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Article ; Online: Correction for Samsa et al., "Uncoupling

Samsa, Marcelo M / Mondotte, Juan A / Caramelo, Julio J / Gamarnik, Andrea V

2024 , Page(s) e0052724

Language	English
Publishing date	2024-04-25
Publishing country	United States
Document type	Journal Article ; Published Erratum
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/jvi.00527-24
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Article ; Online: Fusion of a bacterial cadherin-like domain and green fluorescent protein as a specific probe to study biofilm matrix formation in

Abdian, Patricia L / Malori, María Soledad / Caramelo, Julio J / Checchi, Abi Maglio / Russo, Daniela M / Zorreguieta, Angeles / Berretta, Marcelo F / Benintende, Graciela

Microbiology (Reading, England)

2023 Volume 168, Issue 12

Abstract: ... ...

Abstract	Rhizobium
MeSH term(s)	Rhizobium/metabolism ; Cadherins/metabolism ; Green Fluorescent Proteins ; Extracellular Polymeric Substance Matrix/metabolism ; Rhizobium leguminosarum ; Bacterial Proteins/metabolism
Chemical Substances	Cadherins ; Green Fluorescent Proteins (147336-22-9) ; Bacterial Proteins
Language	English
Publishing date	2023-02-15
Publishing country	England
Document type	Journal Article
ZDB-ID	1180712-x
ISSN	1465-2080 ; 1350-0872
ISSN (online)	1465-2080
ISSN	1350-0872
DOI	10.1099/mic.0.001284
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Article ; Online: A sweet code for glycoprotein folding.

Caramelo, Julio J / Parodi, Armando J

FEBS letters

2015 Volume 589, Issue 22, Page(s) 3379–3387

Abstract: Glycoprotein synthesis is initiated in the endoplasmic reticulum (ER) lumen upon transfer of a glycan (Glc3Man9GlcNAc2) from a lipid derivative to Asn residues (N-glycosylation). N-Glycan-dependent quality control of glycoprotein folding in the ER ... ...

Abstract	Glycoprotein synthesis is initiated in the endoplasmic reticulum (ER) lumen upon transfer of a glycan (Glc3Man9GlcNAc2) from a lipid derivative to Asn residues (N-glycosylation). N-Glycan-dependent quality control of glycoprotein folding in the ER prevents exit to Golgi of folding intermediates, irreparably misfolded glycoproteins and incompletely assembled multimeric complexes. It also enhances folding efficiency by preventing aggregation and facilitating formation of proper disulfide bonds. The control mechanism essentially involves four components, resident lectin-chaperones (calnexin and calreticulin) that recognize monoglucosylated polymannose protein-linked glycans, lectin-associated oxidoreductase acting on monoglucosylated glycoproteins (ERp57), a glucosyltransferase that creates monoglucosylated epitopes in protein-linked glycans (UGGT) and a glucosidase (GII) that removes the glucose units added by UGGT. This last enzyme is the only mechanism component sensing glycoprotein conformations as it creates monoglucosylated glycans exclusively in not properly folded glycoproteins or in not completely assembled multimeric glycoprotein complexes. Glycoproteins that fail to properly fold are eventually driven to proteasomal degradation in the cytosol following the ER-associated degradation pathway, in which the extent of N-glycan demannosylation by ER mannosidases play a relevant role in the identification of irreparably misfolded glycoproteins.
MeSH term(s)	Animals ; Endoplasmic Reticulum/enzymology ; Endoplasmic Reticulum/secretion ; Endoplasmic Reticulum-Associated Degradation ; Glycoproteins/chemistry ; Glycoproteins/metabolism ; Glycoproteins/secretion ; Glycosylation ; Humans ; Lectins/metabolism ; Protein Folding
Chemical Substances	Glycoproteins ; Lectins
Language	English
Publishing date	2015-11-14
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	212746-5
ISSN	1873-3468 ; 0014-5793
ISSN (online)	1873-3468
ISSN	0014-5793
DOI	10.1016/j.febslet.2015.07.021
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Article ; Online: Structural coalescence underlies the aggregation propensity of a β-barrel protein motif.

Angelani, Carla R / Caramelo, Julio J / Curto, Lucrecia M / Delfino, José M

PloS one

2017 Volume 12, Issue 2, Page(s) e0170607

Abstract: A clear understanding of the structural foundations underlying protein aggregation is an elusive goal of central biomedical importance. A step toward this aim is exemplified by the β-barrel motif represented by the intestinal fatty acid binding protein ( ... ...

Abstract	A clear understanding of the structural foundations underlying protein aggregation is an elusive goal of central biomedical importance. A step toward this aim is exemplified by the β-barrel motif represented by the intestinal fatty acid binding protein (IFABP) and two abridged all-β sheet forms (Δ98Δ and Δ78Δ). At odds with the established notion that a perturbation of the native fold should necessarily favor a buildup of intermediate forms with an enhanced tendency to aggregate, the intrinsic stability (ΔG°H2O) of these proteins does not bear a straightforward correlation with their trifluoroethanol (TFE)-induced aggregation propensity. In view of this fact, we found it more insightful to delve into the connection between structure and stability under sub-aggregating conditions (10% TFE). In the absence of the co-solvent, the abridged variants display a common native-like region decorated with a disordered C-terminal stretch. Upon TFE addition, an increase in secondary structure content is observed, assimilating them to the parent protein. In this sense, TFE perturbs a common native like region while exerting a global compaction effect. Importantly, in all cases, fatty acid binding function is preserved. Interestingly, energetic as well as structural diversity in aqueous solution evolves into a common conformational ensemble more akin in stability. These facts reconcile apparent paradoxical findings related to stability and rates of aggregation. This scenario likely mimics the accrual of aggregation-prone species in the population, an early critical event for the development of fibrillation.
MeSH term(s)	Amino Acid Motifs ; Animals ; Fatty Acid-Binding Proteins/chemistry ; Fatty Acid-Binding Proteins/metabolism ; Protein Aggregates ; Protein Stability ; Rats ; Trifluoroethanol/chemistry
Chemical Substances	Fatty Acid-Binding Proteins ; Protein Aggregates ; Trifluoroethanol (75-89-8)
Language	English
Publishing date	2017-02-10
Publishing country	United States
Document type	Journal Article
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0170607
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Article: A sweet code for glycoprotein folding

Caramelo, Julio J / Armando J. Parodi

Federation of European Biochemical Societies FEBS letters. 2015 Nov. 14, v. 589, no. 22

2015

Abstract	Glycoprotein synthesis is initiated in the endoplasmic reticulum (ER) lumen upon transfer of a glycan (Glc3Man9GlcNAc2) from a lipid derivative to Asn residues (N-glycosylation). N-Glycan-dependent quality control of glycoprotein folding in the ER prevents exit to Golgi of folding intermediates, irreparably misfolded glycoproteins and incompletely assembled multimeric complexes. It also enhances folding efficiency by preventing aggregation and facilitating formation of proper disulfide bonds. The control mechanism essentially involves four components, resident lectin-chaperones (calnexin and calreticulin) that recognize monoglucosylated polymannose protein-linked glycans, lectin-associated oxidoreductase acting on monoglucosylated glycoproteins (ERp57), a glucosyltransferase that creates monoglucosylated epitopes in protein-linked glycans (UGGT) and a glucosidase (GII) that removes the glucose units added by UGGT. This last enzyme is the only mechanism component sensing glycoprotein conformations as it creates monoglucosylated glycans exclusively in not properly folded glycoproteins or in not completely assembled multimeric glycoprotein complexes. Glycoproteins that fail to properly fold are eventually driven to proteasomal degradation in the cytosol following the ER-associated degradation pathway, in which the extent of N-glycan demannosylation by ER mannosidases play a relevant role in the identification of irreparably misfolded glycoproteins.
Keywords	calnexin ; calreticulin ; cytosol ; disulfide bonds ; endoplasmic reticulum ; epitopes ; glucose ; glycoproteins ; glycosylation ; lipids ; mannosidases ; polysaccharides ; quality control
Language	English
Dates of publication	2015-1114
Size	p. 3379-3387.
Publishing place	Elsevier B.V.
Document type	Article
ZDB-ID	212746-5
ISSN	1873-3468 ; 0014-5793
ISSN (online)	1873-3468
ISSN	0014-5793
DOI	10.1016/j.febslet.2015.07.021
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Article ; Online: La dolce vita

Julio J. Caramelo

Química Viva, Vol 8, Iss 2, Pp 80-

el papel de los azúcares en la biosíntesis de glicoproteínas

2009 Volume 105

Abstract: El retículo endoplásmico es el lugar en donde se sintetizan las proteínas que ingresan a la vía secretoria. Previo a su salida, las proteínas adquieren su estructura terciaria y, de ser necesario, se ensamblan en oligómeros funcionales. Para facilitar ... ...

Abstract	El retículo endoplásmico es el lugar en donde se sintetizan las proteínas que ingresan a la vía secretoria. Previo a su salida, las proteínas adquieren su estructura terciaria y, de ser necesario, se ensamblan en oligómeros funcionales. Para facilitar estos procesos existen una gran variedad de chaperonas y enzimas facilitadoras del plegamiento. Asimismo, el estado de plegamiento es monitoreado por un sistema de control de calidad, el cual retiene en el retículo endoplásmico a aquellas especies que no han adquirido su conformación nativa. Si una proteína es incapaz de plegarse correctamente es retenida en el retículo endoplásmico y eventualmente es retrotranslocada al citosol para ser degradada por el proteasoma. Concomitantemente con el plegamiento tienen lugar diversas modificaciones postraduccionales, siendo las más destacadas la N-glicosilación y la formación de puentes disulfuro. Cerca de un cuarto de las proteínas de una célula eucarionte son N-glicosiladas, siendo la modificación postraduccional más frecuente. En las proteínas que alcanzaron su destino final los N-glicanos cumplen papeles fundamentales en diversos procesos de reconocimiento celular. Sin embargo los N-glicanos son utilizados también durante la maduración de las glicoproteínas como un sistema que codifica información acerca de su estado conformacional, siendo un elemento clave en varias instancias decisivas a lo largo de la vía secretoria. En este trabajo se presentan las diversas etapas que atraviesa una proteína desde su ingreso al retículo endoplásmico hasta su llegada a su destino final, poniendo especial atención a las funciones tempranas de los N-glicanos.
Keywords	Biotechnology ; TP248.13-248.65 ; Chemical technology ; TP1-1185 ; Technology ; T ; Biochemistry ; QD415-436 ; Organic chemistry ; QD241-441 ; Chemistry ; QD1-999 ; Science ; Q
Language	Spanish
Publishing date	2009-01-01T00:00:00Z
Publisher	Universidad de Buenos Aires
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: TorsinA folding and N-linked glycosylation are sensitive to redox homeostasis.

Honer, Jonas / Niemeyer, Katie M / Fercher, Christian / Diez Tissera, Ana L / Jaberolansar, Noushin / Jafrani, Yohaann M A / Zhou, Chun / Caramelo, Julio J / Shewan, Annette M / Schulz, Benjamin L / Brodsky, Jeffrey L / Zacchi, Lucía F

Biochimica et biophysica acta. Molecular cell research

2021 Volume 1868, Issue 9, Page(s) 119073

Abstract: The Endoplasmic Reticulum (ER) is responsible for the folding and post-translational modification of secretory proteins, as well as for triaging misfolded proteins. During folding, there is a complex yet only partially understood interplay between ... ...

Abstract	The Endoplasmic Reticulum (ER) is responsible for the folding and post-translational modification of secretory proteins, as well as for triaging misfolded proteins. During folding, there is a complex yet only partially understood interplay between disulfide bond formation, which is an enzyme catalyzed event in the oxidizing environment of the ER, along with other post-translational modifications (PTMs) and chaperone-supported protein folding. Here, we used the glycoprotein torsinA as a model substrate to explore the impact of ER redox homeostasis on PTMs and protein biogenesis. TorsinA is a AAA+ ATPase with unusual oligomeric properties and controversial functions. The deletion of a C-terminal glutamic acid residue (∆E) is associated with the development of Early-Onset Torsion Dystonia, a severe movement disorder. TorsinA differs from other AAA+ ATPases since it is an ER resident, and as a result of its entry into the ER torsinA contains two N-linked glycans and at least one disulfide bond. The role of these PTMs on torsinA biogenesis and function and the identity of the enzymes that catalyze them are poorly defined. Using a yeast torsinA expression system, we demonstrate that a specific protein disulfide isomerase, Pdi1, affects the folding and N-linked glycosylation of torsinA and torsinA∆E in a redox-dependent manner, suggesting that the acquisition of early torsinA folding intermediates is sensitive to perturbed interactions between Cys residues and the quality control machinery. We also highlight the role of specific Cys residues during torsinA biogenesis and demonstrate that torsinA∆E is more sensitive than torsinA when these Cys residues are mutated.
MeSH term(s)	Adenosine Triphosphatases/chemistry ; Adenosine Triphosphatases/metabolism ; Endoplasmic Reticulum/metabolism ; Glycosylation ; Homeostasis ; Models, Molecular ; Oxidation-Reduction ; Protein Processing, Post-Translational ; Saccharomyces cerevisiae Proteins/chemistry ; Saccharomyces cerevisiae Proteins/metabolism
Chemical Substances	Saccharomyces cerevisiae Proteins ; Adenosine Triphosphatases (EC 3.6.1.-)
Language	English
Publishing date	2021-05-29
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural ; 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.2021.119073
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Article: Getting in and out from calnexin/calreticulin cycles.

Caramelo, Julio J / Parodi, Armando J

The Journal of biological chemistry

2008 Volume 283, Issue 16, Page(s) 10221–10225

MeSH term(s)	Animals ; Calnexin/chemistry ; Calnexin/physiology ; Calreticulin/chemistry ; Calreticulin/physiology ; Endoplasmic Reticulum/metabolism ; Fungal Proteins/chemistry ; Gene Expression Regulation ; Glycoproteins/chemistry ; Humans ; Models, Biological ; Polysaccharides/chemistry ; Protein Folding
Chemical Substances	Calreticulin ; Fungal Proteins ; Glycoproteins ; Polysaccharides ; Calnexin (139873-08-8)
Language	English
Publishing date	2008-02-26
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.R700048200
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Article: When cells lose water: Lessons from biophysics and molecular biology.

Caramelo, Julio J / Iusem, Norberto D

Progress in biophysics and molecular biology

2009 Volume 99, Issue 1, Page(s) 1–6

Abstract: Organisms living in deserts and anhydrobiotic species are useful models for unraveling mechanisms used to overcome water loss. In this context, late embryogenesis abundant (LEA) proteins and sugars have been extensively studied for protection against ... ...

Abstract	Organisms living in deserts and anhydrobiotic species are useful models for unraveling mechanisms used to overcome water loss. In this context, late embryogenesis abundant (LEA) proteins and sugars have been extensively studied for protection against desiccation stress and desiccation tolerance. This article aims to reappraise the current understanding of these molecules by focusing on converging contributions from biochemistry, molecular biology, and the use of biophysical tools. Such tools have greatly advanced the field by uncovering intriguing aspects of protein 3-D structure, such as folding upon stress. We summarize the current research on cellular responses against water deficit at the molecular level, considering both plausible water loss-sensing mechanisms and genes governing signal transduction pathways. Finally, we propose models that could guide future experimentation, for example, by concentrating on the behavior of selected proteins in living cells.
MeSH term(s)	Biophysics/trends ; Cell Physiological Phenomena ; Heat-Shock Response/physiology ; Models, Biological ; Molecular Biology/trends ; Water/metabolism
Chemical Substances	Water (059QF0KO0R)
Language	English
Publishing date	2009-01
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	209302-9
ISSN	1873-1732 ; 0079-6107
ISSN (online)	1873-1732
ISSN	0079-6107
DOI	10.1016/j.pbiomolbio.2008.10.001
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Article: Progesterone regulates the expression and activity of two mouse isoforms of the glycoprotein folding sensor UDP-Glc: glycoprotein glucosyltransferase (UGGT).

Prados, María B / Caramelo, Julio J / Miranda, Silvia E

Biochimica et biophysica acta

2013 Volume 1833, Issue 12, Page(s) 3368–3374

Abstract: UDP-Glucose:glycoprotein glucosyltransferase (UGGT) is a central component of the endoplasmic reticulum (ER) glycoprotein-folding quality control system, which prevents the exit of partially folded species. UGGT activity can be regulated by the ... ...

Abstract	UDP-Glucose:glycoprotein glucosyltransferase (UGGT) is a central component of the endoplasmic reticulum (ER) glycoprotein-folding quality control system, which prevents the exit of partially folded species. UGGT activity can be regulated by the accumulation of misfolded proteins in the ER, a stimulus that triggers a complex signaling pathway known as unfolded protein response (UPR) which is closely associated with inflammation and disease. In this work, we investigated the effect of progesterone (P4) on the expression and activity of UGGT in a mouse hybridoma. We detected the expression of two UGGT isoforms, UGGT1 and UGGT2, and demonstrated that both isoforms are active in these cells. Interestingly, the expression of each isoform is regulated by high physiological P4 concentrations. This work provides the first evidence of a hormonal regulation of UGGT isoform expression and activity, which might influence the glycoprotein quality control mechanism. These findings could contribute to the study of pathologies triggered by the accumulation of misfolded proteins.
MeSH term(s)	Animals ; Gene Silencing/drug effects ; Glucosyltransferases ; Glycoproteins/chemistry ; Glycoproteins/metabolism ; Hexosyltransferases/metabolism ; Isoenzymes/metabolism ; Mice ; Progesterone/pharmacology ; Protein Folding ; RNA, Small Interfering/metabolism
Chemical Substances	Glycoproteins ; Isoenzymes ; RNA, Small Interfering ; Progesterone (4G7DS2Q64Y) ; Glucosyltransferases (EC 2.4.1.-) ; Hexosyltransferases (EC 2.4.1.-) ; UGGT1 protein, mouse (EC 2.4.1.-) ; UGGT2 protein, mouse (EC 2.4.1.-) ; glycoprotein glycosyltransferase (EC 2.4.1.-)
Language	English
Publishing date	2013-12
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.2013.09.022
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