Homodimerization and intermolecular tyrosine phosphorylation of the Tyk‐2 tyrosine kinase

doi:10.1016/0014-5793(95)01094-u

Cited by 7 publications

(3 citation statements)

References 30 publications

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“…We hypothesize that not only the transmembrane receptor chains but also Jak1, Tyk2 and also RACK-1 need be present in comparable levels for full receptor activity to be observed. Notably, it has been shown that Janus kinases such as Tyk2 and Jak1 interact independantly of receptor activation [42]. A structural model encompassing these requirements is shown in Fig.…”

Section: Discussionmentioning

confidence: 99%

Ligand-independent interaction of the type I interferon receptor complex is necessary to observe its biological activity

Krause¹,

DiGioia²,

Izotova³

et al. 2013

Cytokine

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Ectopic coexpression of the two chains of the Type I and Type III interferon (IFN) receptor complexes (IFN-αR1 and IFN-αR2c, or IFN-λR1 and IL-10R2) yielded sensitivity to IFN-alpha or IFN-lambda in only some cells. We found that IFN-αR1 and IFN-αR2c exhibit FRET only when expressed at equivalent and low levels. Expanded clonal cell lines expressing both IFN-αR1 and IFN-αR2c were sensitive to IFN-alpha only when IFN-αR1 and IFN-αR2c exhibited FRET in the absence of human IFN-alpha. Coexpression of RACK-1 or Jak1 enhanced the affinity of the interaction between IFN-αR1 and IFN-αR2c. Both IFN-αR1 and IFN-αR2c exhibited FRET with Jak1 and Tyk2. Together with data showing that disruption of the preassociation between the IFN-gamma receptor chains inhibited its biological activity, we propose that biologically active IFN receptors require ligand-independent juxtaposition of IFN receptor chains assisted by their associated cytosolic proteins.

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Section: Discussionmentioning

confidence: 99%

Ligand-independent interaction of the type I interferon receptor complex is necessary to observe its biological activity

Krause¹,

DiGioia²,

Izotova³

et al. 2013

Cytokine

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“…We also evaluated JAK1 interaction partners using JAK1 as the query protein. In this case, the majority of proteins related to JAK1 were kinases, including TYK2 and SYK, which have been demonstrated to interact with JAK1 [ 23 , 24 ]. The most common transcription factor family was the STAT family, which are well-proven substrates for JAK1; STAT1 and STAT5b were the most frequent JAK1 partners in the 4 analyzed datasets [ 25 ] (Additional file 1 : Supplementary material S3).…”

Section: Resultsmentioning

confidence: 99%

MSCA: a spectral comparison algorithm between time series to identify protein-protein interactions

Arenas

Echeverry²,

Montoya³

et al. 2015

BMC Bioinformatics

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BackgroundThe interactions between pathogen proteins and their hosts allow pathogens to manipulate host cellular mechanisms to their advantage. The identification of host proteins that are targeted by virulent pathogen proteins is crucial to increase our understanding of infection mechanisms and to propose new therapeutics that target pathogens. Understanding the virulence mechanisms of pathogens requires a detailed molecular description of the proteins involved, but acquiring this knowledge is time consuming and prohibitively expensive. Therefore, we develop a statistical method based on hypothesis testing to compare the time series obtained from conversion of the physicochemical characteristics of the amino acids that form the primary structure of proteins and thus to propose potential functional relation between proteins. We called this algorithm the multiple spectral comparison algorithm (MSCA); the MSCA was inspired by the BLASTP tool and was implemented in R code. The algorithm compares and relates multiple time series according to their spectral similarities, and the biological relation between them could be interpreted as either a similar function or protein-protein interaction (PPI).ResultsA simulation study showed that the MSCA works satisfactorily well when we compare unequal time series generated from ARMA processes because its power was close to 1. The MSCA presented a 70% average accuracy of detecting protein interactions using a threshold of 0.7 for our spectral measure, indicating that this algorithm could predict novel PPIs and pathogen-host interactions (PHIs) with acceptable confidence. The MSCA also was validated by its identification of well-known interactions of the human proteins MAGI1, SCRIB and JAK1, as well as interactions of the virulence proteins ROP16, ROP18, ROP17 and ROP5. We verified the spectral similarities for human intraspecific PPIs and PHIs that were previously demonstrated experimentally by other authors. We suggest that human GBP (GTPase group induced by interferon) and the CREB transcription factor family could be human substrates for the complex of ROP18, ROP17 and ROP5.ConclusionsUsing multiple-hypothesis testing between the spectral densities of a set of unequal time series, we developed an algorithm that is able to identify the similarities or interactions between a set of proteins.Electronic supplementary materialThe online version of this article (doi:10.1186/s12859-015-0599-8) contains supplementary material, which is available to authorized users.

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“…We expressed V, W, GFP and GFP–Vs in 293FT cells along with FLAG-tagged Jak1 or Tyk2, and looked at interactions between these proteins by two assays: (1) the ability of the viral protein to co-precipitate Jak1 or Tyk2, and (2) the ability of the viral protein to block the autophosphorylation observed when either of these kinases is overexpressed, either transiently or as a transgene. This latter activity can be taken as a model of the ability of a protein to block IFN-stimulated activation of the kinase (Chinnakannan et al , 2013; Domanski et al , 1995; Eilers et al , 1996; Quelle et al , 1995; Valmas et al , 2010). We found that, like the complete V protein, GFP–Vs co-precipitated both receptor-associated kinases, whilst the W domain precipitated neither (Fig.…”

Section: Resultsmentioning

confidence: 99%

Different functions of the common P/V/W and V-specific domains of rinderpest virus V protein in blocking IFN signalling

Chinnakannan

Holzer

Bernardo

et al. 2014

Journal of General Virology

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The V proteins of paramyxoviruses are composed of two evolutionarily distinct domains, the N-terminal 75 % being common to the viral P, V and W proteins, and not highly conserved between viruses, whilst the remaining 25 % consists of a cysteine-rich V-specific domain, which is conserved across almost all paramyxoviruses. There is evidence supporting a number of different functions of the V proteins of morbilliviruses in blocking the signalling pathways of type I and II IFNs, but it is not clear which domains of V are responsible for which activities and whether all these activities are required for effective blockade of IFN signalling. We have shown here that the two domains of rinderpest virus V protein have distinct functions: the N-terminal domain acted to bind STAT1, whilst the C-terminal V-specific domain interacted with the IFN receptor-associated kinases Jak1 and Tyk2. Effective blockade of IFN signalling required the intact V protein.

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Homodimerization and intermolecular tyrosine phosphorylation of the Tyk‐2 tyrosine kinase

Cited by 7 publications

References 30 publications

Ligand-independent interaction of the type I interferon receptor complex is necessary to observe its biological activity

Ligand-independent interaction of the type I interferon receptor complex is necessary to observe its biological activity

MSCA: a spectral comparison algorithm between time series to identify protein-protein interactions

Different functions of the common P/V/W and V-specific domains of rinderpest virus V protein in blocking IFN signalling

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