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

Autor: Isabel Ayala, Pierre Gans, Jean-Baptiste Reiser, Marion Sévajol, Philippe Frachet, Jean-Philippe Kleman, Rida Awad, Anne Chouquet
Přispěvatelé: Institut de biologie structurale (IBS - UMR 5075 ), Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Plateforme Grenoble Instruct center cell imaging and flow cytometry facility (M4D), High Field NMR, ANR-10-INBS-0005,FRISBI,Infrastructure Française pour la Biologie Structurale Intégrée(2010), ANR-10-LABX-0049,GRAL,Grenoble Alliance for Integrated Structural Cell Biology(2010), Thomas, Frank, Infrastructure Française pour la Biologie Structurale Intégrée - - FRISBI2010 - ANR-10-INBS-0005 - INBS - VALID, Grenoble Alliance for Integrated Structural Cell Biology - - GRAL2010 - ANR-10-LABX-0049 - LABX - VALID, Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)
Jazyk: angličtina
Rok vydání: 2015
Předmět:
SH3
Src Homology 3 domain
GSH
Glutathione (reduced)
PxP
Polyproline motif
Dock180
[SDV.BBM.BS] Life Sciences [q-bio]/Biochemistry
Molecular Biology/Structural Biology [q-bio.BM]
QH301-705.5
EID
ELMO Inhibitory Domain
Biology
PH
Pleckstrin Homology domain
General Biochemistry
Genetics and Molecular Biology
SH3 domain
Article
Adapter molecule crk
Phagocytosis
DOCK
Downstream Of CrK protein family
TAMs
Tyro3
Axl and Mer receptor tyrosine kinase family
Kinase activity
Biology (General)
Phosphorylation
ELMO
EnguLfment and cell MOtility protein family
ERM
Ezrin–Radixin–Moesin protein family
ELMO
Tyrosine-protein kinase CSK
Hck
[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry
Molecular Biology/Structural Biology [q-bio.BM]
FRET
Förster (Fluorescence) resonance energy transfer
Actin remodeling
Polyproline
GST
Glutathione S-Transferase
Cell biology
SH3
ELMO1
Biochemistry
GEF
Guanine nucleotide Exchange Factor
RBD
Rho-Binding Domain
TEV
Tobacco Etch Virus
Hck
Hematopoietic cell kinase
EAD
ELMO Autoregulatory Domain
Proto-oncogene tyrosine-protein kinase Src
Zdroj: FEBS Open Bio
FEBS Open Bio, Wiley Open Access/Elsevier, 2015, 5, pp.99-106
HAL
FEBS Open Bio, Vol 5, Iss 1, Pp 99-106 (2015)
FEBS Open Bio, 2015, 5, pp.99-106
ISSN: 2211-5463
Popis: Highlights • We determine the mode of interaction between ELMO1 and Hck with direct methods. • The SH3 domain of Hck interacts specifically with the polyproline motif of ELMO1. • ELMO1 polyproline affinity for the SH3 of Hck is modulated by Tyr-phosphorylation.
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 a putative modulator of Hck kinase activity towards ELMO1 that in turn participates in DOCK180 activation and further triggers subsequent signaling towards actin remodeling.
Databáze: OpenAIRE
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