scholarly journals Are prenyl groups on proteins sticky fingers or greasy handles?

2003 ◽  
Vol 376 (1) ◽  
pp. e3-e4 ◽  
Author(s):  
Anthony I. MAGEE ◽  
Miguel C. SEABRA

This Commentary discusses the work of Dietrich et al. in this issue of the Biochemical Journal, which sheds new light on the biological roles of protein-bound prenyl groups by providing evidence that the α-subunit of the heterotrimeric G-protein transducin has a binding site for the geranylgeranyl group of the γ-subunit.

2018 ◽  
Vol 19 (11) ◽  
pp. 3596 ◽  
Author(s):  
Sakura Matsuta ◽  
Aki Nishiyama ◽  
Genki Chaya ◽  
Takafumi Itoh ◽  
Kotaro Miura ◽  
...  

Heterotrimeric G proteins are the molecule switch that transmits information from external signals to intracellular target proteins in mammals and yeast cells. In higher plants, heterotrimeric G proteins regulate plant architecture. Rice harbors one canonical α subunit gene (RGA1), four extra-large GTP-binding protein genes (XLGs), one canonical β-subunit gene (RGB1), and five γ-subunit genes (tentatively designated RGG1, RGG2, RGG3/GS3/Mi/OsGGC1, RGG4/DEP1/DN1/qPE9-1/OsGGC3, and RGG5/OsGGC2) as components of the heterotrimeric G protein complex. Among the five γ-subunit genes, RGG1 encodes the canonical γ-subunit, RGG2 encodes a plant-specific type of γ-subunit with additional amino acid residues at the N-terminus, and the remaining three γ-subunit genes encode atypical γ-subunits with cysteine-rich C-termini. We characterized the RGG4/DEP1/DN1/qPE9-1/OsGGC3 gene product Gγ4 in the wild type (WT) and truncated protein Gγ4∆Cys in the RGG4/DEP1/DN1/qPE9-1/OsGGC3 mutant, Dn1-1, as littele information regarding the native Gγ4 and Gγ4∆Cys proteins is currently available. Based on liquid chromatography-tandem mass spectrometry analysis, immunoprecipitated Gγ4 candidates were confirmed as actual Gγ4. Similar to α-(Gα) and β-subunits (Gβ), Gγ4 was enriched in the plasma membrane fraction and accumulated in the developing leaf sheath. As RGG4/DEP1/DN1/qPE9-1/OsGGC3 mutants exhibited dwarfism, tissues that accumulated Gγ4 corresponded to the abnormal tissues observed in RGG4/DEP1/DN1/qPE9-1/OsGGC3 mutants.


2004 ◽  
Vol 72 (12) ◽  
pp. 6826-6835 ◽  
Author(s):  
Ken Teter ◽  
Michael G. Jobling ◽  
Randall K. Holmes

ABSTRACT Cholera toxin (CT) moves from the cell surface to the endoplasmic reticulum (ER) by retrograde vesicular transport. The catalytic A1 polypeptide of CT (CTA1) then crosses the ER membrane, enters the cytosol, ADP-ribosylates the stimulatory α subunit of the heterotrimeric G protein (Gsα) at the cytoplasmic face of the plasma membrane, and activates adenylate cyclase. The cytosolic pool of CTA1 may reach the plasma membrane and its Gsα target by traveling on anterograde-directed transport vesicles. We examined this possibility with the use of a plasmid-based transfection system that directed newly synthesized CTA1 to either the ER lumen or the cytosol of CHO cells. Such a system allowed us to bypass the CT retrograde trafficking itinerary from the cell surface to the ER. Previous work has shown that the ER-localized pool of CTA1 is rapidly exported from the ER to the cytosol. Expression of CTA1 in either the ER or the cytosol led to the activation of Gsα, and Gsα activation was not inhibited in transfected cells exposed to drugs that inhibit vesicular traffic. Thus, anterograde transport from the ER to the plasma membrane is not required for the cytotoxic action of CTA1.


2016 ◽  
Vol 110 (3) ◽  
pp. 380a
Author(s):  
Ersoy Cholak ◽  
Ines Karmous ◽  
Bihter Avşar ◽  
Zehra Sayers

2000 ◽  
Vol 275 (3) ◽  
pp. 2157-2164 ◽  
Author(s):  
Jingzhen Yuan ◽  
Lee Slice ◽  
John H. Walsh ◽  
Enrique Rozengurt

2019 ◽  
Vol 294 (15) ◽  
pp. 5747-5758 ◽  
Author(s):  
Davide Malfacini ◽  
Julian Patt ◽  
Suvi Annala ◽  
Kasper Harpsøe ◽  
Funda Eryilmaz ◽  
...  

Biochemistry ◽  
2006 ◽  
Vol 45 (43) ◽  
pp. 12986-12997 ◽  
Author(s):  
Najmoutin G. Abdulaev ◽  
Tony Ngo ◽  
Eva Ramon ◽  
Danielle M. Brabazon ◽  
John P. Marino ◽  
...  

2009 ◽  
Vol 84 (1) ◽  
pp. 35-42 ◽  
Author(s):  
Katsuyuki Oki ◽  
Noriko Inaba ◽  
Hidemi Kitano ◽  
Sachiko Takahashi ◽  
Yukiko Fujisawa ◽  
...  

Cell Research ◽  
2006 ◽  
Vol 16 (12) ◽  
pp. 916-922 ◽  
Author(s):  
Lei Wang ◽  
Yun-Yuan Xu ◽  
Qi-Bin Ma ◽  
Dan Li ◽  
Zhi-Hong Xu ◽  
...  

PLoS ONE ◽  
2018 ◽  
Vol 13 (5) ◽  
pp. e0197442 ◽  
Author(s):  
Xueshui Guo ◽  
Natalia A. Riobo-Del Galdo ◽  
Eun Ji Kim ◽  
Gregory R. Grant ◽  
David R. Manning

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