Faculty Opinions recommendation of The interaction of nucleoside diphosphate kinase B with Gbetagamma dimers controls heterotrimeric G protein function.

2009 ◽  
Author(s):  
Philip Wedegaertner
Keyword(s):  
G Protein ◽  
Protein Function ◽  
Nucleoside Diphosphate Kinase ◽  
Heterotrimeric G Protein ◽  
Nucleoside Diphosphate Kinase B

Nucleoside diphosphate kinase B is required for the formation of heterotrimeric G protein containing caveolae

2011 ◽  
Vol 384 (4-5) ◽  
pp. 461-472 ◽  
Author(s):  
Hans-Jörg Hippe ◽  
Nadine M. Wolf ◽  
H. Issam Abu-Taha ◽  
Susanne Lutz ◽  
Soazig Le Lay ◽  
...  
Keyword(s):  
G Protein ◽  
Nucleoside Diphosphate Kinase ◽  
Heterotrimeric G Protein ◽  
Nucleoside Diphosphate Kinase B

Plant heterotrimeric G protein function: insights from Arabidopsis and rice mutants

2004 ◽  
Vol 7 (6) ◽  
pp. 719-731 ◽  
Author(s):  
Laetitia Perfus-Barbeoch ◽  
Alan M Jones ◽  
Sarah M Assmann
Keyword(s):  
G Protein ◽  
Protein Function ◽  
Heterotrimeric G Protein

scholarly journals Regulation of Cardiac cAMP Synthesis and Contractility by Nucleoside Diphosphate Kinase B/G Protein βγ Dimer Complexes

2007 ◽  
Vol 100 (8) ◽  
pp. 1191-1199 ◽  
Author(s):  
Hans-Joerg Hippe ◽  
Mark Luedde ◽  
Susanne Lutz ◽  
Henrike Koehler ◽  
Thomas Eschenhagen ◽  
...  
Keyword(s):  
G Protein ◽  
Nucleoside Diphosphate Kinase ◽  
Camp Synthesis ◽  
Nucleoside Diphosphate Kinase B

scholarly journals The β Subunit of the Heterotrimeric G Protein Triggers the Kluyveromyces lactis Pheromone Response Pathway in the Absence of the γ Subunit

2010 ◽  
Vol 21 (3) ◽  
pp. 489-498 ◽  
Author(s):  
Rocío Navarro-Olmos ◽  
Laura Kawasaki ◽  
Lenin Domínguez-Ramírez ◽  
Laura Ongay-Larios ◽  
Rosario Pérez-Molina ◽  
...  
Keyword(s):  
G Protein ◽  
Protein Function ◽  
Mating Disruption ◽  
Kluyveromyces Lactis ◽  
Dominant Negative ◽  
Generic Model ◽  
Wild Type ◽  
Heterotrimeric G Protein ◽  
Pheromone Response Pathway ◽  
Γ Subunit

The Kluyveromyces lactis heterotrimeric G protein is a canonical Gαβγ complex; however, in contrast to Saccharomyces cerevisiae, where the Gγ subunit is essential for mating, disruption of the KlGγ gene yielded cells with almost intact mating capacity. Expression of a nonfarnesylated Gγ, which behaves as a dominant-negative in S. cerevisiae, did not affect mating in wild-type and ΔGγ cells of K. lactis. In contrast to the moderate sterility shown by the single ΔKlGα, the double ΔKlGα ΔKlGγ mutant displayed full sterility. A partial sterile phenotype of the ΔKlGγ mutant was obtained in conditions where the KlGβ subunit interacted defectively with the Gα subunit. The addition of a CCAAX motif to the C-end of KlGβ, partially suppressed the lack of both KlGα and KlGγ subunits. In cells lacking KlGγ, the KlGβ subunit cofractionated with KlGα in the plasma membrane, but in the ΔKlGα ΔKlGγ strain was located in the cytosol. When the KlGβ-KlGα interaction was affected in the ΔKlGγ mutant, most KlGβ fractionated to the cytosol. In contrast to the generic model of G-protein function, the Gβ subunit of K. lactis has the capacity to attach to the membrane and to activate mating effectors in absence of the Gγ subunit.

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