Proteomics

Dataset Information

0

Autophosphorylation of Entamoeba histolytica atypical kinase EhAK1


ABSTRACT: Phagocytosis plays a key role in survival and pathogenicity of Entamoeba histolytica. We have recently demonstrated that an atypical kinase EhAK1 is involved in phagocytosis in this parasite. It is recruited to the phagocytic cups through interaction with EhCaBP1. EhAK1 manipulates actin dynamics by multiple mechanisms including phosphorylation of G-actin. Biochemical analysis showed that EhAK1 is a serine/threonine kinase with broad ion specificity and undergoes multiple trans-autophosphorylation. Multiple autophosphorylation sites were identified by mass spectrometry. Out of these Thr279 appears to be involved in both autophosphorylation as well as substrate phosphorylation.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Entamoeba Histolytica Hm-1:imss-a

SUBMITTER: gagan jhingan  

LAB HEAD: ALOK BHATTACHARYA

PROVIDER: PXD002691 | Pride | 2018-10-24

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
AKkinase.msf Msf
AKkinase.pep.xml Pepxml
AKkinase.raw Raw
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Publications

Autophosphorylation at Thr279 of Entamoeba histolytica atypical kinase EhAK1 is required for activity and regulation of erythrophagocytosis.

Mansuri M Shahid MS   Babuta Mrigya M   Ali Mohammad Sabir MS   Bharadwaj Ravi R   Deep jhingan Gagan G   Gourinath Samudrala S   Bhattacharya Sudha S   Bhattacharya Alok A  

Scientific reports 20160107


Phagocytosis plays a key role in survival and pathogenicity of Entamoeba histolytica. We have recently demonstrated that an atypical kinase EhAK1 is involved in phagocytosis in this parasite. It is recruited to the phagocytic cups through interaction with EhCaBP1. EhAK1 manipulates actin dynamics by multiple mechanisms including phosphorylation of G-actin. Biochemical analysis showed that EhAK1 is a serine/threonine kinase with broad ion specificity and undergoes multiple trans-autophosphorylati  ...[more]

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