2014
DOI: 10.1111/tpj.12732
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Evidence for an unusual transmembrane configuration of AGG3, a class C Gγ subunit of Arabidopsis

Abstract: SUMMARY Heterotrimeric G proteins are crucial for the perception of external signals and subsequent signal transduction in animal and plant cells. In both model systems, the complex is comprised of one Gα, one Gβ and one Gγ subunit. However, in addition to the canonical Gγ subunits (Class A), plants also possess two unusual, plant-specific classes of Gγ subunits (Classes B and C) not yet found in animals. These include Gγ subunits lacking the C-terminal CaaX motif (Class B) which is important for membrane anch… Show more

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Cited by 35 publications
(38 citation statements)
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References 55 publications
(77 reference statements)
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“…However, because similar signals were detected when XLG2 was cotransfected with unfused nYFP, we conclude that XLG2 and AGB1 may not interact directly, but their interaction requires an AGG subunit. This conclusion is in agreement with a recently established fact that AGB1 protein could not be detected in mutant Arabidopsis plants lacking all three AGGs (Wolfenstetter et al, 2014), indicating that it is probably unstable unless engaged with at least one AGG subunit. Importantly, these interactions take place only at the plasma membrane, and not in the nucleus.…”
Section: Discussionsupporting
confidence: 92%
See 1 more Smart Citation
“…However, because similar signals were detected when XLG2 was cotransfected with unfused nYFP, we conclude that XLG2 and AGB1 may not interact directly, but their interaction requires an AGG subunit. This conclusion is in agreement with a recently established fact that AGB1 protein could not be detected in mutant Arabidopsis plants lacking all three AGGs (Wolfenstetter et al, 2014), indicating that it is probably unstable unless engaged with at least one AGG subunit. Importantly, these interactions take place only at the plasma membrane, and not in the nucleus.…”
Section: Discussionsupporting
confidence: 92%
“…Nevertheless, in all known defense-related functions, AGB1 forms a functional dimer with AGG1 or AGG2 Botella, 2000, 2001;Trusov et al, 2007;Delgado-Cerezo et al, 2012). Moreover, the double mutant agg1 agg2 has reduced steady-state levels of AGB1, while in the triple mutant, lacking all three Gg subunits, AGB1 abundance was even more severely decreased (Wolfenstetter et al, 2014). Therefore, we produced a quadruple mutant agg1 agg2 xlg2 xlg3 to analyze through disease resistance assays.…”
Section: And E)mentioning
confidence: 99%
“…Type B Gg subunits are similar to type A Gg subunits but lack the C-terminal CaaX motif, precluding the possibility of prenylation . Finally, type C Gg subunits have the conserved domain, a transmembrane domain, and a relatively long Cys-rich C-terminal end Wolfenstetter et al, 2015). A similar classification has been reported for soybean (Glycine max) Gg subunits (Choudhury et al, 2011).…”
supporting
confidence: 56%
“…The AGG3-specific COOH-terminal domain was predicted to contain a transmembrane domain followed by a tumor necrosis factor receptor/nerve growth factor receptor (TNFR/NGFR) family type of cysteine-rich signature, as well as four von Willebrand factor type C (VWFC) modules [7]. The initially suggested and recently experimentally proven presence [16] of a transmembrane domain and an extracellular cysteine-rich domain in the COOH-terminus of AGG3 led to the speculation that γ-subunits of the AGG3 type could function as receptors [17]. …”
Section: Introductionmentioning
confidence: 99%