Interaction of G protein Gβγ dimers with small GTP‐binding proteins of the Rho family

Harhammer, Rainer; Gohla, Antje; Schultz, Glauco

doi:10.1016/s0014-5793(96)01327-0

Cited by 31 publications

(24 citation statements)

References 35 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Treatment of neutrophil membranes with either heat or trypsin significantly reduced the translocation of Rho proteins (36), suggesting the existence of a membrane receptor. Furthermore, G␤␥ dimers of heterotrimeric G proteins associate to various GST-Rho proteins in vitro (18) suggesting that these subunits participate in the binding of Rho proteins to membranes. Association of RHO1, the Saccharomyces cerevisiae homolog of the mammalian RhoA, with cortical actin patches is saturable and requires prenylation (38).…”

Section: Discussionmentioning

confidence: 99%

“…Alternatively, the translocation of activated Rho proteins from the cytosol to specific membranes in polarized epithelial cells (17) suggests that receptors could be involved in the targeting process. In addition, G␤␥ dimers of heterotrimeric G proteins bind to GST 1 ⅐Rho fusion proteins in vitro (18) suggesting that G␤␥ dimers facilitate the association of Rho proteins to plasma membranes and possibly with other membrane proteins as well.…”

mentioning

confidence: 99%

See 1 more Smart Citation

Modulation of Rho and Cytoskeletal Protein Attachment to Membranes by a Prenylcysteine Analog

Desrosiers

Gauthier

Lanthier

et al. 2000

Journal of Biological Chemistry

View full text Add to dashboard Cite

The GTPases Rho regulate the assembly of polymerized actin structures. Their C-terminal sequences end with the CAAX motif that undergo a lipidation of the cysteine residue. Analogs to the C-terminal ends of Rho proteins, N-acetyl-S-all-trans,trans-farnesyl-L-cysteine and N-acetyl-S-all-trans-geranylgeranyl-L-cysteine, were used to analyze the role of prenylation in their membrane association. Silver-stained gels indicated that Nacetyl-S-all-trans-geranylgeranyl-L-cysteine treatment released only a few proteins of 20, 46, and 60 kDa. Western blot analysis showed that N-acetyl-S-all-trans-geranylgeranyl-L-cysteine released RhoB (10%), RhoA (28%), and Cdc42 (95%) from membranes, whereas N-acetyl-Sall-trans and trans-farnesyl-L-cysteine did not. Rab1, which possesses two geranylgeranyl groups, was also strongly extracted by N-acetyl-S-all-trans-geranylgeranyl-L-cysteine, whereas Ras, which is farnesylated, was not. Furthermore, N-acetyl-S-all-trans-geranylgeranyl-L-cysteine was very efficient (95%) in dissociating actin and tubulin from membranes but not integral membrane protein P-glycoprotein and sodium/phosphate cotransporter NaP i -2. The extraction of Rho and cytoskeletal proteins occurred below the critical micellar concentration of N-acetyl-S-all-trans-geranylgeranyl-Lcysteine. Membrane treatments with 0.7 M KI totally extracted actin, whereas 70% of Cdc42 was released. Actin was, however, insoluble in Triton X-100-treated membranes, whereas this detergent extracted (80%) Cdc42. These data show that Rho proteins and actin are not physically bound together and suggest that their extraction from membranes by N-acetyl-S-all-trans-geranylgeranyl-L-cysteine likely occurs via different mechanisms.

show abstract

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Modulation of Rho and Cytoskeletal Protein Attachment to Membranes by a Prenylcysteine Analog

Desrosiers

Gauthier

Lanthier

et al. 2000

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…Rho1 associates in vivo with the G␤ subunit (Ste4) as judged by affinity precipitation experiments. Precedents for the association of mammalian RhoA with G␤ subunits reveal that this interaction is highly conserved (4,108). Pkc1 is also recruited to the tips of mating projections in a manner dependent on Rho1 association with G␤, presumably reflecting the recruitment of Pkc1 to GTP-bound Rho1 (21).…”

Section: Pheromone-induced Morphogenesismentioning

confidence: 99%

Cell Wall Integrity Signaling inSaccharomyces cerevisiae

Levin¹

2005

Microbiol Mol Biol Rev

1,039

1,227

View full text Add to dashboard Cite

The yeast cell wall is a highly dynamic structure that is responsible for protecting the cell from rapid changes in external osmotic potential. The wall is also critical for cell expansion during growth and morphogenesis. This review discusses recent advances in understanding the various signal transduction pathways that allow cells to monitor the state of the cell wall and respond to environmental challenges to this structure. The cell wall integrity signaling pathway controlled by the small G-protein Rho1 is principally responsible for orchestrating changes to the cell wall periodically through the cell cycle and in response to various forms of cell wall stress. This signaling pathway acts through direct control of wall biosynthetic enzymes, transcriptional regulation of cell wall-related genes, and polarization of the actin cytoskeleton. However, additional signaling pathways interface both with the cell wall integrity signaling pathway and with the actin cytoskeleton to coordinate polarized secretion with cell wall expansion. These include Ca2+ signaling, phosphatidylinositide signaling at the plasma membrane, sphingoid base signaling through the Pkh1 and -2 protein kinases, Tor kinase signaling, and pathways controlled by the Rho3, Rho4, and Cdc42 G-proteins

show abstract

“…The Gbg complex of the pheromone response pathway, which provides the positional clues for polarity establishment, recruits Rho1 to the site of polarized growth (Bar et al 2003). Precedents for the association of mammalian RhoA with Gb subunits reveal that this interaction is highly conserved (Harhammer et al 1996;Alberts et al 1998). As noted above, the Mid2 sensor is also recruited to mating projections (Hutzler et al 2008).…”

Section: Pheromone-induced Morphogenesismentioning

confidence: 99%

Regulation of Cell Wall Biogenesis in Saccharomyces cerevisiae: The Cell Wall Integrity Signaling Pathway

2011

View full text Add to dashboard Cite

The yeast cell wall is a strong, but elastic, structure that is essential not only for the maintenance of cell shape and integrity, but also for progression through the cell cycle. During growth and morphogenesis, and in response to environmental challenges, the cell wall is remodeled in a highly regulated and polarized manner, a process that is principally under the control of the cell wall integrity (CWI) signaling pathway. This pathway transmits wall stress signals from the cell surface to the Rho1 GTPase, which mobilizes a physiologic response through a variety of effectors. Activation of CWI signaling regulates the production of various carbohydrate polymers of the cell wall, as well as their polarized delivery to the site of cell wall remodeling. This review article centers on CWI signaling in Saccharomyces cerevisiae through the cell cycle and in response to cell wall stress. The interface of this signaling pathway with other pathways that contribute to the maintenance of cell wall integrity is also discussed.

show abstract

Interaction of G protein Gβγ dimers with small GTP‐binding proteins of the Rho family

Cited by 31 publications

References 35 publications

Modulation of Rho and Cytoskeletal Protein Attachment to Membranes by a Prenylcysteine Analog

Modulation of Rho and Cytoskeletal Protein Attachment to Membranes by a Prenylcysteine Analog

Cell Wall Integrity Signaling inSaccharomyces cerevisiae

Regulation of Cell Wall Biogenesis in Saccharomyces cerevisiae: The Cell Wall Integrity Signaling Pathway

Contact Info

Product

Resources

About