Modulation of the Ca2+-Activated Cl− Channel by 14-3-3ε

Chan, Hsiao Chang; Wu, Wei; So, S.C.; Chung, Yiu Wa; Tsang, Lai Ling; Wang, X.F; Yan, Yizhong; Luk, Sharon; Siu, Stephanie; Tsui, Stephen Kwok‐Wing; Fung, Kwok‐Pui; Lee, C.Y; Waye, Mary Miu Yee

doi:10.1006/bbrc.2000.2454

Cited by 24 publications

(12 citation statements)

References 24 publications

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“…The interaction between c-Raf kinase and Cam-agarose was specific because ERK binding to this column was not detected. 14-3-3 proteins have been shown to be a Cam-interacting partner (20,21) and also associated with c-Raf kinase binding (22,23). Consistent with these observations, 14-3-3 proteins were retained on the Cam column as suggested using a pan-specific 14-3-3 antibody.…”

Section: Resultssupporting

confidence: 52%

Gonadotropin-Releasing Hormone Induction of Extracellular-Signal Regulated Kinase Is Blocked by Inhibition of Calmodulin

Roberson

Bliss

Xie

et al. 2005

Molecular Endocrinology

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Our previous studies demonstrate that GnRH-induced ERK activation required influx of extracellular Ca2+ in alphaT3-1 and rat pituitary cells. In the present studies, we examined the hypothesis that calmodulin (Cam) plays a fundamental role in mediating the effects of Ca2+ on ERK activation. Cam inhibition using W7 was sufficient to block GnRH-induced reporter gene activity for the c-Fos, murine glycoprotein hormone alpha-subunit, and MAPK phosphatase (MKP)-2 promoters, all shown to require ERK activation. Inhibition of Cam (using a dominant negative) was sufficient to block GnRH-induced ERK but not c-Jun N-terminal kinase activity activation. The Cam-dependent protein kinase (CamK) II inhibitor KN62 did not recapitulate these findings. GnRH-induced phosphorylation of MAPK/ERK kinase 1 and c-Raf kinase was blocked by Cam inhibition, whereas activity of phospholipase C was unaffected, suggesting that Ca2+/Cam modulation of the ERK cascade potentially at the level of c-Raf kinase. Enrichment of Cam-interacting proteins using a Cam agarose column revealed that c-Raf kinase forms a complex with Cam. Reconstitution studies reveal that recombinant c-Raf kinase can associate directly with Cam in a Ca2+-dependent manner and this interaction is reduced in vitro by addition of W7. Cam was localized in lipid rafts consistent with the formation of a Ca2+-sensitive signaling platform including the GnRH receptor and c-Raf kinase. These data support the conclusion that Cam may have a critical role as a Ca2+ sensor in specifically linking Ca2+ flux with ERK activation within the GnRH signaling pathway.

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Section: Resultssupporting

confidence: 52%

Gonadotropin-Releasing Hormone Induction of Extracellular-Signal Regulated Kinase Is Blocked by Inhibition of Calmodulin

Roberson

Bliss

Xie

et al. 2005

Molecular Endocrinology

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“…Furthermore, we recently showed that K + and H + flux is asymmetric in early embryos and controls LR asymmetry ). 14-3-3 proteins (including 14-3-3E) have recently been shown to be able to modulate K + currents in Xenopus oocytes (Chan et al, 2000;Benzing et al, 2002). In light of the differential LR subcellular localization of ion pumps, such as the H + /K + -ATPase , and of the ability of 14-3-3 proteins to control the localization of their binding partner (Muslin and Xing, 2000), we propose that 14-3-3E protein functions in the LR pathway by differentially regulating the endogenous activity and/or localization of LRrelevant ion channels or pumps on each side of the midline.…”

Section: Discussionmentioning

confidence: 99%

Fusicoccin signaling reveals 14-3-3 protein function as a novel step in left-right patterning during amphibian embryogenesis

Bunney

Boer

Levin³

2003

Development

102

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To gain insight into the molecular mechanisms underlying the control of morphogenetic signals by H+ flux during embryogenesis, we tested Fusicoccin-A (FC), a compound produced by the fungus Fusicoccum amygdali Del. In plant cells, FC complexes with 14-3-3 proteins to activate H+ pumping across the plasma membrane. It has long been thought that FC acts on higher plants only; here, we show that exposing frog embryos to FC during early development specifically results in randomization of the asymmetry of the left-right (LR) axis (heterotaxia). Biochemical and molecular-genetic evidence is presented that 14-3-3-family proteins are an obligate component of Xenopus FC receptors and that perturbation of 14-3-3 protein function results in heterotaxia. The subcellular localization of 14-3-3 mRNAs and proteins reveals novel cytoplasmic destinations, and a left-right asymmetry at the first cell division. Using gain-of-function and loss-of-function experiments, we show that 14-3-3E protein is likely to be an endogenous and extremely early aspect of LR patterning. These data highlight a striking conservation of signaling pathways across kingdoms, suggest common mechanisms of polarity establishment between C. elegans and vertebrate embryos, and uncover a novel entry point into the pathway of left-right asymmetry determination.

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“…For example, the scaffold–adapter 14‐3‐3 proteins serve as major convergence points for osmosensory signals and are characterized by their ability to regulate multiple downstream signal transduction pathways and diverse effectors (Fu et al , 2000; Kültz et al , 2001; Koskinen et al , 2004). In the euryhaline teleost F. heteroclitus , 14‐3‐3 proteins are suspected of modulating ion transport during osmotic stress in several ways, including through the activation of the H + ‐ATPase, which in turn energizes ion transport via the Na + , K + ‐ATPase, by decreasing protein kinase C activity, which in turn can inhibit Na + , K + ‐ATPase in the gill epithelium (Crombie et al , 1996) and by binding calmodulin, which inhibits the Ca +2 activated Cl − channel (Chan et al , 2000; Kültz et al , 2001).…”

Section: Co‐ordination Of Osmotic Stress Responses Through Osmosensinmentioning

confidence: 99%

Co‐ordination of osmotic stress responses through osmosensing and signal transduction events in fishes

Evans

2010

Journal of Fish Biology

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This review centres upon the molecular regulation of osmotic stress responses in fishes, focusing on how osmosensing and signal transduction events co-ordinate changes in the activity and abundance of effector proteins during osmotic stress and how these events integrate into osmotic stress responses of varying magnitude. The concluding sections discuss the relevance of osmosensory signal transduction to the evolution of euryhalinity and present experimental approaches that may best stimulate future research. Iterating the importance of osmosensing and signal transduction during fish osmoregulation may be pertinent amidst the increased use of genomic technologies that typically focus solely on changes in the abundances of gene products, and may limit insight into critical upstream events that occur mainly through post-translational mechanisms.

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Modulation of the Ca2+-Activated Cl− Channel by 14-3-3ε

Cited by 24 publications

References 24 publications

Gonadotropin-Releasing Hormone Induction of Extracellular-Signal Regulated Kinase Is Blocked by Inhibition of Calmodulin

Gonadotropin-Releasing Hormone Induction of Extracellular-Signal Regulated Kinase Is Blocked by Inhibition of Calmodulin

Fusicoccin signaling reveals 14-3-3 protein function as a novel step in left-right patterning during amphibian embryogenesis

Co‐ordination of osmotic stress responses through osmosensing and signal transduction events in fishes

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