Atg11

Backues, Steven K.; Klionsky, Daniel J.

doi:10.4161/auto.21153

Cited by 13 publications

(2 citation statements)

References 24 publications

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“…11,25 Atg11 is a coiled-coil protein suggested to function as a tether in autophagy. 32 For the second intersection, we showed a PM-recycling phenotype for ypt31D/32ts under permissive growth conditions that do not block Golgi exit, and identified Rcy1 as a PM recycling-specific effector of Ypt31/32.…”

Section: Coordination Of the Exocytic And Cellular Recycling Pathwaysmentioning

confidence: 99%

Ypt/Rab GTPases regulate two intersections of the secretory and the endosomal/lysosomal pathways

Lipatova

Segev

2014

Cellular Logistics

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Section: Coordination Of the Exocytic And Cellular Recycling Pathwaysmentioning

confidence: 99%

Ypt/Rab GTPases regulate two intersections of the secretory and the endosomal/lysosomal pathways

Lipatova

Segev

2014

Cellular Logistics

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“…This suggests that the Atg1-Atg11 complex has two functions in autophagy: promoting autophagy initiation and regulating phagophore expansion. The function of Atg11 during nucleation of selective autophagosomes might depend on properties that are similar to those of Atg17, including the recruitment of Atg9 vesicles to the PAS (Backues and Klionsky, 2012).…”

Section: Box 3 Experimental Approaches Involving Artificial Membranesmentioning

confidence: 99%

Reconstruction of destruction – in vitro reconstitution methods in autophagy research

Moparthi

Wollert

2018

Journal of Cell Science

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Autophagy is one of the most elaborative membrane remodeling systems in eukaryotic cells. Its major function is to recycle cytoplasmic material by delivering it to lysosomes for degradation. To achieve this, a membrane cisterna is formed that gradually captures cargo such as organelles or protein aggregates. The diversity of cargo requires autophagy to be highly versatile to adapt the shape of the phagophore to its substrate. Upon closure of the phagophore, a doublemembrane-surrounded autophagosome is formed that eventually fuses with lysosomes. In response to environmental cues such as cytotoxicity or starvation, bulk cytoplasm can be captured and delivered to lysosomes. Autophagy thus supports cellular survival under adverse conditions. During the past decades, groundbreaking genetic and cell biological studies have identified the core machinery involved in the process. In this Review, we are focusing on in vitro reconstitution approaches to decipher the details and spatiotemporal control of autophagy, and how such studies contributed to our current understanding of the pathways in yeast and mammals. We highlight studies that revealed the function of the autophagy machinery at a molecular level with respect to its capacity to remodel membranes.

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Regulation of peroxisome dynamics by phosphorylation

Oeljeklaus

Schummer

Mastalski

et al. 2016

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

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Peroxisomes are highly dynamic organelles that can rapidly change in size, abundance, and protein content in response to alterations in nutritional and other environmental conditions. These dynamic changes in peroxisome features, referred to as peroxisome dynamics, rely on the coordinated action of several processes of peroxisome biogenesis. Revealing the regulatory mechanisms of peroxisome dynamics is an emerging theme in cell biology. These mechanisms are inevitably linked to and synchronized with the biogenesis and degradation of peroxisomes. To date, the key players and basic principles of virtually all steps in the peroxisomal life cycle are known, but regulatory mechanisms remained largely elusive. A number of recent studies put the spotlight on reversible protein phosphorylation for the control of peroxisome dynamics and highlighted peroxisomes as hubs for cellular signal integration and regulation. Here, we will present and discuss the results of several studies performed using yeast and mammalian cells that convey a sense of the impact protein phosphorylation may have on the modulation of peroxisome dynamics by regulating peroxisomal matrix and membrane protein import, proliferation, inheritance, and degradation. We further put forward the idea to make use of current data on phosphorylation sites of peroxisomal and peroxisome-associated proteins reported in advanced large-scale phosphoproteomic studies.

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Atg11

Cited by 13 publications

References 24 publications

Ypt/Rab GTPases regulate two intersections of the secretory and the endosomal/lysosomal pathways

Ypt/Rab GTPases regulate two intersections of the secretory and the endosomal/lysosomal pathways

Reconstruction of destruction – in vitro reconstitution methods in autophagy research

Regulation of peroxisome dynamics by phosphorylation

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