scholarly journals Rice annexin OsANN4 interacting with OsCDPK24, reduces root aerenchyma formation by modulating H2O2 under ABA treatment

2019 ◽  
Author(s):  
Qian Zhang ◽  
Tao Song ◽  
Can Guan ◽  
Yingjie Gao ◽  
Jianchao Ma ◽  
...  
Keyword(s):  
Calcium Binding ◽  
Lateral Roots ◽  
Redox Homeostasis ◽  
Phosphorylation Site ◽  
Lipid Binding ◽  
Biological Processes ◽  
Aerenchyma Formation ◽  
Exogenous Aba ◽  
Root Aerenchyma ◽  
Lipid Binding Proteins

AbstractPlant annexins are calcium- and lipid-binding proteins that have multiple functions, and a significant amount of research on plant annexins has been reported in recent years. However, the functions of annexins in diverse biological processes in rice are largely unclear. Herein, we report that OsANN4, a calcium-binding rice annexin protein, is a substrate for OsCDPK24, and the OsANN4 phosphorylation site is the 13th serine, which is a key site for phosphorylation. Most strikingly, abscisic acid (ABA) promotes the interaction between OsANN4 and OsCDPK24. Moreover, knocking down OsANN4 by RNA interference resulted in visible and invisible phenotypes with exogenous ABA treatment, such as shorter shoots of seedlings, less lateral roots, earlier root aerenchyma formation and so on. The further analyzed results showed that decreased superoxide dismutase (SOD) and catalase (CAT) activity of the RNAi lines, which control H2O2 accumulation for redox homeostasis, and further promoted earlier aerenchyma formation of the root. These results suggest that a proposed molecular mechanism exists between OsANN4 and H2O2 production to response ABA.HighlightOsANN4 enhances SOD and CAT activities to scavenge H2O2 to alleviate the formation of aerenchyma under ABA treatment. OsCDPK24 interacts with and phosphorylates OsANN4, this interaction strengthened under ABA treatment.

scholarly journals OsANN4 modulates ROS production and mediates Ca2+ influx in response to ABA

2021 ◽  
Vol 21 (1) ◽  
Author(s):  
Qian Zhang ◽  
Tao Song ◽  
Can Guan ◽  
Yingjie Gao ◽  
Jianchao Ma ◽  
...  
Keyword(s):  
Calcium Binding ◽  
Lipid Binding ◽  
Binding Activity ◽  
Ros Production ◽  
Biological Processes ◽  
Wild Type ◽  
Phenotypic Differences ◽  
Non Invasive ◽  
Test Technology ◽  
Lipid Binding Proteins

Abstract Background Plant annexins are calcium- and lipid-binding proteins that have multiple functions, and a significant amount of research on plant annexins has been reported in recent years. However, the functions of annexins in diverse biological processes in rice are largely unclear. Results Herein, we report that OsANN4, a calcium-binding rice annexin protein, was induced by abscisic acid (ABA). Under ABA treatment, the plants in which OsANN4 was knocked down by RNA interference showed some visible phenotypic changes compared to the wild type, such as a lower rooting rate and shorter shoot and root lengths. Moreover, the superoxide dismutase (SOD) and catalase (CAT) activities of the RNAi lines were significantly lower and further resulted in higher accumulation of O2.- and H2O2 than those of the wild-type. A Non-invasive Micro-test Technology (NMT) assay showed that ABA-induced net Ca2+ influx was inhibited in OsANN4 knockdown plants. Interestingly, the phenotypic differences caused by ABA were eliminated in the presence of LaCl3 (Ca2+ channel inhibitor). Apart from this, we demonstrated that OsCDPK24 interacted with and phosphorylated OsANN4. When the phosphorylated serine residue of OsANN4 was substituted by alanine, the interaction between OsANN4 and OsCDPK24 was still observed, however, both the conformation of OsANN4 and its binding activity with Ca2+ might be changed. Conclusions OsANN4 plays a crucial role in the ABA response, partially by modulating ROS production, mediating Ca2+ influx or interacting with OsCDPK24.

The role of dynamics in modulating ligand exchange in intracellular lipid binding proteins

2014 ◽  
Vol 1844 (7) ◽  
pp. 1268-1278 ◽  
Author(s):  
Laura Ragona ◽  
Katiuscia Pagano ◽  
Simona Tomaselli ◽  
Filippo Favretto ◽  
Alberto Ceccon ◽  
...  
Keyword(s):  
Ligand Exchange ◽  
Binding Proteins ◽  
Lipid Binding ◽  
Intracellular Lipid ◽  
Lipid Binding Proteins

scholarly journals INTRACELLULAR LIPID-BINDING PROTEINS AND THEIR GENES

1997 ◽  
Vol 17 (1) ◽  
pp. 277-303 ◽  
Author(s):  
David A. Bernlohr ◽  
Melanie A. Simpson ◽  
Ann Vogel Hertzel ◽  
Leonard J. Banaszak
Keyword(s):  
Binding Proteins ◽  
Lipid Binding ◽  
Intracellular Lipid ◽  
Lipid Binding Proteins

scholarly journals APF/CBP, the small, amphipathic, anionic protein(s) in bile and gallstones, consists of lipid-binding and calcium-binding forms

Hepatology ◽  
1997 ◽  
Vol 25 (5) ◽  
pp. 1054-1063 ◽  
Author(s):  
H Lafont ◽  
N Domingo ◽  
A Groen ◽  
E W Kaler ◽  
S P Lee ◽  
...  
Keyword(s):  
Calcium Binding ◽  
Protein S ◽  
Lipid Binding ◽  
Binding Forms

scholarly journals Nanodiscs-based proteomics identify Caj1 as an Hsp40 with affinity for phosphatidic acid lipids

2021 ◽  
Author(s):  
Xiao Xiao Zhang ◽  
John William Young ◽  
Leonard J Foster ◽  
Franck Duong
Keyword(s):  
Phosphatidic Acid ◽  
Protein Quality ◽  
Lipid Binding ◽  
Water Soluble ◽  
Rab Gtpases ◽  
Small Water ◽  
Transient Nature ◽  
C Terminus ◽  
Lipid Binding Proteins ◽  
Lipid Specificity

Many soluble proteins interact with membranes to perform important biological functions, including signal transduction, regulation, transport, trafficking and biogenesis. Despite their importance, these protein-membrane interactions are difficult to characterize due to their often-transient nature as well as phospholipids' poor solubility in aqueous solution. Here, we employ nanodiscs - small, water-soluble patches of lipid bilayer encircled with amphipathic scaffold proteins - along with quantitative proteomics to identify lipid-binding proteins in S. cerevisiae. Using nanodiscs reconstituted with yeast total lipid extracts or only phosphatidylethanolamine (PE-nanodiscs), we capture several known membrane-interacting proteins, including the Rab GTPases Sec4 and Ypt1, which play key roles in vesicle trafficking. Utilizing PE-nanodiscs enriched with phosphatidic acid (PEPA-nanodiscs), we specifically capture a member of the Hsp40/J-protein family, Caj1, whose function has recently been linked to membrane protein quality control. We show that Caj1 interaction with liposomes containing PA is modulated by pH and PE lipids, and depends on two patches of positively charged residues near the C-terminus of the protein. The protein Caj1 is the first example of an Hsp40/J-domain protein with affinity for membranes and phosphatidic acid lipid specificity. These findings highlight the utility of the nanodisc system to identify and characterize protein-lipid interactions that may not be evident using other methods.

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