Protein Ser/Thr phosphatases PPEF interact with calmodulin

Kutuzov, Mikhail A.; Soloveva, O. V.; Андреева, А. В.; Bennett, Nelly

doi:10.1016/s0006-291x(02)00338-8

Cited by 17 publications

(11 citation statements)

References 23 publications

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“…Ppef2 is a serine/threonine-protein phosphatase known to interact with calmodulin via its N-terminus. 30 Ppef2 is also linked to the control of cytokine production in response to LPS 31 but has at present no known role in DC biology. Pftk1 encodes the cyclin-dependent kinase-14, but its function is at present unclear.…”

Section: Discussionmentioning

confidence: 99%

Comparative promoter analysis in vivo: identification of a dendritic cell-specific promoter module

Edelmann

Nelson

Brocker

2011

Blood

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Dendritic cells (DCs) are important immune cells. This study focused on transcriptional networks active in murine DCs, but DCs are difficult to study using conventional molecular techniques. Therefore, comparative promoter analysis was used to identify evolutionarily conserved features between the murine CD11c and DC-STAMP promoters. A promoter framework consisting of 4 transcription factor binding sites was identified that included signal transducer and activator of transcription, homeodomain transcription factors, and 2 members of the Brn POU domain factors family. This promoter module was functionally verified by in vivo promoter analysis and site-directed mutagenesis. Hematopoietic stem cells were engineered by lentiviral vectors and expression of green fluorescent protein reporter was monitored in primary hematopoietic cell types that develop without further manipulation in irradiated recipient mice. The verified promoter module was then modeled and used in a bioinformatics-based search for other potential coregulated genes in murine DCs. A promoter database search identified 2 additional genes, Ppef2 and Pftk1, which have a similar promoter organization and are preferentially expressed in murine DCs. The results define a regulatory network linked to development of murine DCs. (Blood. 2011;118(11):e40-e49) IntroductionDendritic cells (DCs) play key roles in shaping the immune response. 1,2 They are highly specialized in uptake and presentation of antigen. In their steady state, DCs migrate from peripheral tissues to the draining lymph node and present self-antigen to naive T cells, inducing tolerance. On encounter of pathogen, DCs change their phenotype (undergo maturation), which leads to a more pronounced migratory behavior and an increase in stimulatory capacity. 3 Plasticity is a pervasive feature of DC biology. DC subsets from different tissues show differential morphology, phenotypes, and functions. An additional distinction can also be made between conventional DCs (cDCs) and plasmacytoid DCs (pDCs), which are mainly involved in viral immune responses. cDCs also include a subset (CD8 ϩ in mice) specialized in antigen cross-presentation. 4 Networks of genes linked by common control mechanisms may help orchestrate homeostasis, as well as the response of DCs to external stimuli. The prediction and analysis of these networks represent a major challenge in understanding immunology. Transcriptional mechanisms have been very difficult to study in DCs because of their propensity to quickly change phenotypes in response to physical manipulation and their limited numbers. Gene expression is controlled by a series of processes that include locus control regions, chromatin rearrangement, methylation, gene enhancers, etc. These regulatory events ultimately end at the promoter level to effect gene transcription. Promoters integrate this information to achieve the tissue and signal specific control of gene expression required for complex biologic processes, such as DC biology and function.Within promoters, transcri...

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Section: Discussionmentioning

confidence: 99%

Comparative promoter analysis in vivo: identification of a dendritic cell-specific promoter module

Edelmann

Nelson

Brocker

2011

Blood

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“…PPEF2 encodes a neuronally expressed protein phosphatase that binds calmodulin. 32 Given that mGluR5 and PPEF2 both bind calmodulin, we tested whether PPEF2 expression influences mGluR5 levels. HEK293 cells transfected with PPEF2 demonstrated increased levels of mGluR5 in the presence of the mGluR5 agonist (Figure 4), suggesting that disturbance of PPEF2 could lower mGluR5 membrane levels.…”

Section: Functional Evaluation Of Mglur5 and Ppef2mentioning

confidence: 99%

Support for the N -Methyl-D-Aspartate Receptor Hypofunction Hypothesis of Schizophrenia From Exome Sequencing in Multiplex Families

Timms¹,

Dorschner²,

Wechsler³

et al. 2013

JAMA Psychiatry

122

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“…A calmodulin-binding site of the IQ type [28] conserved in PPEFs was predicted [19] and confirmed experimentally for Drosophila and human PPEFs [29,30]. IQ motifs are conserved in PPEFs from all eukaryotes, with two exceptions: (1) in kinetoplastids, it is replaced by a domain containing Zn finger motifs [4], and (2) in a dinoflagellate Karenia brevis, the N-terminal domain shows no significant similarity to any other proteins.…”

Section: Introductionmentioning

confidence: 89%

“…Calmodulin binding to rdgC increases its phosphatase activity and is essential for rhodopsin dephosphorylation in vivo [29]. Although the ability of the IQ motifs of human PPEF1 and PPEF2 to bind calmodulin in vitro has been demonstrated [30], calmodulin reportedly has no effect on phosphatase activity of recombinant human PPEF1 [22]. PPEF1 activity requires Mg 2?…”

Section: Ppef Regulationmentioning

confidence: 99%

PPEF/PP7 protein Ser/Thr phosphatases

Андреева

Kutuzov

2009

Cell. Mol. Life Sci.

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PPEF/PP7 represents one of the five subfamilies of the PPP protein Ser/Thr phosphatases. Studies published in recent years point to a role of plant PP7 at a crossroad of different pathways of light and stress signalling. In animals, PPEFs are highly expressed in sensory neurons, and Drosophila PPEF phosphatase, rdgC, is essential for dephosphorylation of rhodopsin. Expression profiling suggests that mammalian PPEF may play a role in stress-protective responses, cell survival, growth, proliferation, and oncogenesis. Despite structural similarities of the catalytic domains and the fact that some of these phosphatases are involved in light perception both in animals and in plants, the plant and non-plant representatives of this group have distinct domain architecture and appear not to be orthologues.

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Protein Ser/Thr phosphatases PPEF interact with calmodulin

Cited by 17 publications

References 23 publications

Comparative promoter analysis in vivo: identification of a dendritic cell-specific promoter module

Comparative promoter analysis in vivo: identification of a dendritic cell-specific promoter module

Support for the N -Methyl-D-Aspartate Receptor Hypofunction Hypothesis of Schizophrenia From Exome Sequencing in Multiplex Families

PPEF/PP7 protein Ser/Thr phosphatases

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