The SH3 regulatory domain of the hematopoietic cell kinase Hck binds ELMO via its polyproline motif

FEBS Open Bio
Rida AwadJean-Philippe Kleman

Abstract

Eukaryotic EnguLfment and cell MOtility (ELMO) proteins form an evolutionary conserved family of regulators involved in small GTPase dependent actin remodeling processes that regulates the guanine exchange factor activity of some of the Downstream Of CrK (DOCK) family members. Gathered data strongly suggest that DOCK activation by ELMO and the subsequent signaling result from a subtle balance in the binding of partners to ELMO. Among its putative upward modulators, the Hematopoietic cell kinase (Hck), a member of the Src kinase superfamily, has been identified as a binding partner and a specific tyrosine kinase for ELMO1. Indeed, Hck is implicated in distinct molecular signaling pathways governing phagocytosis, cell adhesion, and migration of hematopoietic cells. Although ELMO1 has been shown to interact with the regulatory Src Homology 3 (SH3) domain of Hck, no direct evidence indicating the mode of interaction between Hck and ELMO1 have been provided in the literature. In the present study, we report convergent pieces of evidence that demonstrate the specific interaction between the SH3 domain of Hck and the polyproline motif of ELMO1. Our results also suggest that the tyrosine-phosphorylation state of ELMO1 tail might act as...Continue Reading

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Citations

Jul 25, 2015·Cell Communication and Signaling : CCS·Yoshinori MakinoShinya Tanaka
Apr 26, 2019·International Journal of Molecular Sciences·Katharine A MichiePaul M G Curmi

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Methods Mentioned

BETA
PCR
gel filtration
pull-down
electrophoresis
NMR
flow cytometry
FRET
flow

Software Mentioned

MACSQuantify
NmrViewJ
NMRPipe

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