Remodeling of secretory compartments creates CUPS during nutrient starvation

Cruz-García, David; Curwin, Amy J.; Popoff, Jean-François; Bruns, C.; Durán, Juan M.; Malhotra, Vivek

doi:10.1083/jcb.201407119

Cited by 53 publications

(71 citation statements)

References 31 publications

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“…In addition, several granule-like structures have been observed in stationary phase cultures 1314151819. However, it remains unclear how different granule structures are organized in these two types of cells.…”

Section: Resultsmentioning

confidence: 99%

Differentiated cytoplasmic granule formation in quiescent and non-quiescent cells upon chronological aging

Lee¹,

Cheng²,

Chao³

et al. 2016

MIC

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Stationary phase cultures represent a complicated cell population comprising at least two different cell types, quiescent (Q) and non-quiescent (NQ) cells. Q and NQ cells have different lifespans and cell physiologies. However, less is known about the organization of cytosolic protein structures in these two cell types. In this study, we examined Q and NQ cells for the formation of several stationary phase-prevalent granule structures including actin bodies, proteasome storage granules, stress granules, P-bodies, the compartment for unconventional protein secretion (CUPS), and Hsp42-associated stationary phase granules (Hsp42-SPGs). Most of these structures preferentially form in NQ cells, except for Hsp42-SPGs, which are enriched in Q cells. When nutrients are provided, NQ cells enter mitosis less efficiently than Q cells, likely due to the time requirement for reorganizing some granule structures. We observed that heat shock-induced misfolded proteins often colocalize to Hsp42-SPGs, and Q cells clear these protein aggregates more efficiently, suggesting that Hsp42-SPGs may play an important role in the stress resistance of Q cells. Finally, we show that the cell fate of NQ cells is largely irreversible even if they are allowed to reenter mitosis. Our results reveal that the formation of different granule structures may represent the early stage of cell type differentiation in yeast stationary phase cultures.

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Section: Resultsmentioning

confidence: 99%

Differentiated cytoplasmic granule formation in quiescent and non-quiescent cells upon chronological aging

Lee¹,

Cheng²,

Chao³

et al. 2016

MIC

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show abstract

“…This direct interaction with the protein cargo has already been observed in other situations . Some specific roles have also emerged, such as the participation in the formation of specific autophagosome‐like structures (named compartments of unconventional protein secretion, or CUPS), but regardless of their true nature and existence in yeast , so far there are no evidences that these structures exist in mammalian cells .…”

Section: Introductionmentioning

confidence: 87%

The GRASP domain in golgi reassembly and stacking proteins: differences and similarities between lower and higher Eukaryotes

et al. 2019

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The Golgi complex is part of the endomembrane system and is responsible for receiving transport cargos from the endoplasmic reticulum and for sorting and targeting them to their final destination. To perform its function in higher eukaryotic cells, the Golgi needs to be correctly assembled as a flattened membrane sandwich kept together by a protein matrix. The precise mechanism controlling the Golgi cisternae assembly is not yet known, but it is widely accepted that the Golgi Reassembly and Stacking Protein (GRASP) is a main component of the Golgi protein matrix. Unlike mammalian cells, which have two GRASP genes, lower eukaryotes present only one gene and distinct Golgi cisternae assembly. In this study, we performed a set of biophysical studies to get insights on the structural properties of the GRASP domains (DGRASPs) from both human GRASP55 and GRASP65 and compare them with GRASP domains from lower eukaryotes (Saccharomyces cerevisiae and Cryptococcus neoformans). Our data suggest that both human DGRASPs are essentially different from each other and that DGRASP65 is more similar to the subgroup of DGRASPs from lower eukaryotes in terms of its biophysical properties. GRASP55 is present mainly in the Golgi medial and trans faces, which are absent in both fungi, while GRASP65 is located in the cis‐Golgi. We suggest that the GRASP65 gene is more ancient and that its paralogue GRASP55 might have appeared later in evolution, together with the medial and trans Golgi faces in mammalians.

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“…First, although genetic interconnections between ATGs and Grh1, the yeast GRASP orthologue, exist in Saccharomyces cerevisiae, recent research questions whether autophagy and Grh1 truly converge on a common secretory intermediate 133 . Second, although the early autophagosome-forming core machinery appears to be genetically required for unconventional secretion, it is unclear how the molecules to be secreted, such as Acb1 or CFTR, are actually incorporated into autophagosomes.…”

Section: Box 2 | Autophagy and Secretionmentioning

confidence: 99%

Autophagy at the crossroads of catabolism and anabolism

Kaur

Debnath

2015

Nat Rev Mol Cell Biol

808

801

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Remodeling of secretory compartments creates CUPS during nutrient starvation

Abstract: Starvation triggers relocation of membranes of the secretory compartments and endosomes to create a compartment called CUPS, which may be involved in processing and secretion of proteins that cannot enter the ER–Golgi pathway.

Cited by 53 publications

References 31 publications

Differentiated cytoplasmic granule formation in quiescent and non-quiescent cells upon chronological aging

Differentiated cytoplasmic granule formation in quiescent and non-quiescent cells upon chronological aging

The GRASP domain in golgi reassembly and stacking proteins: differences and similarities between lower and higher Eukaryotes

Autophagy at the crossroads of catabolism and anabolism

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