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Article ; Online: Recent Advances in the Physiology of Ion Channels in Plants.

Pantoja, Omar

2021 Volume 72, Page(s) 463–495

Abstract: Our knowledge of plant ion channels was significantly enhanced by the first application of the patch-clamp technique to isolated guard cell protoplasts over 35 years ago. Since then, research has demonstrated the importance of ion channels in the control ...

Abstract	Our knowledge of plant ion channels was significantly enhanced by the first application of the patch-clamp technique to isolated guard cell protoplasts over 35 years ago. Since then, research has demonstrated the importance of ion channels in the control of gas exchange in guard cells, their role in nutrient uptake in roots, and the participation of calcium-permeable cation channels in the regulation of cell signaling affected by the intracellular concentrations of this second messenger. In recent years, through the employment of reverse genetics, mutant proteins, and heterologous expression systems, research on ion channels has identified mechanisms that modify their activity through protein-protein interactions or that result in activation and/or deactivation of ion channels through posttranslational modifications. Additional and confirmatory information on ion channel functioning has been derived from the crystallization and molecular modeling of plant proteins that, together with functional analyses, have helped to increase our knowledge of the functioning of these important membrane proteins that may eventually help to improve crop yield. Here, an update on the advances obtained in plant ion channel function during the last few years is presented.
MeSH term(s)	Arabidopsis/metabolism ; Arabidopsis Proteins/metabolism ; Calcium/metabolism ; Ion Channels ; Plant Proteins
Chemical Substances	Arabidopsis Proteins ; Ion Channels ; Plant Proteins ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2021-01-11
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2098209-4
ISSN	1545-2123 ; 1543-5008
ISSN (online)	1545-2123
ISSN	1543-5008
DOI	10.1146/annurev-arplant-081519-035925
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Article: Animal trait variation at the within-individual level: erythrocyte size variation and malaria infection in a tropical lizard.

Cruz, Virnaliz / Cruz-Pantoja, Omar / Tremblay, Raymond / Acevedo, Miguel

PeerJ

2022 Volume 10, Page(s) e12761

Abstract: High levels of within-individual variation (WIV) in reiterative components in plants such as leaves, flowers, and fruits have been shown to increase individual fitness by multiple mechanisms including mediating interactions with natural enemies. This ... ...

Abstract	High levels of within-individual variation (WIV) in reiterative components in plants such as leaves, flowers, and fruits have been shown to increase individual fitness by multiple mechanisms including mediating interactions with natural enemies. This relationship between WIV and fitness has been studied almost exclusively in plant systems. While animals do not exhibit conspicuous reiterative components, they have traits that can vary at the individual level such as erythrocyte size. It is currently unknown if WIV in animals can influence individual fitness by mediating the outcome of interactions with natural enemies as it has been shown in plants. To address this issue, we tested for a relationship between WIV in erythrocyte size, hemoparasite infection status, and body condition (a proxy for fitness) in a Caribbean anole lizard. We quantified the coefficient of variation of adult erythrocytes size in $
Language	English
Publishing date	2022-02-23
Publishing country	United States
Document type	Journal Article
ZDB-ID	2703241-3
ISSN	2167-8359
ISSN	2167-8359
DOI	10.7717/peerj.12761
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Article ; Online: A cornichon protein controls polar localization of the PINA auxin transporter in Physcomitrium patens.

Yáñez-Domínguez, Carolina / Lagunas-Gómez, Daniel / Torres-Cifuentes, Diana M / Bezanilla, Magdalena / Pantoja, Omar

Development (Cambridge, England)

2023 Volume 150, Issue 9

Abstract: Newly synthesized membrane proteins pass through the secretory pathway, starting at the endoplasmic reticulum and packaged into COPII vesicles, to continue to the Golgi apparatus before reaching their membrane of residence. It is known that cargo ... ...

Abstract	Newly synthesized membrane proteins pass through the secretory pathway, starting at the endoplasmic reticulum and packaged into COPII vesicles, to continue to the Golgi apparatus before reaching their membrane of residence. It is known that cargo receptor proteins form part of the COPII complex and play a role in the recruitment of cargo proteins for their subsequent transport through the secretory pathway. The role of cornichon proteins is conserved from yeast to vertebrates, but it is poorly characterized in plants. Here, we studied the role of the two cornichon homologs in the secretory pathway of the moss Physcomitrium patens. Mutant analyses revealed that cornichon genes regulate different growth processes during the moss life cycle by controlling auxin transport, with CNIH2 functioning as a specific cargo receptor for the auxin efflux carrier PINA, with the C terminus of the receptor regulating the interaction, trafficking and membrane localization of PINA.
MeSH term(s)	Animals ; Protein Transport ; COP-Coated Vesicles/metabolism ; Membrane Transport Proteins/metabolism ; Biological Transport/physiology ; Membrane Proteins/metabolism ; Carrier Proteins/metabolism ; Golgi Apparatus/metabolism ; Saccharomyces cerevisiae/metabolism
Chemical Substances	Membrane Transport Proteins ; Membrane Proteins ; Carrier Proteins
Language	English
Publishing date	2023-05-05
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	90607-4
ISSN	1477-9129 ; 0950-1991
ISSN (online)	1477-9129
ISSN	0950-1991
DOI	10.1242/dev.201635
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Article ; Online: The C-terminus of the cargo receptor Erv14 affects COPII vesicle formation and cargo delivery.

Lagunas-Gomez, Daniel / Yañez-Dominguez, Carolina / Zavala-Padilla, Guadalupe / Barlowe, Charles / Pantoja, Omar

Journal of cell science

2023 Volume 136, Issue 3

Abstract: The endoplasmic reticulum (ER) is the start site of the secretory pathway, where newly synthesized secreted and membrane proteins are packaged into COPII vesicles through direct interaction with the COPII coat or aided by specific cargo receptors. Little ...

Abstract	The endoplasmic reticulum (ER) is the start site of the secretory pathway, where newly synthesized secreted and membrane proteins are packaged into COPII vesicles through direct interaction with the COPII coat or aided by specific cargo receptors. Little is known about how post-translational modification events regulate packaging of cargo into COPII vesicles. The Saccharomyces cerevisiae protein Erv14, also known as cornichon, belongs to a conserved family of cargo receptors required for the selection and ER export of transmembrane proteins. In this work, we show the importance of a phosphorylation consensus site (S134) at the C-terminus of Erv14. Mimicking phosphorylation of S134 (S134D) prevents the incorporation of Erv14 into COPII vesicles, delays cell growth, exacerbates growth of sec mutants, modifies ER structure and affects localization of several plasma membrane transporters. In contrast, the dephosphorylated mimic (S134A) had less deleterious effects, but still modifies ER structure and slows cell growth. Our results suggest that a possible cycle of phosphorylation and dephosphorylation is important for the correct functioning of Erv14.
MeSH term(s)	Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Membrane Proteins/metabolism ; Carrier Proteins/metabolism ; Membrane Transport Proteins/metabolism ; Biological Transport ; COP-Coated Vesicles/metabolism ; Protein Transport
Chemical Substances	Saccharomyces cerevisiae Proteins ; Membrane Proteins ; Carrier Proteins ; Membrane Transport Proteins
Language	English
Publishing date	2023-02-06
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2993-2
ISSN	1477-9137 ; 0021-9533
ISSN (online)	1477-9137
ISSN	0021-9533
DOI	10.1242/jcs.260527
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Article ; Online: High affinity ammonium transporters: molecular mechanism of action.

Pantoja, Omar

Frontiers in plant science

2012 Volume 3, Page(s) 34

Abstract: The importance of the family of high affinity ammonium transporters is demonstrated by the presence of these proteins in all domains of life, including bacteria, archaea, fungi, plants, and humans. The majority of the proteins that have been studied from ...

Abstract	The importance of the family of high affinity ammonium transporters is demonstrated by the presence of these proteins in all domains of life, including bacteria, archaea, fungi, plants, and humans. The majority of the proteins that have been studied from this family show high affinity and selectivity for ammonium, are impermeable to alkaline cations, saturate rapidly at low millimolar concentrations and most of them, are also permeable to methylammonium. Crystallization of homologue proteins from bacteria and archaea has demonstrated that the functional entity corresponds to a trimer, with each monomer maintaining a conductive pore. Through molecular modeling, it has been demonstrated that even though the identity of the proteins between bacteria/archaea with those from plants is below 25%, the latter seem to maintain similar tertiary and quaternary structures, an observation that has helped to address the functionality of conserved residues by means of mutational analysis. Results have shown that changes in the extracellular binding site of some plant transporters may result in their inhibition or reduction in transport activity, while in Escherichia coli, dissimilar replacements like Phe/Ala or Ser/Leu that eliminate possible π-interactions or H-bonds with ammonium, respectively, lead to more active transporters. Active mutants with changes in the pair of conserved His in the center of the transporter suggest these residues are dispensable. Additional mutations have identified other important amino acids, both in the entrance of the pore and in cytoplasmic loops. Regulation of this family of transporters can be achieved by interactions of the C-terminal with cytoplasmic loops within the same monomer, or with a neighbor in the trimer. Depending on the interacting residues, these contacts may lead to the activation or inhibition of the protein. The aim of this review is to critically evaluate the newest findings on the role of the proposed amino acids that structure the ammonium pathway, as well as highlight the importance of additional residues that have been identified through mutational analyses.
Language	English
Publishing date	2012-03-28
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2613694-6
ISSN	1664-462X ; 1664-462X
ISSN (online)	1664-462X
ISSN	1664-462X
DOI	10.3389/fpls.2012.00034
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Article ; Online: Na+/H+ exchange in the halophyte Mesembryanthemum crystallinum is associated with cellular sites of Na+ storage.

Barkla, Bronwyn J / Vera-Estrella, Rosario / Camacho-Emiterio, Jesus / Pantoja, Omar

Functional plant biology : FPB

2020 Volume 29, Issue 9, Page(s) 1017–1024

Abstract: The tonoplast ... ...

Abstract	The tonoplast Na
Language	English
Publishing date	2020-07-21
Publishing country	Australia
Document type	Journal Article
ZDB-ID	2071582-1
ISSN	1445-4416 ; 1445-4408
ISSN (online)	1445-4416
ISSN	1445-4408
DOI	10.1071/FP02045
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Article ; Online: Erv14 cargo receptor participates in regulation of plasma-membrane potential, intracellular pH and potassium homeostasis via its interaction with K

Zimmermannová, Olga / Felcmanová, Kristina / Rosas-Santiago, Paul / Papoušková, Klára / Pantoja, Omar / Sychrová, Hana

Biochimica et biophysica acta. Molecular cell research

2019 Volume 1866, Issue 9, Page(s) 1376–1388

Abstract: Cargo receptors in the endoplasmic reticulum (ER) recognize and help membrane and soluble proteins along the secretory pathway to reach their location and functional site. We characterized physiological properties of Saccharomyces cerevisiae strains ... ...

Abstract	Cargo receptors in the endoplasmic reticulum (ER) recognize and help membrane and soluble proteins along the secretory pathway to reach their location and functional site. We characterized physiological properties of Saccharomyces cerevisiae strains lacking the ERV14 gene, which encodes a cargo receptor part of COPII-coated vesicles that cycles between the ER and Golgi membranes. The lack of Erv14 resulted in larger cell volume, plasma-membrane hyperpolarization, and intracellular pH decrease. Cells lacking ERV14 exhibited increased sensitivity to toxic cationic drugs and decreased ability to grow on low K
MeSH term(s)	Biological Transport/physiology ; COP-Coated Vesicles/metabolism ; Cation Transport Proteins/genetics ; Cation Transport Proteins/metabolism ; Cell Membrane/metabolism ; Cell Size ; Endoplasmic Reticulum/metabolism ; Gene Deletion ; Gene Expression Regulation, Fungal ; Glucose/metabolism ; Golgi Apparatus/metabolism ; Homeostasis ; Hydrogen-Ion Concentration ; Membrane Potentials/physiology ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Potassium/metabolism ; Potassium Channels/genetics ; Potassium Channels/metabolism ; Proton-Translocating ATPases/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Sodium/metabolism ; Sodium-Potassium-Exchanging ATPase/metabolism ; Transcriptome
Chemical Substances	Cation Transport Proteins ; ENA1 protein, S cerevisiae ; Erv14 protein, S cerevisiae ; Membrane Proteins ; Potassium Channels ; Saccharomyces cerevisiae Proteins ; TOK1 protein, S cerevisiae ; TRK1 protein, S cerevisiae (136956-54-2) ; Sodium (9NEZ333N27) ; Proton-Translocating ATPases (EC 3.6.3.14) ; Sodium-Potassium-Exchanging ATPase (EC 7.2.2.13) ; Glucose (IY9XDZ35W2) ; Potassium (RWP5GA015D)
Language	English
Publishing date	2019-05-25
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbamcr.2019.05.005
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Article ; Online: Ice plant root plasma membrane aquaporins are regulated by clathrin-coated vesicles in response to salt stress.

Gómez-Méndez, María Fernanda / Amezcua-Romero, Julio César / Rosas-Santiago, Paul / Hernández-Domínguez, Eric Edmundo / de Luna-Valdez, Luis Alberto / Ruiz-Salas, Jorge Luis / Vera-Estrella, Rosario / Pantoja, Omar

Plant physiology

2022 Volume 191, Issue 1, Page(s) 199–218

Abstract: The regulation of root Plasma membrane (PM) Intrinsic Protein (PIP)-type aquaporins (AQPs) is potentially important for salinity tolerance. However, the molecular and cellular details underlying this process in halophytes remain unclear. Using free-flow ... ...

Abstract	The regulation of root Plasma membrane (PM) Intrinsic Protein (PIP)-type aquaporins (AQPs) is potentially important for salinity tolerance. However, the molecular and cellular details underlying this process in halophytes remain unclear. Using free-flow electrophoresis and label-free proteomics, we report that the increased abundance of PIPs at the PM of the halophyte ice plant (Mesembryanthemum crystallinum L.) roots under salinity conditions is regulated by clathrin-coated vesicles (CCV). To understand this regulation, we analyzed several components of the M. crystallinum CCV complexes: clathrin light chain (McCLC) and subunits μ1 and μ2 of the adaptor protein (AP) complex (McAP1μ and McAP2μ). Co-localization analyses revealed the association between McPIP1;4 and McAP2μ and between McPIP2;1 and McAP1μ, observations corroborated by mbSUS assays, suggesting that AQP abundance at the PM is under the control of CCV. The ability of McPIP1;4 and McPIP2;1 to form homo- and hetero-oligomers was tested and confirmed, as well as their activity as water channels. Also, we found increased phosphorylation of McPIP2;1 only at the PM in response to salt stress. Our results indicate root PIPs from halophytes might be regulated through CCV trafficking and phosphorylation, impacting their localization, transport activity, and abundance under salinity conditions.
MeSH term(s)	Clathrin-Coated Vesicles ; Mesembryanthemum/genetics ; Ice ; Cell Membrane/metabolism ; Membrane Proteins/metabolism ; Salt Stress ; Salt-Tolerant Plants/metabolism ; Aquaporins/genetics ; Aquaporins/metabolism ; Plant Roots/genetics ; Plant Roots/metabolism
Chemical Substances	Ice ; Membrane Proteins ; Aquaporins
Language	English
Publishing date	2022-11-16
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	208914-2
ISSN	1532-2548 ; 0032-0889
ISSN (online)	1532-2548
ISSN	0032-0889
DOI	10.1093/plphys/kiac515
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Article ; Online: Comparative 2D-DIGE analysis of salinity responsive microsomal proteins from leaves of salt-sensitive Arabidopsis thaliana and salt-tolerant Thellungiella salsuginea.

Vera-Estrella, Rosario / Barkla, Bronwyn J / Pantoja, Omar

Journal of proteomics

2014 Volume 111, Page(s) 113–127

Abstract: Halophytes have evolved unique molecular strategies to overcome high soil salinity but we still know very little about the main mechanisms that these plants use to complete their lifecycle under salinity stress. One useful approach to further our ... ...

Abstract	Halophytes have evolved unique molecular strategies to overcome high soil salinity but we still know very little about the main mechanisms that these plants use to complete their lifecycle under salinity stress. One useful approach to further our understanding in this area is to directly compare the response to salinity of two closely related species which show diverse levels of salt tolerance. Here we present a comparative proteomic study using DIGE of leaf microsomal proteins to identify salt-responsive membrane associated proteins in Arabidopsis thaliana (a glycophyte) and Thellungiella salsuginea (a halophyte). While a small number of distinct protein abundance changes were observed upon salt stress in both species, the most notable differences were observed between species and specifically, in untreated plants with a total of 36 proteins displaying significant abundance changes. Gene ontology (GO) term enrichment analysis showed that the majority of these proteins were distributed into two functional categories; transport (31%) and carbohydrate metabolism (17%). Results identify several novel salt responsive proteins in this system and support the theory that T. salsuginea shows a high degree of salt-tolerance because molecular mechanisms are primed to deal with the stress. This intrinsic ability to anticipate salinity stress distinguishes it from the glycophyte A. thaliana. Biological significance: There is significant interest in understanding the molecular mechanisms that plants use to tolerate salinity as soil salinization is becoming an increasing concern for agriculture with high soil Na(+) levels leading to reduced yields and economic loss. Much of our knowledge on the molecular mechanisms employed by plants to combat salinity stress has come from work on salt-sensitive plants, but studies on naturally occurring highly salt-resistant plants, halophytes, and direct comparisons between closely related glycophytes and halophytes, could help to further our understanding of salinity tolerance mechanisms. In this study, employing two closely related species which differ markedly in their salt-tolerance, we carried out a quantitative proteomic approach using 2D-DIGE to identify salt-responsive proteins and compare and contrast the differences between the two plant species. Our work complements a previous study using iTRAQ technology (34) and highlights the benefits of using alternative technologies and approaches to gain a broader representation of the salt-responsive proteome in these species.
MeSH term(s)	Arabidopsis/metabolism ; Arabidopsis Proteins/metabolism ; Brassica/metabolism ; Carbohydrates/chemistry ; Chlorophyll/chemistry ; Chromatography, Liquid ; Databases, Protein ; Electrophoresis, Gel, Two-Dimensional ; Osmolar Concentration ; Plant Proteins/metabolism ; Protein Biosynthesis ; Proteome ; Proteomics/methods ; Salt-Tolerant Plants/metabolism ; Tandem Mass Spectrometry
Chemical Substances	Arabidopsis Proteins ; Carbohydrates ; Plant Proteins ; Proteome ; Chlorophyll (1406-65-1)
Language	English
Publishing date	2014-06-02
Publishing country	Netherlands
Document type	Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2400835-7
ISSN	1876-7737 ; 1874-3919
ISSN (online)	1876-7737
ISSN	1874-3919
DOI	10.1016/j.jprot.2014.05.018
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Article ; Online: Growing Arabidopsis in vitro: cell suspensions, in vitro culture, and regeneration.

Barkla, Bronwyn J / Vera-Estrella, Rosario / Pantoja, Omar

Methods in molecular biology (Clifton, N.J.)

2014 Volume 1062, Page(s) 53–62

Abstract: An understanding of basic methods in Arabidopsis tissue culture is beneficial for any laboratory working on this model plant. Tissue culture refers to the aseptic growth of cells, organs, or plants in a controlled environment, in which physical, nutrient, ...

Abstract	An understanding of basic methods in Arabidopsis tissue culture is beneficial for any laboratory working on this model plant. Tissue culture refers to the aseptic growth of cells, organs, or plants in a controlled environment, in which physical, nutrient, and hormonal conditions can all be easily manipulated and monitored. The methodology facilitates the production of a large number of plants that are genetically identical over a relatively short growth period. Techniques, including callus production, cell suspension cultures, and plant regeneration, are all indispensable tools for the study of cellular biochemical and molecular processes. Plant regeneration is a key technology for successful stable plant transformation, while cell suspension cultures can be exploited for metabolite profiling and mining. In this chapter we report methods for the successful and highly efficient in vitro regeneration of plants and production of stable cell suspension lines from leaf explants of both Arabidopsis thaliana and Arabidopsis halleri.
MeSH term(s)	Arabidopsis/cytology ; Arabidopsis/growth & development ; Culture Media ; Culture Techniques ; Hydroponics/methods ; Plant Leaves/cytology ; Plant Leaves/growth & development ; Plant Shoots/cytology ; Plant Shoots/growth & development ; Regeneration
Chemical Substances	Culture Media
Language	English
Publishing date	2014
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-62703-580-4_3
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