Analysis of the Rac/Rop Small GTPase Family in Rice: Expression, Subcellular Localization and Role in Disease Resistance

2010 ◽  
Vol 51 (4) ◽  
pp. 585-595 ◽  
Author(s):  
L. Chen ◽  
K. Shiotani ◽  
T. Togashi ◽  
D. Miki ◽  
M. Aoyama ◽  
...  
Keyword(s):  
Disease Resistance ◽  
Subcellular Localization ◽  
Small Gtpase

Subcellular Localization of the Small GTPase Rab5a in Resting and Stimulated Human Neurotrophils

1997 ◽  
Vol 230 (2) ◽  
pp. 415
Author(s):  
Francesca Vita ◽  
Maria Rosa Soranzo ◽  
Violetta Borelli ◽  
Paolo Bertoncin ◽  
Giuliano Zabucchi
Keyword(s):  
Subcellular Localization ◽  
Small Gtpase

scholarly journals Influence of Subcellular Localization and Functional State on Protein Turnover

Cells ◽  
2021 ◽  
Vol 10 (7) ◽  
pp. 1747
Author(s):  
Roya Yousefi ◽  
Kristina Jevdokimenko ◽  
Verena Kluever ◽  
David Pacheu-Grau ◽  
Eugenio F. Fornasiero
Keyword(s):  
Subcellular Localization ◽  
Functional State ◽  
Protein Turnover ◽  
Protein Localization ◽  
Small Gtpase ◽  
Turnover Rates ◽  
Cellular Behavior ◽  
Two Factors ◽  
Brain Creatine Kinase ◽  
Selection Of

Protein homeostasis is an equilibrium of paramount importance that maintains cellular performance by preserving an efficient proteome. This equilibrium avoids the accumulation of potentially toxic proteins, which could lead to cellular stress and death. While the regulators of proteostasis are the machineries controlling protein production, folding and degradation, several other factors can influence this process. Here, we have considered two factors influencing protein turnover: the subcellular localization of a protein and its functional state. For this purpose, we used an imaging approach based on the pulse-labeling of 17 representative SNAP-tag constructs for measuring protein lifetimes. With this approach, we obtained precise measurements of protein turnover rates in several subcellular compartments. We also tested a selection of mutants modulating the function of three extensively studied proteins, the Ca2+ sensor calmodulin, the small GTPase Rab5a and the brain creatine kinase (CKB). Finally, we followed up on the increased lifetime observed for the constitutively active Rab5a (Q79L), and we found that its stabilization correlates with enlarged endosomes and increased interaction with membranes. Overall, our data reveal that both changes in protein localization and functional state are key modulators of protein turnover, and protein lifetime fluctuations can be considered to infer changes in cellular behavior.

scholarly journals Phosphorylation by Protein Kinase Cα Regulates RalB Small GTPase Protein Activation, Subcellular Localization, and Effector Utilization

2012 ◽  
Vol 287 (18) ◽  
pp. 14827-14836 ◽  
Author(s):  
Timothy D. Martin ◽  
Natalia Mitin ◽  
Adrienne D. Cox ◽  
Jen Jen Yeh ◽  
Channing J. Der
Keyword(s):  
Protein Kinase ◽  
Subcellular Localization ◽  
Small Gtpase ◽  
Protein Activation ◽  
Protein Kinase Cα

Subcellular Localization of the Small GTPase Rab5a in Resting and Stimulated Human Neutrophils

1996 ◽  
Vol 227 (2) ◽  
pp. 367-373 ◽  
Author(s):  
Francesca Vita ◽  
Maria Rosa Soranzo ◽  
Violetta Borelli ◽  
Paolo Bertoncin ◽  
Giuliano Zabucchi
Keyword(s):  
Subcellular Localization ◽  
Small Gtpase ◽  
Human Neutrophils

scholarly journals Essential role of the small GTPase Rac in disease resistance of rice

2001 ◽  
Vol 98 (2) ◽  
pp. 759-764 ◽  
Author(s):  
E. Ono ◽  
H. L. Wong ◽  
T. Kawasaki ◽  
M. Hasegawa ◽  
O. Kodama ◽  
...  
Keyword(s):  
Disease Resistance ◽  
Essential Role ◽  
Small Gtpase ◽  
Gtpase Rac

scholarly journals The heterotrimeric G protein   subunit acts upstream of the small GTPase Rac in disease resistance of rice

2002 ◽  
Vol 99 (20) ◽  
pp. 13307-13312 ◽  
Author(s):  
U. Suharsono ◽  
Y. Fujisawa ◽  
T. Kawasaki ◽  
Y. Iwasaki ◽  
H. Satoh ◽  
...  
Keyword(s):  
Disease Resistance ◽  
G Protein ◽  
Small Gtpase ◽  
Protein Subunit ◽  
Heterotrimeric G Protein ◽  
Gtpase Rac

scholarly journals Genome-Wide Identification, Characterization and Expression Analysis of the JAZ Gene Family in Resistance to Gray Leaf Spots in Tomato

2021 ◽  
Vol 22 (18) ◽  
pp. 9974
Author(s):  
Yaoguang Sun ◽  
Chunxin Liu ◽  
Zengbing Liu ◽  
Tingting Zhao ◽  
Jingbin Jiang ◽  
...  
Keyword(s):  
Disease Resistance ◽  
Subcellular Localization ◽  
Plant Disease Resistance ◽  
Regulatory Network ◽  
Plant Disease ◽  
Tobacco Rattle Virus ◽  
Regulatory Role ◽  
Pcr Analysis ◽  
Hormone Regulation ◽  
Leaf Spots

The plant disease resistance system involves a very complex regulatory network in which jasmonates play a key role in response to external biotic or abiotic stresses. As inhibitors of the jasmonic acid (JA) signaling pathway, JASMONATE ZIM domain (JAZ) proteins have been identified in many plant species, and their functions are gradually being clarified. In this study, 26 JAZ genes were identified in tomato. The physical and chemical properties, predicted subcellular localization, gene structure, cis-acting elements, and interspecies collinearity of 26 SlJAZ genes were subsequently analyzed. RNA-seq data combined with qRT-PCR analysis data showed that the expression of most SlJAZ genes were induced in response to Stemphylium lycopersici, methyl jasmonate (MeJA) and salicylic acid (SA). Tobacco rattle virus RNA2-based VIGS vector (TRV2)-SlJAZ25 plants were more resistant to tomato gray leaf spots than TRV2-00 plants. Therefore, we speculated that SlJAZ25 played a negative regulatory role in tomato resistance to gray leaf spots. Based on combining the results of previous studies and those of our experiments, we speculated that SlJAZ25 might be closely related to JA and SA hormone regulation. SlJAZ25 interacted with SlJAR1, SlCOI1, SlMYC2, and other resistance-related genes to form a regulatory network, and these genes played an important role in the regulation of tomato gray leaf spots. The subcellular localization results showed that the SlJAZ25 gene was located in the nucleus. Overall, this study is the first to identify and analyze JAZ family genes in tomato via bioinformatics approaches, clarifying the regulatory role of SlJAZ25 genes in tomato resistance to gray leaf spots and providing new ideas for improving plant disease resistance.

Investigating the functional link between TMEM165 and SPCA1

2019 ◽  
Vol 476 (21) ◽  
pp. 3281-3293 ◽  
Author(s):  
Elodie Lebredonchel ◽  
Marine Houdou ◽  
Hans-Heinrich Hoffmann ◽  
Kateryna Kondratska ◽  
Marie-Ange Krzewinski ◽  
...  
Keyword(s):  
Subcellular Localization ◽  
Complete Loss ◽  
Protein Family ◽  
Uncharacterized Protein ◽  
Functional Link ◽  
P Type

TMEM165 was highlighted in 2012 as the first member of the Uncharacterized Protein Family 0016 (UPF0016) related to human glycosylation diseases. Defects in TMEM165 are associated with strong Golgi glycosylation abnormalities. Our previous work has shown that TMEM165 rapidly degrades with supraphysiological manganese supplementation. In this paper, we establish a functional link between TMEM165 and SPCA1, the Golgi Ca2+/Mn2+ P-type ATPase pump. A nearly complete loss of TMEM165 was observed in SPCA1-deficient Hap1 cells. We demonstrate that TMEM165 was constitutively degraded in lysosomes in the absence of SPCA1. Complementation studies showed that TMEM165 abundance was directly dependent on SPCA1's function and more specifically its capacity to pump Mn2+ from the cytosol into the Golgi lumen. Among SPCA1 mutants that differentially impair Mn2+ and Ca2+ transport, only the Q747A mutant that favors Mn2+ pumping rescues the abundance and Golgi subcellular localization of TMEM165. Interestingly, the overexpression of SERCA2b also rescues the expression of TMEM165. Finally, this paper highlights that TMEM165 expression is linked to the function of SPCA1.

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