Are the Functional Roles of Arabidopsis G Protein α Subunit Extended to Tomato Plants?

2020 ◽  
Author(s):  
Thao Ninh
Keyword(s):  
G Protein ◽  
Α Subunit ◽  
Tomato Plants ◽  
Functional Roles ◽  
G Protein Α Subunit

scholarly journals The G-Protein α-Subunit GasC Plays a Major Role in Germination in the Dimorphic FungusPenicillium marneffei

Genetics ◽  
2003 ◽  
Vol 164 (2) ◽  
pp. 487-499 ◽  
Author(s):  
Sophie Zuber ◽  
Michael J Hynes ◽  
Alex Andrianopoulos
Keyword(s):  
G Protein ◽  
Germination Rate ◽  
Yeast Cells ◽  
Class Iii ◽  
Temperature Dependent ◽  
Gene Encoding ◽  
Α Subunit ◽  
G Protein Α Subunit ◽  
Opportunistic Human Pathogen

AbstractThe opportunistic human pathogen Penicillium marneffei exhibits a temperature-dependent dimorphic switch. At 25°, multinucleate, septate hyphae that can undergo differentiation to produce asexual spores (conidia) are produced. At 37° hyphae undergo arthroconidiation to produce uninucleate yeast cells that divide by fission. This work describes the cloning of the P. marneffei gasC gene encoding a G-protein α-subunit that shows high homology to members of the class III fungal Gα-subunits. Characterization of a ΔgasC mutant and strains carrying a dominant-activating gasCG45R or a dominant-interfering gasCG207R allele show that GasC is a crucial regulator of germination. A ΔgasC mutant is severely delayed in germination, whereas strains carrying a dominant-activating gasCG45R allele show a significantly accelerated germination rate. Additionally, GasC signaling positively affects the production of the red pigment by P. marneffei at 25° and negatively affects the onset of conidiation and the conidial yield, showing that GasC function overlaps with functions of the previously described Gα-subunit GasA. In contrast to the S. cerevisiae ortholog Gpa2, our data indicate that GasC is not involved in carbon or nitrogen source sensing and plays no major role in either hyphal or yeast growth or in the switch between these two forms.

Analysis by mRNA levels of the expression of six G protein α-subunit genes in mammalian cells and tissues

1991 ◽  
Vol 1094 (2) ◽  
pp. 193-199 ◽  
Author(s):  
Jermelina Linor R. Garibay ◽  
Tohru Kozasa ◽  
Hiroshi Itoh ◽  
Toshihiko Tsukamoto ◽  
Masaaki Matsuoka ◽  
...  
Keyword(s):  
G Protein ◽  
Mammalian Cells ◽  
Mrna Levels ◽  
Α Subunit ◽  
G Protein Α Subunit

scholarly journals Large G protein α-subunit XLαs limits clathrin-mediated endocytosis and regulates tissue iron levels in vivo

2017 ◽  
Vol 114 (45) ◽  
pp. E9559-E9568 ◽  
Author(s):  
Qing He ◽  
Richard Bouley ◽  
Zun Liu ◽  
Marc N. Wein ◽  
Yan Zhu ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
G Protein ◽  
Critical Role ◽  
Hek293 Cells ◽  
Activity Levels ◽  
Α Subunit ◽  
Proteomic Screen ◽  
Protein Levels ◽  
G Protein Α Subunit

Alterations in the activity/levels of the extralarge G protein α-subunit (XLαs) are implicated in various human disorders, such as perinatal growth retardation. Encoded by GNAS, XLαs is partly identical to the α-subunit of the stimulatory G protein (Gsα), but the cellular actions of XLαs remain poorly defined. Following an initial proteomic screen, we identified sorting nexin-9 (SNX9) and dynamins, key components of clathrin-mediated endocytosis, as binding partners of XLαs. Overexpression of XLαs in HEK293 cells inhibited internalization of transferrin, a process that depends on clathrin-mediated endocytosis, while its ablation by CRISPR/Cas9 in an osteocyte-like cell line (Ocy454) enhanced it. Similarly, primary cardiomyocytes derived from XLαs knockout (XLKO) pups showed enhanced transferrin internalization. Early postnatal XLKO mice showed a significantly higher degree of cardiac iron uptake than wild-type littermates following iron dextran injection. In XLKO neonates, iron and ferritin levels were elevated in heart and skeletal muscle, where XLαs is normally expressed abundantly. XLKO heart and skeletal muscle, as well as XLKO Ocy454 cells, showed elevated SNX9 protein levels, and siRNA-mediated knockdown of SNX9 in XLKO Ocy454 cells prevented enhanced transferrin internalization. In transfected cells, XLαs also inhibited internalization of the parathyroid hormone and type 2 vasopressin receptors. Internalization of transferrin and these G protein-coupled receptors was also inhibited in cells expressing an XLαs mutant missing the Gα portion, but not Gsα or an N-terminally truncated XLαs mutant unable to interact with SNX9 or dynamin. Thus, XLαs restricts clathrin-mediated endocytosis and plays a critical role in iron/transferrin uptake in vivo.

Isolation of a gene encoding a G protein α subunit involved in the regulation of cAMP levels in the yeastKluyveromyces lactis

Yeast ◽  
1996 ◽  
Vol 12 (11) ◽  
pp. 1125-1133 ◽  
Author(s):  
Alma L. Saviñón-Tejeda ◽  
Laura Ongay-Larios ◽  
Jorge RamíRez ◽  
Roberto Coria
Keyword(s):  
G Protein ◽  
Gene Encoding ◽  
Α Subunit ◽  
G Protein Α Subunit ◽  
Camp Levels

scholarly journals Rational design of a heterotrimeric G protein α subunit with artificial inhibitor sensitivity

2019 ◽  
Vol 294 (15) ◽  
pp. 5747-5758 ◽  
Author(s):  
Davide Malfacini ◽  
Julian Patt ◽  
Suvi Annala ◽  
Kasper Harpsøe ◽  
Funda Eryilmaz ◽  
...  
Keyword(s):  
G Protein ◽  
Rational Design ◽  
Heterotrimeric G Protein ◽  
Α Subunit ◽  
G Protein Α Subunit

scholarly journals Subtype-specific increase in G-protein α-subunit mRNA by interleukin 1β

FEBS Letters ◽  
1989 ◽  
Vol 249 (2) ◽  
pp. 139-142 ◽  
Author(s):  
Richard T. Lee ◽  
Tommy A. Brock ◽  
Cynthia Tolman ◽  
Kenneth D. Bloch ◽  
J.G. Seidman ◽  
...  
Keyword(s):  
G Protein ◽  
Interleukin 1Β ◽  
Α Subunit ◽  
Subunit Mrna ◽  
Specific Increase ◽  
G Protein Α Subunit
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