Kinase Family RIPK

Kinase Classification: Group TKL: Family RIPK

[This article is a stub]

Receptor Interacting Protein Kinases (RIPK) interact with TNF and other death receptors and transduce their signals.

Evolution

RIPK are clearly found in vertebrates and other chordates [1]. Arthropods appear to have a RIPK1 homolog that has lost the kinase domain (e.g. imd in Drosophila) and mollusks such as Crassostrea gigas also have a likely RIPK gene.

Domain Structure

All vertebrate RIPK have an N-terminal TKL kinase domain, and a long C-terminal extension that contains one of several interaction domains. RIPK1 has a death domain and an RHIM motif. RIPK has the RHIM but no death domain, and RIPK2 has a CARD domain, which is related to the death domain. SgK288 and RIPK4 (ANKRD3) both have an array of ankyrin repeats.

Invertebrate RIPKs have more divergent domain architectures. Arthopods have the imd (immune defective) protein that has a RIPK-like death domain but has no kinase domain, while urchin and lancelet homologs have Leucine Rich Repeats or Ankyrin repeat that are N-terminal of the kinase domain.

References

1. Manning G, Young SL, Miller WT, and Zhai Y. The protist, Monosiga brevicollis, has a tyrosine kinase signaling network more elaborate and diverse than found in any known metazoan. Proc Natl Acad Sci U S A. 2008 Jul 15;105(28):9674-9. DOI:10.1073/pnas.0801314105 |