF213 selectively ubiquitylates abnormal glycogen. Cryo-EM analysis of RNF213 bound to glycogen-derived maltoheptaose revealed its CBM20 domain binds linear oligosaccharides. Disrupting carbohydrate binding results in gain of E3 ligase activity towards physiological glycogen, indicating the CBM20 domain limits RNF213 activity towards physiological glycogen. Epistasis analysis places RNF213 upstream of LUBAC, suggesting a hierarchical network of multiple E3 ligases surveying glycogen quality. Ubiquitylated polyglucosan recruits the autophagy receptors SQSTM1, TAX1BP1, and optineurin, thereby triggering uptake into autophagosomes. These findings identify RNF213 as a quality control factor preventing polyglucosan accumulation in astrocytes through direct ubiquitylation of polyglucosan, revealing an essential role for non-protein ubiquitylation in glycogen quality control.
External links	Nature / PubMed:42744304
Methods	EM (single particle) / EM (tomography)
Resolution	2.7 - 3.1 Å
Structure data	55686 9t8h EMDB-55686, PDB-9t8h: Murine RNF213 bound to maltoheptaose Method: EM (single particle) / Resolution: 3.0 Å EMDB-55687: Murine RNF213 bound to maltoheptaose (Consensus refinement) Method: EM (single particle) / Resolution: 3.0 Å EMDB-55688: Murine RNF213 bound to maltoheptaose (Focused refinement of ATPase domain) Method: EM (single particle) / Resolution: 2.7 Å EMDB-55689: Murine RNF213 bound to maltoheptaose (Focused refinement of stalk) Method: EM (single particle) / Resolution: 3.0 Å EMDB-55690: Murine RNF213 bound to maltoheptaose (Focused refinement of top of stalk) Method: EM (single particle) / Resolution: 2.8 Å EMDB-55691: Murine RNF213 bound to maltoheptaose (Focused refinement of CBM20 domain) Method: EM (single particle) / Resolution: 2.9 Å EMDB-55692: Murine RNF213 bound to maltoheptaose (Focused refinement of E3 module) Method: EM (single particle) / Resolution: 2.8 Å EMDB-55693: Murine RNF213 bound to maltoheptaose (Focused refinement of E3 shell) Method: EM (single particle) / Resolution: 2.9 Å 55694 9t8i EMDB-55694, PDB-9t8i: Murine RNF213 Method: EM (single particle) / Resolution: 3.1 Å EMDB-55695: Murine RNF213 (Consensus refinement) Method: EM (single particle) / Resolution: 3.0 Å EMDB-55696: Murine RNF213 (Focused refinement of ATPase domain) Method: EM (single particle) / Resolution: 2.9 Å EMDB-55697: Murine RNF213 (Focused refinement of stalk) Method: EM (single particle) / Resolution: 3.1 Å EMDB-55698: Murine RNF213 (Focused refinement of top of stalk) Method: EM (single particle) / Resolution: 3.0 Å EMDB-55699: Murine RNF213 (Focused refinement of CBM20 domain) Method: EM (single particle) / Resolution: 3.1 Å EMDB-55700: Murine RNF213 (Focused refinement of E3 module) Method: EM (single particle) / Resolution: 2.9 Å EMDB-55701: Murine RNF213 (Focused refinement of E3 shell) Method: EM (single particle) / Resolution: 3.0 Å EMDB-59437: Murine RNF213 (Y434A) (Focused refinement of ATPase domain) Method: EM (single particle) / Resolution: 2.9 Å EMDB-59438: Murine RNF213 (Y434A) (focused refinement of stalk) Method: EM (single particle) / Resolution: 3.1 Å EMDB-59439: murine RNF213 (Y434A) (focused refinement of top of stalk) Method: EM (single particle) / Resolution: 3.0 Å EMDB-59440: murine RNF213 (Y434A) (focused refinement of CBM20 domain) Method: EM (single particle) / Resolution: 3.1 Å EMDB-59441: murine RNF213 (Y434A) (focused refinement of E3) Method: EM (single particle) / Resolution: 3.1 Å EMDB-59442: murine RNF213 (Y434A) (focused refinement of E3 shell) Method: EM (single particle) / Resolution: 2.9 Å EMDB-59443: murine RNF213 (Y434A) (consensus refinement) Method: EM (single particle) / Resolution: 3.1 Å 59444 33hm EMDB-59444, PDB-33hm: Murine RNF213 (Y434A) Method: EM (single particle) / Resolution: 3.1 Å EMDB-59854: Cryo-electron tomogram of MEF cell containing polyglucosan Method: EM (tomography)
Chemicals	ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying moleculeYM ChemComp-ZN*: Unknown entry
Source	mus musculus (house mouse)
Keywords	SUGAR BINDING PROTEIN / E3 ubiquitin ligase / AAA+ ATPase / CBM20