Ca2+-ATPase function is required for intracellular trafficking of the Notch receptor in Drosophila

Periz, Goran; Fortini, Mark E.

doi:10.1093/emboj/18.21.5983

Cited by 56 publications

(59 citation statements)

References 44 publications

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“…These studies suggest similar fundamental functions of P-type Ca 2+ -ATPases in plants and animals as the generation of KO mice revealed perturbations upon the targeted ablation of specific Ca 2+ -ATPases including lethality, tumorigenesis, skin and muscle diseases, deafness, balance disorders, and male infertility (20). It is assumed that these defects rely on the role of animal Ca 2+ -ATPases in the clearance of [Ca 2+ ] cyt , making them critical factors in Ca 2+ -mediated signaling cascades (21)(22)(23).…”

mentioning

confidence: 99%

A P _IIB -type Ca ²⁺ -ATPase is essential for stress adaptation in Physcomitrella patens

Qudeimat

Faltusz

Wheeler

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

101

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Transient cytosolic Ca 2+ ([Ca 2+ ] cyt ) elevations are early events in plant signaling pathways including those related to abiotic stress. The restoration of [Ca 2+ ] cyt to prestimulus levels involves ATP-driven Ca 2+ pumps, but direct evidence for an essential role of a plant Ca 2+ -ATPase in abiotic stress adaptation is missing. Here, we report on a stress-responsive Ca 2+ -ATPase gene ( PCA1 ) from the moss Physcomitrella patens. Functional analysis of PCA1 in a Ca 2+ transport-deficient yeast mutant suggests that PCA1 encodes a P IIB -type Ca 2+ -ATPase harboring an N-terminal autoinhibitory domain. In vivo localizations identified membranes of small vacuoles as the integration site for a PCA1:GFP fusion protein. PCA1 mRNA levels are up-regulated by dehydration, NaCl, and abscisic acid, and PCA1 loss-of-function mutants (Δ PCA1 ) exhibit an enhanced susceptibility to salt stress. The Δ PCA1 lines show sustained elevated [Ca 2+ ] cyt in response to salt treatment in contrast to WT that shows transient Ca 2+ elevations, indicating a direct role for PCA1 in the restoration of prestimulus [Ca 2+ ] cyt . The altered Ca 2+ response of the Δ PCA1 mutant lines correlates with altered expression levels of stress-induced genes, suggesting disturbance of a stress-associated signaling pathway. We propose that PCA1 is an essential component for abiotic stress adaptation in Physcomitrella involved in the generation of a specific salt-induced Ca 2+ signature.

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mentioning

confidence: 99%

A P _IIB -type Ca ²⁺ -ATPase is essential for stress adaptation in Physcomitrella patens

Qudeimat

Faltusz

Wheeler

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

101

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“…Furthermore, the involvement of the ER Ca 2+ store in junctional biogenesis has been demonstrated in primary keratinocytes from normal and DD patients [7] and in MDCK cell lines [32], where inhibition of the SERCA pump was shown to inhibit the formation of tight junctions and desmosome assembly. Similarly, in Drosophila S2 cells, reduced SERCA activity has been shown to impair Notch receptor processing and trafficking to the plasma membrane [33]. These findings provide explicit evidence for the compromised SERCA pump activity associated with DD pathophysiology.…”

Section: Darier's Disease and Ca 2+ Signalingmentioning

confidence: 67%

Darier’s disease: a calcium-signaling perspective

Pani

Singh

2007

Cell. Mol. Life Sci.

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Ca 2+ influx evoked across the plasma membrane upon internal store depletion is essential for a myriad of cellular functions including gene expression, cell proliferation, differentiation and even apoptosis. Darier's disease (DD), an autosomal dominant inherited disorder of the skin, arising due to mutations in the isoform 2 of the sarco (endo) plasmic reticulum Ca 2+ ATPase (SERCA2), exemplifies an anomaly of Ca 2+ signaling disturbances. Owing to loss of function mutations in SERCA2, keratinocytes in DD patients have a reduced pool of endoplasmic reticulum (ER) Ca 2+ . Importantly, the status of ER Ca 2+ is critical for the activation of a class of plasma membrane Ca 2+ channels referred to as store operated Ca 2+ channels (SOCs). The widely expressed transient receptor potential (TRP) family of channels is proposed to be SOCs. In this review we discuss DD from the viewpoint of Ca 2+ signaling and present a potential role for TRPC1 in the disease pathogenesis.

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“…To determine whether Notch accumulates predominantly in secretory or endocytic membrane compartments, we employed a live-cell antibody binding method on Catsup clonebearing wing discs. When live, non-permeabilized discs are incubated with antibodies that bind to the extracellular domain of Notch (mAb C458.2H; Diederich et al, 1994), antibody access requires exposure of the Notch epitope at the cell surface, so the antibody fails to label the secretory pool of newly synthesized Notch that has not yet reached the surface (Periz and Fortini, 1999). Incubating Catsup mosaic mutant discs with anti-Notch extracellular antibody C458.2H, followed by tissue fixation and imaging revealed that no abnormal Notch accumulation was observed for the non-permeabilized mutant cells, implying that the aberrant Notch trafficking detected in the earlier total Notch immunostaining analysis reflected an accumulation of Notch in the secretory pathway ( Fig.…”

Section: Research Articlementioning

confidence: 99%

Protein trafficking abnormalities inDrosophilatissues with impaired activity of the ZIP7 zinc transporter Catsup

et al. 2013

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Developmental patterning requires the precise interplay of numerous intercellular signaling pathways to ensure that cells are properly specified during tissue formation and organogenesis. The spatiotemporal function of the Notch signaling pathway is strongly influenced by the biosynthesis and intracellular trafficking of signaling components. Receptors and ligands must be trafficked to the cell surface where they interact, and their subsequent endocytic internalization and endosomal trafficking is crucial for both signal propagation and its down-modulation. In a forward genetic screen for mutations that alter intracellular Notch receptor trafficking in Drosophila epithelial tissues, we recovered mutations that disrupt the Catsup gene, which encodes the Drosophila ortholog of the mammalian ZIP7 zinc transporter. Loss of Catsup function causes Notch to accumulate abnormally in the endoplasmic reticulum (ER) and Golgi compartments, resulting in impaired Notch signaling. In addition, Catsup mutant cells exhibit elevated ER stress, suggesting that impaired zinc homeostasis causes increased levels of misfolded proteins within the secretory compartment.

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Ca2+-ATPase function is required for intracellular trafficking of the Notch receptor in Drosophila

Cited by 56 publications

References 44 publications

A P _IIB -type Ca ²⁺ -ATPase is essential for stress adaptation in Physcomitrella patens

A P _IIB -type Ca ²⁺ -ATPase is essential for stress adaptation in Physcomitrella patens

Darier’s disease: a calcium-signaling perspective

Protein trafficking abnormalities inDrosophilatissues with impaired activity of the ZIP7 zinc transporter Catsup

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Ca2+-ATPase function is required for intracellular trafficking of the Notch receptor in Drosophila

Cited by 56 publications

References 44 publications

A P IIB -type Ca 2+ -ATPase is essential for stress adaptation in Physcomitrella patens

A P IIB -type Ca 2+ -ATPase is essential for stress adaptation in Physcomitrella patens

Darier’s disease: a calcium-signaling perspective

Protein trafficking abnormalities inDrosophilatissues with impaired activity of the ZIP7 zinc transporter Catsup

Contact Info

Product

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A P _IIB -type Ca ²⁺ -ATPase is essential for stress adaptation in Physcomitrella patens

A P _IIB -type Ca ²⁺ -ATPase is essential for stress adaptation in Physcomitrella patens