Nuclear localization of Formyl-Peptide Receptor 2 in human cancer cells

Cattaneo, Fabio; Parisi, Melania; Fioretti, Tiziana; Sarnataro, Daniela; Esposito, Gabriella; Ammendola, Rosario

doi:10.1016/j.abb.2016.05.006

Cited by 29 publications

(36 citation statements)

References 62 publications

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Section: Formyl-peptide Receptorsmentioning

confidence: 99%

“…In both compartments MAPK signal transduction system is regulated by serine/threonine phosphorylation. In isolated intact CaLu-6 and AGS nuclei stimulated with WKYMVm, a time-dependent phosphorylation of nuclear p42MAPK, but not of p44MAPK, is observed, which is prevented by preincubation with a FPR2 antagonist (Table 1) [74].…”

Section: Formyl-peptide Receptorsmentioning

confidence: 99%

“…In fact, FPR2, but not FPR1 and FPR3, is expressed in nuclei isolated from human lung carcinoma CaLu-6 and human gastric adenocarcinoma AGS cell lines, as demonstrated by western blot analysis, immunofluorescence experiments and radioligand binding assays [74]. Furthermore, in AGS cells stably transfected with a short hairpin RNA targeting FPR2 (AGS shFPR2), nuclear FPR2 expression is significantly reduced [74]. FPR2 sequence has been analyzed for the search of NLS by using cNLS mapper program (http://nls-mapper.iab.keio.ac.jp) [75] and the results show a stretch of basic aminoacids (227-KIHKK-231) in the third cytoplasmic loop of the receptor (Table 2).…”

Section: Formyl-peptide Receptorsmentioning

confidence: 99%

“…Nuclear FPR2 is a functional receptor and can respond to a specific agonist (WKYMVm), since it participates in intra-nuclear Signaling, as assessed by decreased Gi protein-FPR2 association upon stimulation of intact nuclei from CaLu-6 and AGS cells with WKYMVm [74]. Effectors associated with post G protein GPCR signaling, including mitogen-activated protein kinase (MAPK) pathway, are also present in the nucleus and p42MAPK and p44MAPK are nuclear and cytoplasmic protein kinases.…”

Section: Formyl-peptide Receptorsmentioning

confidence: 99%

“…Additionally, a HomoloGene/ NCBI database search for the NLS within FPR2 reveals that the KIHKK sequence has been conserved among species. K230 and K231 are replaced by the basic residues RR in mouse and rat [74].…”

Section: Formyl-peptide Receptorsmentioning

confidence: 99%

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Intranuclear Signaling Cascades Triggered by Nuclear GPCRs

Cattaneo¹,

Parisi²,

Fioretti³

et al. 2016

J Cell Signal

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G protein-couped receptors (GPCRs) play a key role on cellular membranes, where they respond to a broad array of extracellular signals such as lipids, peptides, proteins and sensory agents. Intracellular biological responses triggered by these receptors include hormone secretion, muscle contraction, cellular metabolism a tyrosine kinase receptors transactivation. Recent results indicate that GPCRs localize to and signal also at nuclear level, thus regulating distinct signaling pathways which can also result from the integration of extracellular and intracellular stimuli. Nuclear GPCRs play a central role in many cellular processes, including regulation of gene transcription, cellular proliferation, neovascularization and RNA synthesis. On nuclear membranes and in nucleoplasm are present all the downstream signal transduction components of GPCRs, including G proteins, adenylyl cyclase, and second messengers such as Ca ++ , ERKs, p38MAPK and other protein kinases. Nuclear GPCRs may be constitutively active or may be activated by ligands internalized from the extracellular space or synthesized within the cell. The translocation of membrane receptors to the nucleus could be attributed to the presence of a Nuclear Localization Signal, which is present in the eighth helix or in the third intracellular loop of a limited number of GPCRs. However, several sequence motifs that do not resemble classical Nuclear Localization Signals can promote import of GPCRs. In this review we discuss the most recent results on nuclear localization and signaling of several GPCRS.

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Section: Formyl-peptide Receptorsmentioning

confidence: 99%

Section: Formyl-peptide Receptorsmentioning

confidence: 99%

Section: Formyl-peptide Receptorsmentioning

confidence: 99%

Section: Formyl-peptide Receptorsmentioning

confidence: 99%

Section: Formyl-peptide Receptorsmentioning

confidence: 99%

See 3 more Smart Citations

Intranuclear Signaling Cascades Triggered by Nuclear GPCRs

Cattaneo¹,

Parisi²,

Fioretti³

et al. 2016

J Cell Signal

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GPCR Signaling from Intracellular Membranes

Jong¹,

Harmon²,

O’Malley³

2022

GPCRs as Therapeutic Targets

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Formyl Peptide Receptors in Cellular Differentiation and Inflammatory Diseases

Lee

Bae

2017

J of Cellular Biochemistry

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Formyl peptide receptors (FPRs) are a family of classical chemoattractant receptors. Although FPRs are mainly expressed in phagocytic innate immune cells including monocytes/macrophages and neutrophils, recent reports demonstrated that additional different cell types such as T-lymphocytes and several non-immune cells also express functional FPRs. FPRs were first reported as a specific receptor to detect bacteria-derived N-formyl peptides. However, accumulating evidence has shown that FPRs can recognize various ligands derived from pathogens, mitochondria, and host. This review summarizes studies on some interesting endogenous agonists for FPRs. Here, we discuss functional roles of FPRs and their ligands concerning the regulation of cellular differentiation focusing on myeloid lineage cells. Accumulating evidence also suggests that FPRs may contribute to the control of inflammatory diseases. Here, we briefly review the current understanding of the functional role of FPRs and their ligands in inflammatory disorders in some animal disease models. J. Cell. Biochem. 118: 1300-1307, 2017. © 2017 Wiley Periodicals, Inc.

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Nuclear localization of Formyl-Peptide Receptor 2 in human cancer cells

Cited by 29 publications

References 62 publications

Intranuclear Signaling Cascades Triggered by Nuclear GPCRs

Intranuclear Signaling Cascades Triggered by Nuclear GPCRs

GPCR Signaling from Intracellular Membranes

Formyl Peptide Receptors in Cellular Differentiation and Inflammatory Diseases

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