Characterizations and functions of regulator of G protein signaling (RGS) in fungi

Abstract

Proteins that serve as regulator of G protein signaling (RGS) primarily function as GTPase accelerators that promote GTP hydrolysis by the Gα subunits, thereby inactivating the G protein and rapidly switching off G protein-coupled signaling pathways. Since the first RGS protein was identified from the budding yeast Saccharomyces cerevisiae, more than 30 RGS and RGS-like proteins have been characterized from several model fungi, such as Aspergillus nidulans, Beauveria bassiana, Candida albicans, Fusarium verticillioides, Magnaporthe oryzae, and Metarhizium anisopliae. In this review, the partial biochemical properties and functional domains of RGS and RGS-like proteins were predicted and compared, and the roles of RGS and RGS-like proteins in different fungi were summarized. Moreover, the phylogenetic relationship among RGS and RGS-like proteins from various fungi was analyzed and discussed.

Host‐induced gene silencing of a regulator of G protein signalling gene (VdRGS1) confers resistance to Verticillium wilt in cotton

“…The availability of data on the whole‐genome of sequenced fungi made it possible to identify the encoding genes of RGS and RGS‐like proteins on a genomewide scale and to enrich our understanding of the properties and molecular mechanisms of the RGS and RGS‐like genes. There are generally four to eight RGS and RGS‐like genes in fungi, and their transcriptional direction is irregular (Wang et al ., ). Generally, the RGS domain is the core of RGS proteins and each RGS protein typically contains one such domain (Wang et al ., ).…”

“…There are generally four to eight RGS and RGS‐like genes in fungi, and their transcriptional direction is irregular (Wang et al ., ). Generally, the RGS domain is the core of RGS proteins and each RGS protein typically contains one such domain (Wang et al ., ). Interestingly, RGS domains can be found in conjunction with a variety of other domains, such as DEP for membrane targeting, phosphatidylinositol binding (Phox, PX) for phosphatidylinositol binding (IPR001683), Phox‐associated (PXA), which is associated with PX (IPR003114), and G protein gamma subunit‐like (GGL) for binding Gβ subunits (IPR001770) (De Vries et al ., ).…”

The Accordant Trend of Both Parameters (rgs Expression and cAMP Content) Follows the Pattern of Development of Fruiting Body in Volvariella volvacea

“…The RGS proteins are a family of multi-functional signaling proteins [25]. Except for RgsC2 in Fusarium verticillioides [16], most RGS proteins have an RGS domain, which comprises the core of these proteins.…”

“…Except for RgsC2 in Fusarium verticillioides [16], most RGS proteins have an RGS domain, which comprises the core of these proteins. These proteins can bind directly to Ga subunit of heterotrimeric G protein [25]. Besides the activity of GTPase-activating proteins (GAP), RGS proteins can enhance the activation of G protein by serving as effectors, scaffold proteins to gather receptors, G proteins, effectors, and other regulatory molecules together [31].…”

Transcriptome Analyses Shed New Insights into Primary Metabolism and Regulation of Blumeria graminis f. sp. tritici during Conidiation

“…Additionally, at least two G protein mediated signal transduction pathways are involved in A. nidulans conidiation by negatively regulating the BrlA pathway (Yu, 2006). Conidiation-related heterotrimeric G protein signaling components include G protein coupled receptors (GPCRs), heterotrimeric G proteins and regulators of G protein signaling proteins (Park and Yu, 2012; Wang et al, 2013). Recently, a few small monomeric GTPases have also been shown to be implicated in various cellular processes including conidiation and tolerance to multi-stressors such as H 2 O 2 (Guan et al, 2015).…”