S100A13 Is Involved in the Regulation of Fibroblast Growth Factor-1 and p40 Synaptotagmin-1 Release in Vitro

Carreira, Carla Mouta; LaVallee, Theresa; Tarantini, Francesca; Jackson, Anthony; Lathrop, Julia Tait; Hampton, Brian; Burgess, Wilson H.; Maciag, Thomas

doi:10.1074/jbc.273.35.22224

Cited by 116 publications

(118 citation statements)

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“…When cultured cells were deprived of serum, both ProTa and S100A13 were completely lost from cells at the time point of 3 h. The cellular loss of S100A13 and ProTa was also blocked by amlexanox, a potent inhibitor of S100A13. [8][9][10][11]18 Quantitative immunoblot analysis confirmed that amlexanox abolished the serum-deprivation stressinduced extracellular release of ProTa (Figure 3c). …”

Section: Resultsmentioning

confidence: 67%

“…[15][16][17] It has been reported that S100A13 is involved in the non-classical extracellular release of target molecules containing fibroblast growth factor-1 (FGF-1) and interleukin-1a. [9][10][11]19,34,35 In this study, we successfully showed that ProTa is another example of stress-induced non-vesicular extracellular release, using S100A13, a cargo molecule. Furthermore, we revealed that the C-terminal regions of ProTa and S100A13 are essential for their interaction, which precedes extracellular release of both proteins, and that caspase-3 cleaves off C-terminal regions of ProTa.…”

Section: Discussionmentioning

confidence: 99%

“…This re-distribution was completely reversed by co-injection of ATP (Figure 2c, upper right 4 panels). On the other hand, serum deprivation caused a re-distribution of ProTa from nucleus to cytosol, but did not result in extracellular release in the presence of amlexanox, which inhibits the release of proteins lacking a signal peptide sequence [8][9][10][11] (Figure 2c, lower panels). Similarly, co-injection of ATP reversed the nucleusto-cytosol export.…”

Section: Resultsmentioning

confidence: 99%

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Stress-induced non-vesicular release of prothymosin-α initiated by an interaction with S100A13, and its blockade by caspase-3 cleavage

Matsunaga

Ueda

2010

Cell Death Differ

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The nuclear protein prothymosin-a (ProTa), which lacks a signal peptide sequence, is released from neurons and astrocytes on ischemic stress and exerts a unique form of neuroprotection through an anti-necrotic mechanism. Ischemic stress-induced ProTa release is initiated by a nuclear release, followed by extracellular release in a non-vesicular manner, in C6 glioma cells. These processes are caused by ATP loss and elevated Ca 2 þ , respectively. S100A13, a Ca 2 þ -binding protein, was identified to be a major protein co-released with ProTa in an immunoprecipitation assay. The Ca 2 þ -dependent interaction between ProTa and S100A13 was found to require the C-terminal peptide sequences of both proteins. In C6 glioma cells expressing a D88-98 mutant of S100A13, serum deprivation caused the release of S100A13 mutant, but not of ProTa. When cells were administered apoptogenic compounds, ProTa was cleaved by caspase-3 to generate a C-terminal peptide-deficient fragment, which lacks the nuclear localization signal (NLS). However, there was no extracellular release of ProTa. All these results suggest that necrosisinducing stress induces an extacellular release of ProTa in a non-vesicular manner, whereas apoptosis-inducing stress does not, owing to the loss of its interaction with S100A13, a cargo molecule for extracellular release.

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Section: Resultsmentioning

confidence: 67%

Section: Discussionmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Stress-induced non-vesicular release of prothymosin-α initiated by an interaction with S100A13, and its blockade by caspase-3 cleavage

Matsunaga

Ueda

2010

Cell Death Differ

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“…However, the similarities between release of FGF1 and Prdx 1 and 2 end there. In fact, although FGF1 homodimers are absolutely necessary for secretion, they form only one part of a much larger multiprotein complex that is required for release (29,30). Export from the cell then occurs via translocation through the cell membrane (31) and not via exosomal release, as shown here for Prdx1 and 2.…”

Section: Discussionmentioning

confidence: 80%

Cysteine Oxidation Targets Peroxiredoxins 1 and 2 for Exosomal Release through a Novel Mechanism of Redox-Dependent Secretion

Mullen

Hanschmann

Lillig

et al. 2015

Mol Med

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“…In cell cultures it can stimulate growth, cell migration, and differentiation. As the growth factor lacks a classical signal sequence, its mechanism of secretion is still unclear, but it appears to involve a pathway different from the classical secretion pathway through the endoplasmic reticulum and Golgi apparatus (7)(8)(9). At the cell surface, aFGF binds with high affinity to transmembrane FGF-receptors (FGFR) containing a cytoplasmic split tyrosine kinase domain.…”

mentioning

confidence: 99%

Requirement of Phosphatidylinositol 3-Kinase Activity for Translocation of Exogenous aFGF to the Cytosol and Nucleus

Klingenberg¹,

dłocha

Citores³

et al. 2000

Journal of Biological Chemistry

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Acidic fibroblast growth factor (aFGF) is a potent mitogen for many cells. Exogenous aFGF is able to enter the cytosol and nucleus of sensitive cells. There are indications that both activation of the receptor tyrosine kinase and translocation of aFGF to the nucleus are of importance for mitogenesis. However, the mechanism of transport of aFGF from the cell surface to the nucleus is poorly understood. In this work we demonstrate that inhibition of phosphatidylinositol (PI) 3-kinase by chemical inhibitors and by expression of a dominant negative mutant of PI 3-kinase blocks translocation of aFGF to the cytosol and nucleus. Translocation to the cytosol and nucleus was monitored by cell fractionation, by farnesylation of aFGF modified to contain a farnesylation signal, and by phosphorylation by protein kinase C of aFGF added externally to cells. If aFGF is fused to diphtheria toxin A-fragment, it can be artificially translocated from the cell surface to the cytoplasm by the diphtheria toxin pathway. Upon further incubation, the fusion protein enters the nucleus due to a nuclear localization sequence in aFGF. We demonstrate here that upon inhibition of PI 3-kinase the fusion protein remains in the cytosol. We also provide evidence that the phosphorylation status of the fusion protein does not regulate its nucleocytoplasmic distribution. Acidic fibroblast growth factor (aFGF)1 is considered to be involved in several important physiological and pathological processes, such as angiogenesis, wound healing (1), and atheromatosis (2-6). In cell cultures it can stimulate growth, cell migration, and differentiation. As the growth factor lacks a classical signal sequence, its mechanism of secretion is still unclear, but it appears to involve a pathway different from the classical secretion pathway through the endoplasmic reticulum and Golgi apparatus (7-9). At the cell surface, aFGF binds with high affinity to transmembrane FGF-receptors (FGFR) containing a cytoplasmic split tyrosine kinase domain. There are four different genes encoding FGFR (FGFR1-4) with several different splicing variants. aFGF also binds to heparan sulfate proteoglycans at the cell surface, although with lower affinity. Upon activation, the FGFR is phosphorylated on tyrosine residues, and it activates downstream effectors such as phosholipase C␥ and the mitogen-activated protein kinase pathway. There are some conflicting data as to whether phosphatidylinositol (PI) 3-kinase is also activated (10 -13). After binding to high affinity cell surface receptors, aFGF is translocated across cellular membranes and transported to the nucleus (14 -22). The mechanism of this process is not well defined. It depends on FGFR and, at least in the case of FGFR4, also on the intactness of the C terminus of its cytosolic part. 2Human PI 3-kinases phosphorylate PI in the 3Ј position of the inositol ring and can be divided into three main classes on the basis of in vitro substrate specificity (23). Class I phosphorylates PI, PI 4-phosphate and PI 4,5-diphosphate and include...

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S100A13 Is Involved in the Regulation of Fibroblast Growth Factor-1 and p40 Synaptotagmin-1 Release in Vitro

Cited by 116 publications

References 73 publications

Stress-induced non-vesicular release of prothymosin-α initiated by an interaction with S100A13, and its blockade by caspase-3 cleavage

Stress-induced non-vesicular release of prothymosin-α initiated by an interaction with S100A13, and its blockade by caspase-3 cleavage

Cysteine Oxidation Targets Peroxiredoxins 1 and 2 for Exosomal Release through a Novel Mechanism of Redox-Dependent Secretion

Requirement of Phosphatidylinositol 3-Kinase Activity for Translocation of Exogenous aFGF to the Cytosol and Nucleus

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