Literature DB >> 31758832

Subcellular localization of Rap1 GTPase activator CalDAG-GEFI is orchestrated by interaction of its atypical C1 domain with membrane phosphoinositides.

Muzaddid Sarker1, Ardeshir Goliaei1, Florence Golesi2, Marjorie Poggi2, Aaron A Cook1, Mohammad A I Khan1, Brenda R Temple1,3, Lucia Stefanini4, Matthias Canault2, Wolfgang Bergmeier1,5, Sharon L Campbell1,5.   

Abstract

BACKGROUND: The small GTPase Rap1 and its guanine nucleotide exchange factor, CalDAG-GEFI (CDGI), are critical for platelet function and hemostatic plug formation. CDGI function is regulated by a calcium binding EF hand regulatory domain and an atypical C1 domain with unknown function.
OBJECTIVE: Here, we investigated whether the C1 domain controls CDGI subcellular localization, both in vitro and in vivo.
METHODS: CDGI interaction with phosphoinositides was studied by lipid co-sedimentation assays and molecular dynamics simulations. Cellular localization of CDGI was studied in heterologous cells by immunofluorescence and subcellular fractionation assays.
RESULTS: Lipid co-sedimentation studies demonstrated that the CDGI C1 domain associates with membranes through exclusive recognition of phosphoinositides, phosphatidylinositol (4,5)-biphosphate (PIP2) and phosphatidylinositol (3,4,5)-triphosphate (PIP3). Molecular dynamics simulations identified a phospholipid recognition motif consisting of residues exclusive to the CDGI C1 domain. Mutation of those residues abolished co-sedimentation of the C1 domain with lipid vesicles and impaired membrane localization of CDGI in heterologous cells.
CONCLUSION: Our studies identify a novel interaction between an atypical C1 domain and phosphatidylinositol (4,5)-biphosphate and phosphatidylinositol (3,4,5)-triphosphate in cellular membranes, which is critical for Rap1 signaling in health and disease.
© 2019 International Society on Thrombosis and Haemostasis.

Entities:  

Keywords:  C1 domain; CalDAG-GEF; membrane; platelet; thrombosis

Mesh:

Substances:

Year:  2019        PMID: 31758832      PMCID: PMC7050387          DOI: 10.1111/jth.14687

Source DB:  PubMed          Journal:  J Thromb Haemost        ISSN: 1538-7836            Impact factor:   5.824


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