Receptor-interacting protein (RIP) kinase family

Zhang, Duanwu; Lin, Juan; Han, Jiahuai

doi:10.1038/cmi.2010.10

Cited by 169 publications

(203 citation statements)

References 84 publications

(110 reference statements)

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“…Bivalve sequences have been identified by BLAST due to their DD similarity, but their clustering is not well supported due to low bootstrap values, even with IMD from arthropods, an homologue of vertebrate RIP, which also do not contain the kinase domain. Only RIP1 and RIP2 out of the 7 members of the human RIP protein family have a C-terminal DD (Zhang et al, 2010), but all of them contained one kinase domain. Consequently, we suggested to named the Mytilus sequences, MgRIP-like and MeRIP-like.…”

Section: Resultsmentioning

confidence: 99%

Toll signal transduction pathway in bivalves: Complete cds of intermediate elements and related gene transcription levels in hemocytes of immune stimulated Mytilus galloprovincialis

Toubiana

Rosani

Giambelluca

et al. 2014

Developmental & Comparative Immunology

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a b s t r a c tBased on protein domain structure and organization deduced from mRNA contigs, 15 transcripts of the Toll signaling pathway have been identified in the bivalve, Mytilus galloprovincialis. Identical searches performed on publicly available Mytilus edulis ESTs revealed 11 transcripts, whereas searches performed in genomic and new transcriptome sequences of the Pacific oyster, Crassostrea gigas, identified 21 Toll-related transcripts. The remarkable molecular diversity of TRAF and IKK coding sequences of C. gigas, suggests that the sequence data inferred from Mytilus cDNAs may not be exhaustive. Most of the Toll pathway genes were constitutively and ubiquitously expressed in M. galloprovincialis, although at different levels, and clearly induced after in vivo injection with bacteria. Such over-transcription was more rapid and intense with Gram-negative than with Gram-positive bacteria. Injection of a fungus modulated the transcription of few Toll pathway genes, with the induction levels of TLR/MyD88 complex being always less intense. Purified LPS and b-glucans had marginal effect whereas peptidoglycans were ineffective. At the moment, we found no evidence of an IMD transcript in bivalves. In conclusion, mussels possess a complete Toll pathway which can be triggered either by Gram-positive or Gram-negative bacteria.

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Section: Resultsmentioning

confidence: 99%

Toll signal transduction pathway in bivalves: Complete cds of intermediate elements and related gene transcription levels in hemocytes of immune stimulated Mytilus galloprovincialis

Toubiana

Rosani

Giambelluca

et al. 2014

Developmental & Comparative Immunology

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“…7 In addition to its N-terminal KD, RIP1 contains a C-terminal death domain (DD) and a bridging intermediate domain (ID) that also harbours a RIP homotypic interaction motif (RHIM). RIP2 also contains the N-terminal KD, an ID (lacking a RHIM) and a C-terminal caspase activation and recruitment domain (CARD).…”

Section: The Rip Kinase Familymentioning

confidence: 99%

“…The functions of RIP 4-7 are poorly understood and are well reviewed elsewhere. 7 Briefly, RIP4 was initially identified as a PKCd-interacting protein 8 and was subsequently shown to activate NFkB. 9 It has a key role in keratinocyte differentiation 10 and cutaneous inflammation.…”

Section: The Rip Kinase Familymentioning

confidence: 99%

RIP kinases: key decision makers in cell death and innate immunity

et al. 2014

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“…[3][4][5] RIPK4 is a member of the RIP serine/threonine kinase family, which act as integrators of stress signals leading to the activation of NF-κB, MAP kinases, cell death or inflammation. 6,7 All RIPKs contain a homologous kinase domain but have different protein-protein interaction domains allowing them to function in different pathways. RIPK4 consists of an N-terminal kinase domain, an intermediate domain and a C-terminus containing 11 ankyrin repeats.…”

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confidence: 99%

A novel RIPK4–IRF6 connection is required to prevent epithelial fusions characteristic for popliteal pterygium syndromes

et al. 2014

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Receptor-interacting protein kinase 4 (RIPK4)-deficient mice have epidermal defects and fusion of all external orifices. These are similar to Bartsocas-Papas syndrome and popliteal pterygium syndrome (PPS) in humans, for which causative mutations have been documented in the RIPK4 and IRF6 (interferon regulatory factor 6) gene, respectively. Although genetically distinct, these syndromes share the anomalies of marked pterygia, syndactyly, clefting and hypoplastic genitalia. Despite the strong resemblance of these two syndromes, no molecular connection between the transcription factor IRF6 and the kinase RIPK4 was known and the mechanism underlying the phenotype was unclear. Here we describe that RIPK4 deficiency in mice causes epithelial fusions associated with abnormal periderm development and aberrant ectopic localization of E-cadherin on the apical membrane of the outer peridermal cell layers. In Xenopus, RIPK4 depletion causes the absence of ectodermal epiboly and concomitant gastrulation defects that phenocopy ectopic expression of dominant-negative IRF6. We found that IRF6 controls RIPK4 expression and that wild-type, but not kinase-dead, RIPK4 can complement the gastrulation defect in Xenopus caused by IRF6 malfunctioning. In contrast to the mouse, we observed only minor effects on cadherin membrane expression in Xenopus RIPK4 morphants. However, gastrulation defects were associated with a virtual absence of cortical actin in the ectodermal cells that face the blastocoel cavity and this was phenocopied in embryos expressing dominant-negative IRF6. A role for RIPK4 in actin cytoskeleton organization was also revealed in mouse epidermis and in human epithelial HaCaT cells. In conclusion, we showed that in mice RIPK4 is implicated in cortical actin organization and in E-cadherin localization or function, which can explain the characteristic epithelial fusions observed in PPSs. In addition, we provide a novel molecular link between IRF6 and RIPK4 that unifies the different PPSs to a common molecular pathway.

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Receptor-interacting protein (RIP) kinase family

Cited by 169 publications

References 84 publications

Toll signal transduction pathway in bivalves: Complete cds of intermediate elements and related gene transcription levels in hemocytes of immune stimulated Mytilus galloprovincialis

Toll signal transduction pathway in bivalves: Complete cds of intermediate elements and related gene transcription levels in hemocytes of immune stimulated Mytilus galloprovincialis

RIP kinases: key decision makers in cell death and innate immunity

A novel RIPK4–IRF6 connection is required to prevent epithelial fusions characteristic for popliteal pterygium syndromes

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