The annexins: spatial and temporal coordination of signaling events during cellular stress

Monastyrskaya, Katia; Babiychuk, Eduard B.; Draeger, Annette

doi:10.1007/s00018-009-0027-1

Cited by 124 publications

(99 citation statements)

References 210 publications

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“…We found that starvation provokes a translocation of this protein from the Golgi complex to lysosomes and, to a much lesser extent, to late endosomes. Several reports have associated annexin A5 with the Golgi complex and the ER (Barwise and Walker, 1996;Rambotti et al, 1993), late endosomal membranes (Diakonova et al, 1997;Rambotti et al, 1993) and also with the nucleus (reviewed by Monastyrskaya et al, 2009). Our results do not show a significant nuclear localisation of annexin A5, probably because our experiments were carried out in the absence of serum, which appears to contain factors necessary for nuclear localisation (Barwise and Walker, 1996;Mohiti et al, 1997).…”

Section: Discussionsupporting

confidence: 38%

“…They are present in all eukaryotic cells and share a common folding motif, the 'annexin core', with Ca 2+ -and lipidbinding sites. Annexins participate in a variety of intracellular processes, ranging from the regulation of membrane dynamics to cell migration, proliferation and apoptosis (Monastyrskaya et al, 2009). Annexin A5, one of the most abundant annexins in mammalian cells, has a hitherto unknown function within the intracellular environment, although it has been found to modulate the activities of protein kinase C as well as phospholipase A by interfering with their binding to negatively charged phospholipids and Ca 2+ (Russo-Marie, 1999).…”

Section: Discussionmentioning

confidence: 99%

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Annexin A5 stimulates autophagy and inhibits endocytosis

Ghislat

Aguado

Knecht

2012

Journal of Cell Science

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SummaryMacroautophagy is a major lysosomal catabolic process activated particularly under starvation in eukaryotic cells. A new organelle, the autophagosome, engulfs cytoplasmic substrates, which are degraded after fusion with endosomes and/or lysosomes. During a shotgun proteome analysis of purified lysosomal membranes from mouse fibroblasts, a Ca 2+ -dependent phospholipid-binding protein, annexin A5, was found to increase on lysosomal membranes under starvation. This suggests a role for this protein, an abundant annexin with a still unknown intracellular function, in starvation-induced lysosomal degradation. Transient overexpression and silencing experiments showed that annexin A5 increased lysosomal protein degradation, and colocalisation experiments, based on GFP sensitivity to lysosomal acidic pH, indicated that this was mainly the result of inducing autophagosome-lysosome fusion. Annexin A5 also inhibited the endocytosis of a fluid-phase marker and cholera toxin, but not receptor-mediated endocytosis. Therefore, we propose a double and opposite role of annexin A5 in regulating the endocytic and autophagic pathways and the fusion of autophagosomes with lysosomes and endosomes.

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Section: Discussionsupporting

confidence: 38%

Section: Discussionmentioning

confidence: 99%

Annexin A5 stimulates autophagy and inhibits endocytosis

Ghislat

Aguado

Knecht

2012

Journal of Cell Science

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“…25,[27][28][29] It is, moreover, instrumental in the inward vesiculation in multivesicular endosomes -a process that is driven by a budding and fusion of the organellelimiting membrane. 30 Hence, massive, Ca 2 þ -induced local accumulation of annexin A1 would cross-link the neck membranes of a bleb and efficiently block any communication between it and the rest of the cell.…”

Section: Resultsmentioning

confidence: 99%

Blebbing confers resistance against cell lysis

et al. 2010

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The plasma membrane constitutes a barrier that maintains the essential differences between the cytosol and the extracellular environment. Plasmalemmal injury is a common event during the life of many cells that often leads to their premature, necrotic death. Blebbing -a display of plasmalemmal protrusions -is a characteristic feature of injured cells. In this study, we disclose a previously unknown role for blebbing in furnishing resistance to plasmalemmal injury. Blebs serve as precursors for injuryinduced intracellular compartments that trap damaged segments of the plasma membrane. Hence, loss of cytosol and the detrimental influx of extracellular constituents are confined to blebs that are sealed off from the cell body by plugs of annexin A1 -a Ca 2 þ -and membrane-binding protein. Our findings shed light on a fundamental process that contributes to the survival of injured cells. By targeting annexin A1/blebbing, new therapeutic approaches could be developed to avert the necrotic loss of cells in a variety of human pathologies.

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“…In addition, pH and other lipids, such as phosphatidylinositol-4,5-bisphosphate, cholesterol and ceramide, facilitate the opportunity for differential function and behavior of annexins (Gerke and Moss, 2002;Hayes et al, 2004;Gerke et al, 2005;Grewal and Enrich, 2009;Monastyrskaya et al, 2009).…”

Section: +mentioning

confidence: 99%

Annexins – insights from knockout mice

Grewal

Wason

Enrich

et al. 2016

Biological Chemistry

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Annexins are a highly conserved protein family that bind to phospholipids in a calcium (Ca 2+ ) -dependent manner. Studies with purified annexins, as well as overexpression and knockdown approaches identified multiple functions predominantly linked to their dynamic and reversible membrane binding behavior. However, most annexins are found at multiple locations and interact with numerous proteins. Furthermore, similar membrane binding characteristics, overlapping localizations and shared interaction partners have complicated identification of their precise functions. To gain insight into annexin function in vivo, mouse models deficient of annexin A1 (AnxA1), A2, A4, A5, A6 and A7 have been generated. Interestingly, with the exception of one study, all mice strains lacking one or even two annexins are viable and develop normally. This suggested redundancy within annexins, but examining these knockout (KO) strains under stress conditions revealed striking phenotypes, identifying underlying mechanisms specific for individual annexins, often supporting Ca 2+ homeostasis and membrane transport as central for annexin biology. Conversely, mice lacking AnxA1 or A2 show extracellular functions relevant in health and disease that appear independent of membrane trafficking or Ca 2+ signaling. This review will summarize the mechanistic insights gained from studies utilizing mouse models lacking members of the annexin family.

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The annexins: spatial and temporal coordination of signaling events during cellular stress

Cited by 124 publications

References 210 publications

Annexin A5 stimulates autophagy and inhibits endocytosis

Annexin A5 stimulates autophagy and inhibits endocytosis

Blebbing confers resistance against cell lysis

Annexins – insights from knockout mice

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