| http://purl.uniprot.org/citations/21378159 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/21378159 | http://www.w3.org/2000/01/rdf-schema#comment | "Phospholipase D (PLD) and small GTPases are vital to cell signaling. We report that the Rac2 and the PLD2 isoforms exist in the cell as a lipase-GTPase complex that enables the two proteins to elicit their respective functionalities. A strong association between the two molecules was demonstrated by co-immunoprecipitation and was confirmed in living cells by FRET with CFP-Rac2 and YFP-PLD2 fluorescent chimeras. We have identified the amino acids in PLD2 that define a specific binding site to Rac2. This site is composed of two CRIB (Cdc42-and Rac-interactive binding) motifs that we have named "CRIB-1" and "CRIB-2" in and around the PH domain in PLD2. Deletion mutants PLD2-ΔCRIB-1/2 negate co-immunoprecipitation with Rac2 and diminish the FRET signal in living cells. The PLD2-Rac2 association was further confirmed in vitro using affinity-purified recombinant proteins. Binding was saturable with an apparent K(d) of 3 nm and was diminished with PLD2-ΔCRIB mutants. Furthermore, PLD2 bound more efficiently to Rac2-GTP than to Rac2-GDP or to a GDP-constitutive Rac2-N17 mutant. Increasing concentrations of recombinant Rac2 in vitro and in vivo during cell adhesion inhibit PLD2. Conversely, Rac2 activity is increased in the presence of PLD2-WT but not in PLD2-ΔCRIB. We propose that in activated cells PLD2 affects Rac2 in an initial positive feedback, but as Rac2-GTP accumulates in the cell, this constitutes a "termination signal" leading to PLD2 inactivation."xsd:string |
| http://purl.uniprot.org/citations/21378159 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m110.206672"xsd:string |
| http://purl.uniprot.org/citations/21378159 | http://purl.uniprot.org/core/author | "Peng H.J."xsd:string |
| http://purl.uniprot.org/citations/21378159 | http://purl.uniprot.org/core/author | "Dinauer M.C."xsd:string |
| http://purl.uniprot.org/citations/21378159 | http://purl.uniprot.org/core/author | "Gomez-Cambronero J."xsd:string |
| http://purl.uniprot.org/citations/21378159 | http://purl.uniprot.org/core/author | "Henkels K.M."xsd:string |
| http://purl.uniprot.org/citations/21378159 | http://purl.uniprot.org/core/author | "Mahankali M."xsd:string |
| http://purl.uniprot.org/citations/21378159 | http://purl.uniprot.org/core/date | "2011"xsd:gYear |
| http://purl.uniprot.org/citations/21378159 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/21378159 | http://purl.uniprot.org/core/pages | "16308-16320"xsd:string |
| http://purl.uniprot.org/citations/21378159 | http://purl.uniprot.org/core/title | "Evidence for two CRIB domains in phospholipase D2 (PLD2) that the enzyme uses to specifically bind to the small GTPase Rac2."xsd:string |
| http://purl.uniprot.org/citations/21378159 | http://purl.uniprot.org/core/volume | "286"xsd:string |
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