Molecular and functional characterization of EhPAK3, a p21 activated kinase from Entamoeba histolytica

Dutta, Suman; Sardar, Anupama; Ray, Deepshikha; Raha, Sanghamitra

doi:10.1016/j.gene.2007.07.022

Cited by 9 publications

(9 citation statements)

References 35 publications

(50 reference statements)

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“…95 EhPAK3 is also expressed in trophozoites, and both recombinant EhPAK3 purified under denaturing conditions and EhPAK3 immunoprecipitated from amebic lysates exhibit apparent kinase activity. 96 …”

Section: Ras Superfamily Gtpases In E Histolyticamentioning

confidence: 99%

G protein signaling in the parasite Entamoeba histolytica

Bosch

Siderovski

2013

Exp Mol Med

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The parasite Entamoeba histolytica causes amebic colitis and systemic amebiasis. Among the known amebic factors contributing to pathogenesis are signaling pathways involving heterotrimeric and Ras superfamily G proteins. Here, we review the current knowledge of the roles of heterotrimeric G protein subunits, Ras, Rho and Rab GTPase families in E. histolytica pathogenesis, as well as of their downstream signaling effectors and nucleotide cycle regulators. Heterotrimeric G protein signaling likely modulates amebic motility and attachment to and killing of host cells, in part through activation of an RGS-RhoGEF (regulator of G protein signaling–Rho guanine nucleotide exchange factor) effector. Rho family GTPases, as well as RhoGEFs and Rho effectors (formins and p21-activated kinases) regulate the dynamic actin cytoskeleton of E. histolytica and associated pathogenesis-related cellular processes, such as migration, invasion, phagocytosis and evasion of the host immune response by surface receptor capping. A remarkably large family of 91 Rab GTPases has multiple roles in a complex amebic vesicular trafficking system required for phagocytosis and pinocytosis and secretion of known virulence factors, such as amebapores and cysteine proteases. Although much remains to be discovered, recent studies of G protein signaling in E. histolytica have enhanced our understanding of parasitic pathogenesis and have also highlighted possible targets for pharmacological manipulation.

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Section: Ras Superfamily Gtpases In E Histolyticamentioning

confidence: 99%

G protein signaling in the parasite Entamoeba histolytica

Bosch

Siderovski

2013

Exp Mol Med

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“…Moreover, the functional studies of EhPAK2 show that C terminal of the domain had activity toward the myelin basic protein (57). Another member EhPAK3 is a serine/threonine kinase which phosphorylates histone in vitro in absence of any small GTPase (58). So far only biochemical properties of these kinases are known but they have not been linked to cellular processes, more research on this kinase is required to establish the role of these kinases in amoebic biology.…”

Section: P21 Activated Kinase Family (Ehpak)mentioning

confidence: 99%

Role of kinases in virulence and pathogenesis of protozoan parasite i E Histolytica i

et al. 2020

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“…The kinase domains of the two putative PAK-like proteins (XP_652252 and XP_651577) have diverged from the conserved sequence. Only six putative PAKs have conserved CRIB domains however, it is uncertain if these and other amebic PAKs are regulated by small GTPases [62][63][64]. EhPAK1 possesses a kinase domain but lacks a CRIB domain.…”

Section: P21-activated Kinases (Paks)mentioning

confidence: 99%