Carboxyl Terminal of G Protein β Subunit Is Required for Association with γ Subunit

1995 ◽  
Vol 214 (2) ◽  
pp. 694-700 ◽  
Author(s):  
J. Yamauchi ◽  
Y. Kaziro ◽  
H. Itoh
Keyword(s):  
G Protein ◽  
Β Subunit ◽  
Γ Subunit ◽  
Carboxyl Terminal

scholarly journals A brain-specific γ subunit of G protein freed from the corresponding β subunit under non-denaturing conditions

FEBS Letters ◽  
1994 ◽  
Vol 337 (1) ◽  
pp. 23-26 ◽  
Author(s):  
Rika Morishita ◽  
Kanefusa Kato ◽  
Tomiko Asano
Keyword(s):  
G Protein ◽  
Β Subunit ◽  
Γ Subunit

scholarly journals Proper processing of a G protein γ subunit depends on complex formation with a β subunit

FEBS Letters ◽  
1993 ◽  
Vol 328 (1-2) ◽  
pp. 89-93 ◽  
Author(s):  
Alexey N. Pronin ◽  
Narasimhan Gautam
Keyword(s):  
Complex Formation ◽  
G Protein ◽  
Β Subunit ◽  
Γ Subunit

Cloning and Analyzing of G-protein β-Subunit Gene in Rhizoctonia solani Causing Soybean Sharp Eyespot

2009 ◽  
Vol 35 (2) ◽  
pp. 370-374
Author(s):  
Bing-Tian MA ◽  
Guang-Lin QU ◽  
Wen-Juan HUANG ◽  
Yu-Fan LIN ◽  
Shi-Gui LI
Keyword(s):  
Rhizoctonia Solani ◽  
G Protein ◽  
Β Subunit ◽  
Subunit Gene ◽  
Sharp Eyespot

scholarly journals The Mitochondrial Genome Integrity Gene, MGI1, of Kluyveromyces lactis Encodes the β-Subunit of F1-ATPase

Genetics ◽  
1996 ◽  
Vol 144 (4) ◽  
pp. 1445-1454 ◽  
Author(s):  
Xin Jie Chen ◽  
G Desmond Clark-Walker
Keyword(s):  
Mitochondrial Genome ◽  
Kluyveromyces Lactis ◽  
Three Dimensional ◽  
Genome Integrity ◽  
Dimensional Structure ◽  
Deletion Mutants ◽  
Β Subunit ◽  
Gain Of Function ◽  
F1 Atpase ◽  
Γ Subunit

In a previous report, we found that mutations at the mitochondrial genome integrity locus, MGI1, can convert Kluyveromyces lactis into a petite-positive yeast. In this report, we describe the isolation of the MGI1 gene and show that it encodes the β-subunit of the mitochondrial F1-ATPase. The site of mutation in four independently isolated mgi1 alleles is at Arg435, which has changed to Gly in three cases and Ile in the fourth isolate. Disruption of MGI1 does not lead to the production of mitochondrial genome deletion mutants, indicating that an assembled F1 complex is needed for the “gain-of-function” phenotype found in mgi1 point mutants. The location of Arg435 in the β-subunit, as deduced from the three-dimensional structure of the bovine F1-ATPase, together with mutational sites in the previously identified mgi2 and mgi5 alleles, suggests that interaction of the β- and α- (MGI2) subunits with the γ-subunit (MGI5) is likely to be affected by the mutations.

scholarly journals Mice with Deficiency of G Protein γ3 Are Lean and Have Seizures

2004 ◽  
Vol 24 (17) ◽  
pp. 7758-7768 ◽  
Author(s):  
William F. Schwindinger ◽  
Kathryn E. Giger ◽  
Kelly S. Betz ◽  
Anna M. Stauffer ◽  
Elaine M. Sunderlin ◽  
...  
Keyword(s):  
Signaling Pathways ◽  
G Protein ◽  
Gene Targeting ◽  
Wild Type ◽  
Phenotypic Changes ◽  
Reduced Body ◽  
Γ Subunit ◽  
Body Weights ◽  
The Brain ◽  
Increased Susceptibility

ABSTRACT Emerging evidence suggests that the γ subunit composition of an individual G protein contributes to the specificity of the hundreds of known receptor signaling pathways. Among the twelve γ subtypes, γ3 is abundantly and widely expressed in the brain. To identify specific functions and associations for γ3, a gene-targeting approach was used to produce mice lacking the Gng3 gene (Gng3 −/−). Confirming the efficacy and specificity of gene targeting, Gng3 −/− mice show no detectable expression of the Gng3 gene, but expression of the divergently transcribed Bscl2 gene is not affected. Suggesting unique roles for γ3 in the brain, Gng3 −/− mice display increased susceptibility to seizures, reduced body weights, and decreased adiposity compared to their wild-type littermates. Predicting possible associations for γ3, these phenotypic changes are associated with significant reductions in β2 and αi3 subunit levels in certain regions of the brain. The finding that the Gng3 −/− mice and the previously reported Gng7 −/− mice display distinct phenotypes and different αβγ subunit associations supports the notion that even closely related γ subtypes, such as γ3 and γ7, perform unique functions in the context of the organism.

scholarly journals Epigenetic control of pheromone MAPK signaling determines sexual fecundity inCandida albicans

2017 ◽  
Vol 114 (52) ◽  
pp. 13780-13785 ◽  
Author(s):  
Christine M. Scaduto ◽  
Shail Kabrawala ◽  
Gregory J. Thomson ◽  
William Scheving ◽  
Andy Ly ◽  
...  
Keyword(s):  
Candida Albicans ◽  
G Protein ◽  
Map Kinases ◽  
Mapk Pathway ◽  
Cell Types ◽  
Mapk Signaling ◽  
Toggle Switch ◽  
Β Subunit ◽  
Epigenetic Control ◽  
Incandida Albicans

Several pathogenicCandidaspecies are capable of heritable and reversible switching between two epigenetic states, “white” and “opaque.” InCandida albicans, white cells are essentially sterile, whereas opaque cells are mating-proficient. Here, we interrogate the mechanism by which the white-opaque switch regulates sexual fecundity and identify four genes in the pheromone MAPK pathway that are expressed at significantly higher levels in opaque cells than in white cells. These genes encode the β subunit of the G-protein complex (STE4), the pheromone MAPK scaffold (CST5), and the two terminal MAP kinases (CEK1/CEK2). To define the contribution of each factor to mating,C. albicanswhite cells were reverse-engineered to express elevated, opaque-like levels of these factors, either singly or in combination. We show that white cells co-overexpressingSTE4,CST5, andCEK2undergo mating four orders of magnitude more efficiently than control white cells and at a frequency approaching that of opaque cells. Moreover, engineered white cells recapitulate the transcriptional and morphological responses of opaque cells to pheromone. These results therefore reveal multiple bottlenecks in pheromone MAPK signaling in white cells and that alleviation of these bottlenecks enables efficient mating by these “sterile” cell types. Taken together, our findings establish that differential expression of several MAPK factors underlies the epigenetic control of mating inC. albicans. We also discuss how fitness advantages could have driven the evolution of a toggle switch to regulate sexual reproduction in pathogenicCandidaspecies.

scholarly journals Neural regulation of the formation of skeletal muscle phosphorylase kinase holoenzyme in adult and developing rat muscle

1997 ◽  
Vol 325 (3) ◽  
pp. 793-800 ◽  
Author(s):  
Dean C. NG ◽  
Richard C. CARLSEN ◽  
Donal A. WALSH
Keyword(s):  
Skeletal Muscle ◽  
Muscle Development ◽  
Rapid Decline ◽  
Phosphorylase Kinase ◽  
Β Subunit ◽  
Subunit Protein ◽  
Subunit Mrna ◽  
Γ Subunit ◽  
Muscle Phosphorylase ◽  
Denervated Muscles

Neural influences on the co-ordination of expression of the multiple subunits of skeletal muscle phosphorylase kinase and their assembly to form the holoenzyme complex, α4β4γ4δ4, have been examined during denervation and re-innervation of adult skeletal muscle and during neonatal muscle development. Denervation of the tibialis anterior and extensor digitorum longus muscles of the rat hindlimb was associated with a rapid decline in the mRNA for the γ subunit, and an abrupt decrease in γ-subunit protein. The levels of the α- and β-subunit proteins in the denervated muscles also declined rapidly, their time course of reduction being similar to that for the γ-subunit protein, but they did not decrease to the same extent. In contrast with the rapid decline in γ-subunit mRNA upon denervation, α- and β-subunit mRNAs stayed at control innervated levels for approx. 8–10 days, but then decreased rapidly. Their decline coincided very closely with the onset of re-innervation. Re-innervation of the denervated muscles, which occurs rapidly and uniformly after the sciatic nerve crush injury, produced an eventual slow and prolonged recovery of the mRNA for all three subunits and parallel increases in each of the subunit proteins. A similar co-ordinated increase of both subunit mRNA and subunit proteins of the phosphorylase kinase holoenzyme was observed during neonatal muscle development, during the period when the muscles were attaining their adult pattern of motor activity. The phosphorylase kinase holoenzyme remains in a non-activated form during all of these physiological changes, as is compatible with the presence of the full complement of the regulatory subunits. These data are consistent with a model whereby the transcriptional and translational expression of phosphorylase kinase γ subunit occurs only with concomitant expression of the α and β subunits. This would ensure that free and unregulated, activated γ subunit alone, which would give rise to unregulated glycogenolysis, is not produced. The data also suggest that control of phosphorylase kinase subunit expression and the formation of the holoenzyme in skeletal muscle is provided by the motor nerve, probably through imposed levels or patterns of muscle activity.

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