Jieqiong Gao, Lars Langemeyer ... Christian Ungermann
The endosomal GEF Mon1-Ccz1 binds to Atg8 on autophagosomes, and recruits its substrate, the Rab7-like Ypt7, which then mediates fusion of the autophagosomes with the lysosome.
An image-based multiplex autophagosome RNAi screen targeting all Rab GTPases as well as their GAPs and GEFs identifies the Rab GEF SMCR8 as multifaceted autophagy modulator, which regulates kinase activity and gene expression of ULK1.
A posttranslational regulatory mechanism for a Ras family small GTPase could open up new directions to understand and control the Ras family of proteins that are important for physiology and diseases.
Ryan C Vignogna, Mariateresa Allocca ... Gregory I Lang
Experimental evolution of yeast models of congenital disorders of glycosylation reveals that reduction, but not loss, of phosphoglucomutase activity best compensates for impaired phosphomannomutase activity.
The crosstalk between autophagy and the phagocytosis of apoptotic cells, two cellular clearance pathways, promotes the fusion of the double-membrane autophagosomes to the phagosomes and plays an important role in the degradation of engulfed apoptotic cells.
Phosphorylation of a core trafficking component, the COPII coat subunit Sec24, regulates cross-talk between the secretory and autophagy machinery during starvation.
Daniel K Weber, U Venkateswara Reddy ... Gianluigi Veglia
A spectroscopic analysis of the sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA)-phospholamban membrane complex reveals the importance of the relative transmembrane orientation for inhibition or activation of the ATPase.
Two GAP proteins bound to mitochondria regulate the enyzme Rab7, and thereby the expansion of the isolation membrane during mitophagy, downstream of PINK1 and Parkin, two proteins that are mutated in familial Parkinson's disease.
Under normal nutritional conditions, G-protein coupled receptors can control autophagy by regulating the degradation of key autophagic regulator Atg14L through ZBTB16-mediated ubiquitination and proteasome degradation.
A new post-translational regulatory mechanism of K-Ras is identified, which expands the function of reversible protein lysine fatty acylation and offers new possibility to target the K-Ras oncoprotein.
