Secondary literature sources for DEP
The following references were automatically generated.
- Lussier MP et al.
- MxA, a member of the dynamin superfamily, interacts with the ankyrin-likerepeat domain of TRPC.
- J Biol Chem. 2005; 280: 19393-400
- Display abstract
Mammalian transient receptor potential canonical channels have beenproposed as the molecular entities associated with calcium entry activityin nonexcitable cells. Amino acid sequence analyses of TRPCs revealed thepresence of ankyrin-like repeat domains, one of the most commonprotein-protein interaction motifs. Using a yeast two-hybrid interactionassay, we found that the second ankyrin-like repeat domain of TRPC6interacted with MxA, a member of the dynamin superfamily. Using a GSTpull-down and co-immunoprecipitation assay, we showed that MxA interactedwith TRPC1, -3, -4, -5, -6, and -7. Overexpression of MxA in HEK293T cellsslightly increased endogenous calcium entry subsequent to stimulation ofG(q) protein-coupled receptors or store depletion by thapsigargin.Co-expression of MxA with TRPC6 enhanced agonist-induced or OAG-inducedcalcium entry activity. GTP binding-defective MxA mutants had only a minorpotentiating effect on OAG-induced TRPC6 activity. However, a MxA mutantthat could bind GTP but that lacked GTPase activity produced the sameeffect as MxA on OAG-induced TRPC6 activity. These results indicated thatMxA interacted specifically with the second ankyrin-like repeat domain ofTRPCs and suggested that monomeric MxA regulated the activity of TRPC6 bya mechanism requiring GTP binding. Additional results showed that anincrease in the endogenous expression of MxA, induced by a treatment withinterferon alpha, regulated the activity of TRPC6. The study clearlyidentified MxA as a new regulatory protein involved in Ca2+ signaling.
- Cozier GE, Carlton J, Bouyoucef D, Cullen PJ
- Membrane targeting by pleckstrin homology domains.
- Curr Top Microbiol Immunol. 2004; 282: 49-88
- Display abstract
Pleckstrin homology (PH) domains are small modular domains that occur once, or occasionally several times, in a large variety of signalling proteins. In a number of instances, PH domains act to target their host protein to the cytosolic face of cellular membranes through an ability to associate with phosphoinositides. In this review, we discuss recent advances in our understanding of PH domain function. In particular we describe the structural aspects of how PH domains have evolved to bind various phosphoinositides, how PH domains regulate phosphoinositide-mediated association to plasma and internals membranes, and finally raise the issue of PH domains in protein:protein interactions and the allosteric regulation of their host protein.
- Hunt RA, Edris W, Chanda PK, Nieuwenhuijsen B, Young KH
- Snapin interacts with the N-terminus of regulator of G protein signaling7.
- Biochem Biophys Res Commun. 2003; 303: 594-9
- Display abstract
The N-terminus of regulator of G protein signaling 7 (RGS7) contains adishevelled/egl-10/pleckstrin (DEP) domain of unknown function. To gaininsight into its function, we used yeast two-hybrid analysis to screen ahuman whole brain cDNA library in order to identify proteins that interactspecifically with the N-terminus of human RGS7 (amino acid residues1-248). From this analysis, we identified snapin, a protein associatedwith the SNARE complex in neurons, as an interactor with the N-terminus ofRGS7. Deletion mutation analysis in yeast demonstrated that theinteraction between RGS7 and snapin is specific and is mediated primarilyby amino acid residues 1-69 of RGS7 (which contains the proximal portionof the DEP domain). The interaction between RGS7 and snapin was alsodemonstrated in mammalian cells by coimmunoprecipitation and pull-downassays. Our results suggest that RGS7 could play a role in synapticvesicle exocytosis through its interaction with snapin.
- Wang T, Dowal L, El-Maghrabi MR, Rebecchi M, Scarlata S
- The pleckstrin homology domain of phospholipase C-beta(2) links thebinding of gbetagamma to activation of the catalytic core.
- J Biol Chem. 2000; 275: 7466-9
- Display abstract
Pleckstrin homology (PH) domains are membrane tethering devices found inmany signal transducing proteins. These domains also couple to thebetagamma subunits of GTP binding proteins (G proteins), but whether thisassociation transmits allosteric information to the catalytic core isunclear. To address this question, we constructed protein chimeras inwhich the PH domain of phospholipase C-beta(2) (PLC-beta(2)), which isregulated by Gbetagamma, replaces the PH domain of PLC-delta(1) whichbinds to, but is not regulated by, Gbetagamma. We found that attachment ofthe PH domain of PLC-beta(2) onto PLC-delta(1) not only causes themembrane-binding properties of PLC-delta(1) to become similar to those ofPLC-beta(2), but also results in a Gbetagamma-regulated enzyme. Thus, PHdomains are more than simple tethering devices and mediate regulatorysignals to the host protein.
- Kasahara S, Wang P, Nuss DL
- Identification of bdm-1, a gene involved in G protein beta-subunitfunction and alpha-subunit accumulation.
- Proc Natl Acad Sci U S A. 2000; 97: 412-7
- Display abstract
Targeted disruption of Galpha and Gbeta genes has established therequirement of an intact G protein signaling pathway for optimal executionof several important physiological processes, including pathogenesis, inthe chestnut blight fungus Cryphonectria parasitica. We now report theidentification of a G protein signal transduction component, betadisruption mimic factor-1, BDM-1. Disruption of the corresponding gene,bdm-1, resulted in a phenotype indistinguishable from that previouslyobserved after disruption of the Gbeta subunit gene, cpgb-1. The BDM-1deduced amino acid sequence contained several significant clusters ofidentity with mammalian phosducin, including a domain corresponding to ahighly conserved 11-amino acid stretch that has been implicated in bindingto the Gbetagamma dimer and two regions of defined Gbeta/phosducin contactpoints. Unlike the negative regulatory function proposed for mammalianphosducin, the genetic data presented in this report suggest that BDM-1 isrequired for or facilitates Gbeta function. Moreover, disruption of eitherbdm-1 or cpgb-1 resulted in a significant, posttranscriptional reductionin the accumulation of CPG-1, a key Galpha subunit required for a range ofvital physiological processes.
